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Conserved domains on  [gi|564379397|ref|XP_006249419|]
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coiled-coil domain-containing protein 62 isoform X4 [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 ...
 66-329 3.14e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    66 EKQRKELQLLIGELKDRDKEL----------NDMVAVHQRQL----LSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELeelqeelkeaEEELEELTAELqeleEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   132 MKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   212 IIEAvnhisdcSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKttENNEQREEIIRLKQEKSC 291
Cdd:TIGR02168  381 LETL-------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE 451

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 564379397   292 LHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-329 3.14e-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: 60.46  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    66 EKQRKELQLLIGELKDRDKEL----------NDMVAVHQRQL----LSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELeelqeelkeaEEELEELTAELqeleEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   132 MKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   212 IIEAvnhisdcSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKttENNEQREEIIRLKQEKSC 291
Cdd:TIGR02168  381 LETL-------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE 451

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 564379397   292 LHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 51-329 1.01e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  51 YRRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKS 130
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 131 LMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDK 210
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 211 DIIEAVNHISDcsgkfklLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKS 290
Cdd:COG1196  394 AAAELAAQLEE-------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564379397 291 CLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:COG1196  467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 61-378 9.22e-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: 45.88  E-value: 9.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    61 ESSTIEKQrkeLQLLIGELKDRDKELNdmVAVHQRQLLsWEEDRQKVLTLEErcskLEGELHKRTDIIKSLMKKVKTLES 140
Cdd:pfam15921  371 ESGNLDDQ---LQKLLADLHKREKELS--LEKEQNKRL-WDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAMKS 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   141 nqmECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQA---LTTMIKLKDKdIIEAVN 217
Cdd:pfam15921  441 ---ECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdLTASLQEKER-AIEATN 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   218 -HISDCSGKFkllehalrDAKMAETCVVKEKQDYkqkLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQ--------- 287
Cdd:pfam15921  517 aEITKLRSRV--------DLKLQELQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrta 585

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   288 -----EKSCLHDELiftverEKRKDEL--LDIAKSKQDRTNSELQnlrqiyvKQQSDLQFLNFNVEN--SQELIQIHGLK 358
Cdd:pfam15921  586 gamqvEKAQLEKEI------NDRRLELqeFKILKDKKDAKIRELE-------ARVSDLELEKVKLVNagSERLRAVKDIK 652

                          330       340
                   ....*....|....*....|
gi 564379397   359 MEEPKALECSRDmCLSDLDN 378
Cdd:pfam15921  653 QERDQLLNEVKT-SRNELNS 671
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
61-361 6.68e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 6.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  61 ESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLtleERCSKLEGELHKRTDIIKSLMKKVKTLES 140
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL---AEAGLDDADAEAVEARREELEDRDEELRD 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 141 NQMECQTALQKTQQQLQEMAQKAthsallsEDLEARNEnlsstlvdlsaqvgqlQAREQALTTmiklkDKDIIEAVNHIS 220
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDA-------DDLEERAE----------------ELREEAAEL-----ESELEEAREAVE 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 221 DCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEII---RLKQEKSC------ 291
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaeALLEAGKCpecgqp 460

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564379397 292 LHDELIFTV--EREKRKDEL---LDIAKSKQDRTNSELQNLRQIyVKQQSDLQFLNFNVENSQELIQIHGLKMEE 361
Cdd:PRK02224 461 VEGSPHVETieEDRERVEELeaeLEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEE 534
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-329 3.14e-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: 60.46  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    66 EKQRKELQLLIGELKDRDKEL----------NDMVAVHQRQL----LSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELeelqeelkeaEEELEELTAELqeleEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   132 MKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   212 IIEAvnhisdcSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKttENNEQREEIIRLKQEKSC 291
Cdd:TIGR02168  381 LETL-------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE 451

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 564379397   292 LHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 51-329 1.01e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  51 YRRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKS 130
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 131 LMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDK 210
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 211 DIIEAVNHISDcsgkfklLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKS 290
Cdd:COG1196  394 AAAELAAQLEE-------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564379397 291 CLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:COG1196  467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-321 2.24e-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: 57.76  E-value: 2.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    47 STTLYRRQNI----------GSEVESSTIEKQ--RKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERC 114
Cdd:TIGR02168  670 SSILERRREIeeleekieelEEKIAELEKALAelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   115 SKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKAthsallsEDLEARNENLSSTLVDLSAQVGQL 194
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-------KALREALDELRAELTLLNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   195 QAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTE 274
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 564379397   275 NNEQREEIIRLKQEksclHDELiftveREKRKDELLDIAKSKQDRTN 321
Cdd:TIGR02168  903 LRELESKRSELRRE----LEEL-----REKLAQLELRLEGLEVRIDN 940
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 52-329 1.94e-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: 54.69  E-value: 1.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    52 RRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   132 MKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   212 IIEAVNHISDCSGKFKLLEHALRDAKMaetcvvkEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQeksc 291
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSE-------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA---- 462

