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Conserved domains on  [gi|300794015|ref|NP_001178596|]
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BICD family-like cargo adapter 1 [Rattus norvegicus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-479 9.25e-12

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: 9.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   104 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEGRVSELETDVKQLQD 180
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkdlARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   181 ELERQQVHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLS---MQVHALKEDFREKNSstnqhiiRLESLQAEIK 257
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelrAELTLLNEEAANLRE-------RLESLERRIA 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   258 MLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERslqs 337
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR---- 910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   338 saatstsllSEIEQSMEAEELEQEREQLRLQLWEAycQVRYLCSHLR--GNDSADSAVSTDSSMDESSEtssakdvpagS 415
Cdd:TIGR02168  911 ---------SELRRELEELREKLAQLELRLEGLEV--RIDNLQERLSeeYSLTLEEAEALENKIEDDEE----------E 969

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300794015   416 LRTALNDLKRLIQSIVDgveptVTLLSV-EMTALKEERDRLRVTSED-KEPKEQLQKAIRDRDEAI 479
Cdd:TIGR02168  970 ARRRLKRLENKIKELGP-----VNLAAIeEYEELKERYDFLTAQKEDlTEAKETLEEAIEEIDREA 1030
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-479 9.25e-12

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: 9.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   104 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEGRVSELETDVKQLQD 180
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkdlARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   181 ELERQQVHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLS---MQVHALKEDFREKNSstnqhiiRLESLQAEIK 257
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelrAELTLLNEEAANLRE-------RLESLERRIA 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   258 MLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERslqs 337
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR---- 910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   338 saatstsllSEIEQSMEAEELEQEREQLRLQLWEAycQVRYLCSHLR--GNDSADSAVSTDSSMDESSEtssakdvpagS 415
Cdd:TIGR02168  911 ---------SELRRELEELREKLAQLELRLEGLEV--RIDNLQERLSeeYSLTLEEAEALENKIEDDEE----------E 969

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300794015   416 LRTALNDLKRLIQSIVDgveptVTLLSV-EMTALKEERDRLRVTSED-KEPKEQLQKAIRDRDEAI 479
Cdd:TIGR02168  970 ARRRLKRLENKIKELGP-----VNLAAIeEYEELKERYDFLTAQKEDlTEAKETLEEAIEEIDREA 1030
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 130-351 7.23e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 7.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 130 RQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEgrvsELETDVKQLQDELERQQVHLREADREKTRAVQELS---EQ 206
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYELLAELARLEQDIArleER 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 207 NQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEE-----NDLLQ 281
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEleelaEELLE 390

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 282 GTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERSLQSSAATSTSLLSEIEQ 351
Cdd:COG1196  391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 106-316 4.97e-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: 54.65  E-value: 4.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  106 QKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFE------------------------NRE 161
Cdd:pfam04849  77 EKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDllqiysndaeesetesscstplrrNES 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  162 GEWEGRVSELETDVKQLQdELERQQVHLREADREKTRAVQELSEQNQRLL----DQLSRASEVERQLSMQVHALKEDFRE 237
Cdd:pfam04849 157 FSSLHGCVQLDALQEKLR-GLEEENLKLRSEASHLKTETDTYEEKEQQLMsdcvEQLSEANQQMAELSEELARKMEENLR 235

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300794015  238 KNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqghdkdlQLHQSQLELQEVR 316
Cdd:pfam04849 236 QQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLG-------MLHEAQEELKELR 307
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
132-348 3.76e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 132 YEQMHKELTDKLEHLEQEKHELRRRFENRE---GEWEGR---VSELETDVKQLQD---ELERQQVHLREADREKTRAVQE 202
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADevlEEHEERreeLETLEAEIEDLREtiaETEREREELAEEVRDLRERLEE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 203 LSEQNQRLLDQL-------SRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDR-------KRELEH 268
Cdd:PRK02224 291 LEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERaeelreeAAELES 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 269 RLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEE-RSLQSSAATSTSLLS 347
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATlRTARERVEEAEALLE 450


                 .
gi 300794015 348 E 348
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 ...
 104-479 9.25e-12

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: 9.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   104 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEGRVSELETDVKQLQD 180
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkdlARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   181 ELERQQVHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLS---MQVHALKEDFREKNSstnqhiiRLESLQAEIK 257
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelrAELTLLNEEAANLRE-------RLESLERRIA 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   258 MLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERslqs 337
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR---- 910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   338 saatstsllSEIEQSMEAEELEQEREQLRLQLWEAycQVRYLCSHLR--GNDSADSAVSTDSSMDESSEtssakdvpagS 415
Cdd:TIGR02168  911 ---------SELRRELEELREKLAQLELRLEGLEV--RIDNLQERLSeeYSLTLEEAEALENKIEDDEE----------E 969

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300794015   416 LRTALNDLKRLIQSIVDgveptVTLLSV-EMTALKEERDRLRVTSED-KEPKEQLQKAIRDRDEAI 479
Cdd:TIGR02168  970 ARRRLKRLENKIKELGP-----VNLAAIeEYEELKERYDFLTAQKEDlTEAKETLEEAIEEIDREA 1030
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 99-335 1.11e-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: 67.77  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015    99 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTD---KLEHLEQEKHELRRRFENREGEWEgrvsELETDV 175
Cdd:TIGR02168  716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaEIEELEERLEEAEEELAEAEAEIE----ELEAQI 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   176 KQLQDELERQQVHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSM---QVHALKEDFREKNSSTNQHIIRLESL 252
Cdd:TIGR02168  792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleeQIEELSEDIESLAAEIEELEELIEEL 871

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   253 QAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQvkvEELTEE 332
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ---ERLSEE 948


                   ...
gi 300794015   333 RSL 335
Cdd:TIGR02168  949 YSL 951
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 130-351 7.23e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 7.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 130 RQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEgrvsELETDVKQLQDELERQQVHLREADREKTRAVQELS---EQ 206
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYELLAELARLEQDIArleER 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 207 NQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEE-----NDLLQ 281
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEleelaEELLE 390

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 282 GTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERSLQSSAATSTSLLSEIEQ 351
Cdd:COG1196  391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 104-348 1.63e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 104 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELtDKLEHLEQEKHELRRRFENREGEWEGRVSELETDVKQLQDELE 183
Cdd:COG1196  262 LAELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 184 RQQVHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQ---HIIRLESLQAEIKMLS 260
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQleeLEEAEEALLERLERLE 420

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 261 DRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERSLQSSAA 340
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500


                 ....*...
gi 300794015 341 TSTSLLSE 348
Cdd:COG1196  501 ADYEGFLE 508
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 119-334 2.55e-10

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: 63.55  E-value: 2.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   119 KALLERNQDMSRQYEQMHKELT---DKLEHLEQEKHELRRRFEnregEWEGRVSELETDVKQLQDELERQQVHLREADRE 195
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSslqSELRRIENRLDELSQELS----DASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   196 KTRAVQELSEQNQRLLDQLSRASEVERQLsmqvHALKEDFREKNSSTNQHIIR-----LESLQAEIKMLSDRKRELEHRL 270
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKL 821

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300794015   271 SATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERS 334
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-345 8.16e-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: 62.00  E-value: 8.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   104 IRQKEKDLvLAARLG--KALLERNQDMSRQYEQMHKELTD-------KLEHLEQEKHELRRRFENREGEWE---GRVSEL 171
Cdd:TIGR02168  222 LRELELAL-LVLRLEelREELEELQEELKEAEEELEELTAelqeleeKLEELRLEVSELEEEIEELQKELYalaNEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   172 ETDV-------KQLQDELERQQVHLREADREKTRA----------VQELSEQNQRLLDQLSRASEVERQLSMQVHALKED 234
Cdd:TIGR02168  301 EQQKqilrerlANLERQLEELEAQLEELESKLDELaeelaeleekLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   235 FREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDK---DLQLHQSQLE 311
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeleELQEELERLE 460

                          250       260       270
                   ....*....|....*....|....*....|....
gi 300794015   312 LQEVRLSYRQLQVKVEELTEERSLQSSAATSTSL 345
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSL 494
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 106-316 4.97e-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: 54.65  E-value: 4.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  106 QKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFE------------------------NRE 161
Cdd:pfam04849  77 EKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDllqiysndaeesetesscstplrrNES 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  162 GEWEGRVSELETDVKQLQdELERQQVHLREADREKTRAVQELSEQNQRLL----DQLSRASEVERQLSMQVHALKEDFRE 237
Cdd:pfam04849 157 FSSLHGCVQLDALQEKLR-GLEEENLKLRSEASHLKTETDTYEEKEQQLMsdcvEQLSEANQQMAELSEELARKMEENLR 235

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300794015  238 KNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqghdkdlQLHQSQLELQEVR 316
Cdd:pfam04849 236 QQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLG-------MLHEAQEELKELR 307
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 236-532 7.25e-08

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: 55.45  E-value: 7.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   236 REKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEV 315
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   316 RLSYRQLQVKVEELTEERSLQSSA-ATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAY----------CQVRYLCSHLR 384
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelraeltlLNEEAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   385 GNDSADSAVSTDSSMDESSETSSAKDVPAGSLRTALNDLKRLIQSIVDGVEPTVTLLSVEMTALKEERDRLRVTSED-KE 463
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElRE 905

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300794015   464 PKEQLQKAIRDRDEAIAKKKAVELELAKCKMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQL 532
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 136-372 8.42e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 8.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 136 HKELTDKLEHLEQEKHELRRR-FENREGEWEGRVSELETDVKQLQDELERQQVHLREADREKTRAVQELSEQNQRLLDQL 214
Cdd:COG1196  215 YRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 215 SRASEVERQLSMQV---HALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRV 291
Cdd:COG1196  295 AELARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 292 LILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERSLQSSAATStslLSEIEQSMEAEELEQEREQLRLQLWE 371
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEE 451


                 .
gi 300794015 372 A 372
Cdd:COG1196  452 A 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 122-345 1.27e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   122 LERNQD-MSRQYE--QMHKELTDKLEHLE--------QEKHELRRRFENREGEWEGRVSELETDVKQLQDELERQQVHLR 190
Cdd:TIGR02168  198 LERQLKsLERQAEkaERYKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   191 EADREKTRAVQELSEQNQRLLD---QLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELE 267
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300794015   268 HRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERSLQSSAATSTSL 345
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
COG5022 COG5022
Myosin heavy chain [General function prediction only];
169-349 1.60e-07

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 54.70  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  169 SELETDVKQLQDELERQQVHLREADREktraVQELSEQNQRLLdqlSRASEVERQLSmqvhalkEDFREKNSSTNQHIIR 248
Cdd:COG5022   867 ETIYLQSAQRVELAERQLQELKIDVKS----ISSLKLVNLELE---SEIIELKKSLS-------SDLIENLEFKTELIAR 932

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  249 LESL--QAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVL---ILERQGHDKDLQLHQSQLELQEVRLSYRQLQ 323
Cdd:COG5022   933 LKKLlnNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKkstILVREGNKANSELKNFKKELAELSKQYGALQ 1012

                         170       180
                  ....*....|....*....|....*.
gi 300794015  324 VKVEELTEERSLQSSAATSTSLLSEI 349
Cdd:COG5022  1013 ESTKQLKELPVEVAELQSASKIISSE 1038
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
140-334 2.50e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  140 TDKLEHLEQEKHELRRRFEnregEWEGRVSELETDVKQLQDELERQQVHLREADREK-TRAVQELSEQNQRLLDQLSRAS 218
Cdd:COG4913   609 RAKLAALEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDEIdVASAEREIAELEAELERLDASS 684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  219 EVERQLSMQVHALKEdfreknsstnqhiiRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQG 298
Cdd:COG4913   685 DDLAALEEQLEELEA--------------ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 300794015  299 HDKDLQLHQSQLELQEVRlsyRQLQVKVEELTEERS 334
Cdd:COG4913   751 LEERFAAALGDAVERELR---ENLEERIDALRARLN 783
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 106-334 3.13e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.53  E-value: 3.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   106 QKEKDLVLAARL----GKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRfENREGEWEGRVSELETDVKQLQDE 181
Cdd:TIGR02169  209 KAERYQALLKEKreyeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISEL-EKRLEEIEQLLEELNKKIKDLGEE 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   182 LERQ---QVHLREADREKTRAVQELSEQNQRLLDQLSRASEVER---------------QLSMQVHALKEDFREKNSSTN 243
Cdd:TIGR02169  288 EQLRvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIdkllaeieelereieEERKRRDKLTEEYAELKEELE 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   244 QHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQL---HQSQLELQEVRLSyr 320
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagiEAKINELEEEKED-- 445

                          250
                   ....*....|....
gi 300794015   321 qLQVKVEELTEERS 334
Cdd:TIGR02169  446 -KALEIKKQEWKLE 458
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 99-540 1.21e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  99 ELLSVIRQKEKDLVLAARLGKALLERNQdmsrQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELETDVKQL 178
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 179 QDE----LERQQVHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQvhalKEDFREKNSSTNQHIIRLESLQA 254
Cdd:COG1196  368 LEAeaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE----EELEELEEALAELEEEEEEEEEA 443

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 255 EIKMLSDRKRELEHRLSATLEENDLLQgtVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERS 334
Cdd:COG1196  444 LEEAAEEEAELEEEEEALLELLAELLE--EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 335 LQSSAATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAYCQVRYLCSHLRGN-----DSADSAVSTDSSMDESSETSSAK 409
Cdd:COG1196  522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRatflpLDKIRARAALAAALARGAIGAAV 601

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 410 DVPAGSLRTALNDLKRLIQSIVDGVEPTVTLLSVEMTALKEERDRLRVTSEDKE----PKEQLQKAIRDRDEAIAKKKAV 485
Cdd:COG1196  602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGgsagGSLTGGSRRELLAALLEAEAEL 681

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300794015 486 ELELAKCKMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQLMDTHLKEQ 540
Cdd:COG1196  682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
130-329 1.37e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  130 RQYEQMHKELTDKLEHLEQEKHELRRRFENRE-GEWEGRVSELETDVKQLQDELERQQVHLREADREKTRAVQELSEQNQ 208
Cdd:COG4913   258 RELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  209 RLLDQL----SRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDL----L 280
Cdd:COG4913   338 DRLEQLereiERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAalrdL 417

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300794015  281 QGTVEELQDRVLILERQGHDKDLQLHQSQLELQEvrlsyrQLQVKVEEL 329
Cdd:COG4913   418 RRELRELEAEIASLERRKSNIPARLLALRDALAE------ALGLDEAEL 460
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-337 3.56e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  109 KDLVLAARLGKALLERNQDMSRQYEQMHKELTD---KLEHLEQ--EKHELRRRFENREGEWEGRVSELETDVKQLQDELE 183
Cdd:COG4913   214 REYMLEEPDTFEAADALVEHFDDLERAHEALEDareQIELLEPirELAERYAAARERLAELEYLRAALRLWFAQRRLELL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  184 RQQvhLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSmqvhalkedfrekNSSTNqhiiRLESLQAEIKMLSDRK 263
Cdd:COG4913   294 EAE--LEELRAELARLEAELERLEARLDALREELDELEAQIR-------------GNGGD----RLEQLEREIERLEREL 354

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300794015  264 RELEH---RLSATLEENDL-LQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEE-RSLQS 337
Cdd:COG4913   355 EERERrraRLEALLAALGLpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiASLER 433
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 128-340 4.44e-06

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: 49.73  E-value: 4.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   128 MSRQYEQMHKELTDKLEHLeQEKHELRRRFENREGEWEGRVSELETdvkqlqdelerQQVHLREADREKTRAVQELSEQN 207
Cdd:pfam15921  588 MQVEKAQLEKEINDRRLEL-QEFKILKDKKDAKIRELEARVSDLEL-----------EKVKLVNAGSERLRAVKDIKQER 655

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   208 QRLLDQLSRASEVERQLSMQVHALKEDFREKN----SSTNQHIIRLESLQAEIKMLSDRKRELE--------------HR 269
Cdd:pfam15921  656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSeemeTTTNKLKMQLKSAQSELEQTRNTLKSMEgsdghamkvamgmqKQ 735

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300794015   270 LSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEEL-TEERSLQSSAA 340
Cdd:pfam15921  736 ITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLrSQERRLKEKVA 807
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 135-333 2.23e-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: 46.07  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 135 MHKELtDKLEHLeQEKHELRRRFENREGEWEGRVSELETDVKQLQDELERQQVHLREADREKTRAVQELSEQNQRLldql 214
Cdd:COG1579    2 MPEDL-RALLDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 215 sraSEVERQLsMQVHALKEdfreknsstnqhiirLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLIL 294
Cdd:COG1579   76 ---KKYEEQL-GNVRNNKE---------------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL 136

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 300794015 295 ERqghdkdlQLHQSQLELQEVRlsyRQLQVKVEELTEER 333
Cdd:COG1579  137 EA-------ELEEKKAELDEEL---AELEAELEELEAER 165
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 111-345 2.35e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 111 LVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGewegRVSELETDVKQLQDELERQQVHLR 190
Cdd:COG4942   11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 191 EADREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDF--------------REKNSSTNQHIIRLESLQAEI 256
Cdd:COG4942   87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFldavrrlqylkylaPARREQAEELRADLAELAALR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 257 KMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERqghdkdlQLHQSQLELQEVRLSYRQLQVKVEELTEERSLQ 336
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEK-------ELAELAAELAELQQEAEELEALIARLEAEAAAA 239


                 ....*....
gi 300794015 337 SSAATSTSL 345
Cdd:COG4942  240 AERTPAAGF 248
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 104-526 2.82e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 104 IRQKEKDLVLAARLG--KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSEL---------- 171
Cdd:COG1196  319 EELEEELAELEEELEelEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELlealraaael 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 172 ----------ETDVKQLQDELERQQVHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSS 241
Cdd:COG1196  399 aaqleeleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 242 TNQHIIRLESLQAEIKMLSDRKRELEHRLSATLE-----ENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVR 316
Cdd:COG1196  479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAalllaGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 317 LSYRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAYCQVR-YLCSHLRGNDSADSAVST 395
Cdd:COG1196  559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGdTLLGRTLVAARLEAALRR 638

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 396 DSSMDES--SETSSAKDVPAGSLRTALNDLKRLIQSIVDGVEPTVTLLSVEMTALKEERDRLRVTSEDKEPKEQLQKAIR 473
Cdd:COG1196  639 AVTLAGRlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 300794015 474 DRDEAIAKKKAVELELAKCKMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHR 526
Cdd:COG1196  719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
132-348 3.76e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 132 YEQMHKELTDKLEHLEQEKHELRRRFENRE---GEWEGR---VSELETDVKQLQD---ELERQQVHLREADREKTRAVQE 202
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADevlEEHEERreeLETLEAEIEDLREtiaETEREREELAEEVRDLRERLEE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 203 LSEQNQRLLDQL-------SRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDR-------KRELEH 268
Cdd:PRK02224 291 LEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERaeelreeAAELES 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 269 RLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEE-RSLQSSAATSTSLLS 347
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATlRTARERVEEAEALLE 450


                 .
gi 300794015 348 E 348
Cdd:PRK02224 451 A 451
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 109-342 9.35e-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: 45.27  E-value: 9.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  109 KDLVLAARLGKALLERNqdmsrqyeqmhkELTDKLEHLEQEKHELRRRFENREGEWEGRVSELETDVKQLQDELER---Q 185
Cdd:pfam07888  28 RAELLQNRLEECLQERA------------ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQsreK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  186 QVHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRE 265
Cdd:pfam07888  96 HEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300794015  266 LEHRLSATLEENDLLQGTVEELQDrvliLERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEE-RSLQSSAATS 342
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQELRN----SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElRSLQERLNAS 249
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-334 1.43e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 104 IRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELtDKLEHLEQEKHELRRRFENREGEwegrVSELETDVKQLQDELE 183
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEELEKELESLEGS----KRKLEEKIRELEERIE 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 184 RQQVHLREAdREKTRAVQELSEQNQRLLdQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRK 263
Cdd:PRK03918 270 ELKKEIEEL-EEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL 347

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300794015 264 RELEHRLsatleendllqgtvEELQDRVLILER----QGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERS 334
Cdd:PRK03918 348 KELEKRL--------------EELEERHELYEEakakKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 99-297 1.56e-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: 44.73  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   99 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQ----------EKHELRRRFENREGEwegrV 168
Cdd:pfam05557  52 ELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADarevisclknELSELRRQIQRAELE----L 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  169 SELETDVKQLQDELERQQVHLREAdrekTRAVQELSEQNQRLLDQLSRASEVERQLSMQvhalkEDFREKNSSTNQHIIR 248
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEA----EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQ-----EQDSEIVKNSKSELAR 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300794015  249 LESLQAEIKmlsdRKRELEHRLSATLEENDLLQGTVEELQDRvliLERQ 297
Cdd:pfam05557 199 IPELEKELE----RLREHNKHLNENIENKLLLKEEVEDLKRK---LERE 240
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 126-332 2.08e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.27  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   126 QDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELETDVKQLQDELERQQVHLREADREKTRAvqelsE 205
Cdd:TIGR00606  694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI-----E 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   206 QNQRLLDQLSRASEVERQLSMQV---HALKEDFREKNSSTNQHIIRLES--LQAEIKMLSDRKRELEHRLSATLEENDLL 280
Cdd:TIGR00606  769 EQETLLGTIMPEEESAKVCLTDVtimERFQMELKDVERKIAQQAAKLQGsdLDRTVQQVNQEKQEKQHELDTVVSKIELN 848

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 300794015   281 QGTVEELQDRVLILErqghDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEE 332
Cdd:TIGR00606  849 RKLIQDQQEQIQHLK----SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
112-276 3.05e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  112 VLAARLGKALLERNQDmsrQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEG----RVSELETDVKQLQDELERQQv 187
Cdd:COG4913   283 LWFAQRRLELLEAELE---ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERE- 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  188 HLREADREKTRAV--------QELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSstnqhiiRLESLQAEIKML 259
Cdd:COG4913   359 RRRARLEALLAALglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR-------ELRELEAEIASL 431

                         170
                  ....*....|....*..
gi 300794015  260 SDRKRELEHRLSATLEE 276
Cdd:COG4913   432 ERRKSNIPARLLALRDA 448
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
122-494 3.17e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 122 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELETDVKQLQDELERQQVHLREADREKTRAVQ 201
Cdd:COG4717  148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 202 ELSE-----QNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEE 276
Cdd:COG4717  228 ELEQlenelEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 277 NDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRlSYRQLQVKVEELTEERSLQSSAATSTSLLSEIEQSMEAE 356
Cdd:COG4717  308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 357 ELEQEREQLRLQLWEAycQVRYLCSHLRGNDSADSAVSTDSSMDEssetssakdvpagsLRTALNDLKRLIQSIVDgvep 436
Cdd:COG4717  387 LRAALEQAEEYQELKE--ELEELEEQLEELLGELEELLEALDEEE--------------LEEELEELEEELEELEE---- 446

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 300794015 437 tvtllsvEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKKAVELELAKCKM 494
Cdd:COG4717  447 -------ELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKL 497
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 132-351 3.70e-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: 43.47  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  132 YEQMHKELTDKLEHLEQEKhelrrrfenregewegrvSELETDVKQLQDELERQQVHLREADREktraVQELSEQNQRLL 211
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQN------------------NQLKDNIEKKQQEINEKTTEISNTQTQ----LNQLKDEQNKIK 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  212 DQLSR-ASEVER------QLSMQVHALKEDFREKNSSTNQHIIRleSLQAEIKMLSDRKRELEHRLSATLEENDLLQGTV 284
Cdd:TIGR04523 267 KQLSEkQKELEQnnkkikELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300794015  285 EELQDRVLILERQGHDKDLQLHQSQLELQEVRlsyRQLQVKVEELTeerSLQSSaatSTSLLSEIEQ 351
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLK---KENQSYKQEIK---NLESQ---INDLESKIQN 402
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
137-289 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 300794015 137 KELTDKLEHLEQEKHELRRRFENR----EGEWEGRVSELET------DVKQLQDELERQQVHLREADREKTRAVQELSEQ 206
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAET 638

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 207 NQRLLDQLSRASEVERQLSMQVHA-LKEDFREKNSstnqhiiRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVE 285
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEYEeLREEYLELSR-------ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711


                 ....
gi 300794015 286 ELQD 289
Cdd:PRK03918 712 ELEK 715
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 169-355 1.02e-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: 41.67  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 169 SELETDVKQLQDELERQQVHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSmqvhALKEDFREKNSSTNQHIIR 248
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 249 LESLQAEIK--MLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLS--YRQLQV 324
Cdd:COG4942   99 LEAQKEELAelLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEaeRAELEA 178

                        170       180       190
                 ....*....|....*....|....*....|..
gi 300794015 325 KVEELTEER-SLQSSAATSTSLLSEIEQSMEA 355
Cdd:COG4942  179 LLAELEEERaALEALKAERQKLLARLEKELAE 210
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
122-523 1.28e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 122 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFEnregEWEGRVSELETDVKQLQDELERQQvhLREADREKTRAVQ 201
Cdd:COG4717   76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELE----ELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 202 ELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQhiiRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQ 281
Cdd:COG4717  150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELE 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 282 GTVEELQDRVLILERQghdKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERS-LQSSAATSTSLLSEIEQSMEAEELEQ 360
Cdd:COG4717  227 EELEQLENELEAAALE---ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgVLFLVLGLLALLFLLLAREKASLGKE 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 361 EREQLRLQLWEAYCQVRYlcSHLRGNDSADSAVSTDSSMDESSETSSAKDvpagsLRTALNDLKRLIQSIVDGVEPTVTL 440
Cdd:COG4717  304 AEELQALPALEELEEEEL--EELLAALGLPPDLSPEELLELLDRIEELQE-----LLREAEELEEELQLEELEQEIAALL 376

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 441 LSVEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDE---------AIAKKKAVELELAKCKMDMMSLNSQLLDAIQQKL 511
Cdd:COG4717  377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEllgeleellEALDEEELEEELEELEEELEELEEELEELREELA 456

                        410
                 ....*....|..
gi 300794015 512 NLSQQLEAWQDD 523
Cdd:COG4717  457 ELEAELEQLEED 468
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 130-274 1.34e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 130 RQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEG---RVSELETDVKQLQDELERQQVHLREADREK---------- 196
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeie 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 197 --TRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQhiiRLESLQAEIKMLSDRKRELEHRLSATL 274
Cdd:COG1579  100 slKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAEREELAAKIPPEL 176
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 125-351 1.50e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  125 NQDMSRQYEQMHKEL----------TDKLEHLEQEKHELRRRFENREGEWEgrvsELETDVKQLQ---DELERQQVHLRE 191
Cdd:TIGR04523 358 NSEKQRELEEKQNEIeklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQ----QKDEQIKKLQqekELLEKEIERLKE 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  192 ADREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLS 271
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  272 ATLEENDLLQGTVEELQDRVLILERQGHDKDlqlhqSQLELQEVRLSYRQLQVKVEELTEErsLQSSAATSTSLLSEIEQ 351
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEKKEKESKISDLE-----DELNKDDFELKKENLEKEIDEKNKE--IEELKQTQKSLKKKQEE 586
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 118-541 1.68e-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: 41.64  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   118 GKALLERN-QDMSRQYEQMHKELTDKLEHLEQEKHELRRRfenregewegrVSELETDVKQLQdeLERQQvhLREADREK 196
Cdd:pfam15921   72 GKEHIERVlEEYSHQVKDLQRRLNESNELHEKQKFYLRQS-----------VIDLQTKLQEMQ--MERDA--MADIRRRE 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   197 TRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRK------------R 264
Cdd:pfam15921  137 SQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfR 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   265 ELEHRLSATLEEND----LLQGTVEELQDRVLILERQGHDK-DLQLHQSQLELQEVrlsYRQLQVKVEELTEERSLQSSA 339
Cdd:pfam15921  217 SLGSAISKILRELDteisYLKGRIFPVEDQLEALKSESQNKiELLLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQ 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   340 ATSTSLLSEIEQSmeaeeleqereqlrlqlweaycQVRYLCS-HLRGNDSADSAVStdssmdessetssakdvpagSLRT 418
Cdd:pfam15921  294 ANSIQSQLEIIQE----------------------QARNQNSmYMRQLSDLESTVS--------------------QLRS 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   419 ALNDLKRLIQSIVDGVEPTVTLLSVEMTALKEERDRLrvTSEDKEPKEQLQKAIRDRDEAiAKKKAVELELAKCKMDMMS 498
Cdd:pfam15921  332 ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQF--SQESGNLDDQLQKLLADLHKR-EKELSLEKEQNKRLWDRDT 408

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 300794015   499 LNSQLLDAIQQKLN--------LSQQLEAWQDDMHRVIDRQLMDTHLKEQS 541
Cdd:pfam15921  409 GNSITIDHLRRELDdrnmevqrLEALLKAMKSECQGQMERQMAAIQGKNES 459
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-297 1.74e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015    96 QDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEwegrVSELETDV 175
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELI 868

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   176 KQLQDELErqqvhlreadrEKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAE 255
Cdd:TIGR02168  869 EELESELE-----------ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 300794015   256 IKMLSDRKRELEHRLSATLEEN-DLLQGTVEELQDRVLILERQ 297
Cdd:TIGR02168  938 IDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENK 980
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 169-272 1.78e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.07  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 169 SELETDVKQLQDElerQQVHLREA----DREKTRAVQELSEQNQRLLDQLSRASEVE-----RQLSMQVHALKEDFREKN 239
Cdd:PRK05771  16 SYKDEVLEALHEL---GVVHIEDLkeelSNERLRKLRSLLTKLSEALDKLRSYLPKLnplreEKKKVSVKSLEELIKDVE 92

                         90       100       110
                 ....*....|....*....|....*....|...
gi 300794015 240 SSTNQHIIRLESLQAEIKMLSDRKRELEHRLSA 272
Cdd:PRK05771  93 EELEKIEKEIKELEEEISELENEIKELEQEIER 125
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
131-350 1.87e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 131 QYEQMHKELTDKLEHLEQEKHELRRRFENREG--EWEGRVSELETDVKQLQDELERQqvhlREADREKTRAVQELSEQNQ 208
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDlvEAEDRIERLEERREDLEELIAER----RETIEEKRERAEELRERAA 547

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 209 RL----LDQLSRASEVERQLSMQVHALK--EDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQG 282
Cdd:PRK02224 548 ELeaeaEEKREAAAEAEEEAEEAREEVAelNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRE 627

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300794015 283 TVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSyrQLQVKVEELTEER-SLQSSAATSTSLLSEIE 350
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE--QVEEKLDELREERdDLQAEIGAVENELEELE 694
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 119-354 2.09e-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: 41.19  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   119 KALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRrfenregewegRVSELETDVKQLQDELERQQVHLREADREKtr 198
Cdd:TIGR00606  304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ-----------EKTELLVEQGRLQLQADRHQEHIRARDSLI-- 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   199 avqeLSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLE-EN 277
Cdd:TIGR00606  371 ----QSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIElKK 446

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300794015   278 DLLQGTVEELQDRVLILER-QGHDKDLQLHQSQLELQEVRLSYRQLQVKVE-ELTEERSLQSSAATSTSLLSEIEQSME 354
Cdd:TIGR00606  447 EILEKKQEELKFVIKELQQlEGSSDRILELDQELRKAERELSKAEKNSLTEtLKKEVKSLQNEKADLDRKLRKLDQEME 525
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 99-297 3.62e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  99 ELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELETDVKQL 178
Cdd:COG4942   41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQP 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 179 QDELERQQVHLREADReKTRAVQELSEQNQRLLDQLSRASEverQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKM 258
Cdd:COG4942  121 PLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 300794015 259 LSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQ 297
Cdd:COG4942  197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 123-217 4.48e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.93  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  123 ERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGE---WEGRVSELETDVKQLQDELERQQVHLREADRE---- 195
Cdd:PRK11448  138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQElvaLEGLAAELEEKQQELEAQLEQLQEKAAETSQErkqk 217

                          90       100       110
                  ....*....|....*....|....*....|
gi 300794015  196 -KTRAVQ-----ELSEQNQRLL--DQLSRA 217
Cdd:PRK11448  218 rKEITDQaakrlELSEEETRILidQQLRKA 247
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 121-355 5.09e-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: 39.72  E-value: 5.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   121 LLERNQDMSRQYEQMHK----ELTDKLEHLEQEKHELRRRFE-------NREGEWEGRVSELETDVKQLQDELerqqvhl 189
Cdd:pfam15921  261 LLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEiiqeqarNQNSMYMRQLSDLESTVSQLRSEL------- 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   190 READREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDR------- 262
Cdd:pfam15921  334 REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsit 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   263 ----KRELEHRLSATLEENDLLQGTVEELQDRvliLERQG---HDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEER-S 334
Cdd:pfam15921  414 idhlRRELDDRNMEVQRLEALLKAMKSECQGQ---MERQMaaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKmT 490

                          250       260
                   ....*....|....*....|....
gi 300794015   335 LQSSAATSTSL---LSEIEQSMEA 355
Cdd:pfam15921  491 LESSERTVSDLtasLQEKERAIEA 514
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 130-286 6.18e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.55  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  130 RQYEQMHKELTDKLEHLEQEKHELR-RRFENREGEWEGRVSELETDVKQLQDELERQQVHLREADREKTRAVQELSEQNQ 208
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLRaERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  209 RLLDQLSRASEVERQLSMQVHALKE-------DFREKNSSTNQHIIRLESLQAEIKmlSDRKRELEHRLSatlEENDLLQ 281
Cdd:pfam15709 395 RLEEERQRQEEEERKQRLQLQAAQErarqqqeEFRRKLQELQRKKQQEEAERAEAE--KQRQKELEMQLA---EEQKRLM 469


                  ....*
gi 300794015  282 GTVEE 286
Cdd:pfam15709 470 EMAEE 474
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-295 6.20e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 6.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 115 ARLGKALLERNQDMsRQYEQMHKELTDKLEHLEQEKHELR---RRFENREGEWEG--RVSELETDVKQLQDELERQQVHL 189
Cdd:PRK03918 241 EELEKELESLEGSK-RKLEEKIRELEERIEELKKEIEELEekvKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRL 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015 190 READREKTRAVQELSEQNQRLLDQLSRASEVERQLSM--QVHALKEDFREKNSSTNQHIIRL-----ESLQAEIKMLSDR 262
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKA 399

                        170       180       190
                 ....*....|....*....|....*....|...
gi 300794015 263 KRELEHRLSATLEENDLLQGTVEELQDRVLILE 295
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELK 432
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 96-333 9.11e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 38.95  E-value: 9.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015    96 QDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTD------KLEH-LEQEKHELRRRFENREGEWEGRV 168
Cdd:pfam15921  378 QLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDrnmevqRLEAlLKAMKSECQGQMERQMAAIQGKN 457

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   169 SELETdVKQLQDELERQQVHLREADREKTRAVQELSEQNQRLLDQLSRASEVERqlsmQVHALKEDFREKNSSTNQHIIR 248
Cdd:pfam15921  458 ESLEK-VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER----AIEATNAEITKLRSRVDLKLQE 532

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015   249 LESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKD-LQLHQSQL---------ELQEVRL- 317
Cdd:pfam15921  533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGaMQVEKAQLekeindrrlELQEFKIl 612

                          250       260
                   ....*....|....*....|..
gi 300794015   318 ------SYRQLQVKVEELTEER 333
Cdd:pfam15921  613 kdkkdaKIRELEARVSDLELEK 634
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 122-486 9.74e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.93  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  122 LERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRfENREGEWEGRVSELETDVKQLQDELERQQVHLREADREKTRAVQ 201
Cdd:pfam05483  70 FENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQK-ENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIK 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  202 ELSEQNQ---RLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKmlsDRKRELEHRLSatlEEND 278
Cdd:pfam05483 149 ENNATRHlcnLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAE---NARLEMHFKLK---EDHE 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  279 LLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQVKVEELTEERSLQSSAATS--------TSLLSEIE 350
Cdd:pfam05483 223 KIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKEliekkdhlTKELEDIK 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300794015  351 QSME-AEELEQEREQLRLQLWEAYCQVrylcshlrgndsadsAVSTDSSMDESSETSSAKDVPAGSLRT---ALNDLKRL 426
Cdd:pfam05483 303 MSLQrSMSTQKALEEDLQIATKTICQL---------------TEEKEAQMEELNKAKAAHSFVVTEFEAttcSLEELLRT 367

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300794015  427 IQSIVDGVEPTVTLLSVEMTALKEERDRLRVTSEDKEPK-EQLQKAIRDRDEAIAKKKAVE 486
Cdd:pfam05483 368 EQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDEKKQFE 428
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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