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 564379397   292 lhdeliftvEREKRKDELLDIaKSKQDRTNSELQNLRQ 329
Cdd:TIGR02169  463 ---------DLSKYEQELYDL-KEEYDRVEKELSKLQR 490
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 62-316 5.55e-07

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: 52.07  E-value: 5.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  62 SSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESN 141
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 142 QMECQTALQKTQQQLQEMAQKATHSALLS----EDLEARNENLSSTLVDLSAQVGQLQAREQALTTmiklkdkdiieavn 217
Cdd:COG4942   99 LEAQKEELAELLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRADLAELAA-------------- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 218 hisdcsgkfklLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELI 297
Cdd:COG4942  165 -----------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233

                        250
                 ....*....|....*....
gi 564379397 298 FTVEREKRKDELLDIAKSK 316
Cdd:COG4942  234 AEAAAAAERTPAAGFAALK 252
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 96-329 2.81e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  96 QLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKAthsALLSEDLEA 175
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL---AELEKEIAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 176 RNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNhisdcsgKFKLLEHALR-DAKMAEtcvvkEKQDYKQKL 254
Cdd:COG4942   95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR-------RLQYLKYLAPaRREQAE-----ELRADLAEL 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564379397 255 KALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELiftVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:COG4942  163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEA 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 125-370 3.63e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 3.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   125 TDIIKSLMKKVKTLESnQMECQTALQKTQQQLqemaqKATHSALLSEDLEARNENLSStlvdLSAQVGQLQAREQALTTM 204
Cdd:TIGR02168  192 EDILNELERQLKSLER-QAEKAERYKELKAEL-----RELELALLVLRLEELREELEE----LQEELKEAEEELEELTAE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   205 IKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEV--------------NKLREDLNE 270
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLeeleaqleelesklDELAEELAE 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   271 KTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNVENSQE 350
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421

                          250       260
                   ....*....|....*....|
gi 564379397   351 LIQIHGLKMEEPKALECSRD 370
Cdd:TIGR02168  422 EIEELLKKLEEAELKELQAE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 125-366 3.73e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 125 TDIIKSLMKKVKTLESnqmECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTM 204
Cdd:COG1196  192 EDILGELERQLEPLER---QAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 205 IKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIR 284
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 285 LKQEKSCLHDELIFTVEREKRKD-ELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNVENSQELIQIHGLKMEEPK 363
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEaELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428


                 ...
gi 564379397 364 ALE 366
Cdd:COG1196  429 ALA 431
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 65-324 3.13e-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: 47.37  E-value: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    65 IEKQRKELQLLIGELKDRDKELNDMvavhqRQLLSWEEdrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQME 144
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDEL-----SQELSDAS--RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   145 CQTALQKTQQQLQEMAQKATHSALLSEDLEAR------------NENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDI 212
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   213 IEAVNHISDCSGKFKLLEHALRDAKmaetcvvKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKscl 292
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLN-------GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI--- 905

                          250       260       270
                   ....*....|....*....|....*....|..
gi 564379397   293 hDELIFTVEREKRKDELLDIAKSKQDRTNSEL 324
Cdd:TIGR02169  906 -EELEAQIEKKRKRLSELKAKLEALEEELSEI 936
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
85-288 5.09e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   85 ELNDMVAVHQRQLLSWEeDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQtALQKTQQQLQEMAQkaT 164
Cdd:COG4913   591 EKDDRRRIRSRYVLGFD-NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVAS--A 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  165 HSALlsEDLEARNENLSSTLVDLSA---QVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAkmAET 241
Cdd:COG4913   667 EREI--AELEAELERLDASSDDLAAleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDL 742

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564379397  242 CVVKEKQDYKQKLKALRIE--VNKLREDLNEK----TTENNEQREEIIRLKQE 288
Cdd:COG4913   743 ARLELRALLEERFAAALGDavERELRENLEERidalRARLNRAEEELERAMRA 795
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 61-378 9.22e-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: 45.88  E-value: 9.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    61 ESSTIEKQrkeLQLLIGELKDRDKELNdmVAVHQRQLLsWEEDRQKVLTLEErcskLEGELHKRTDIIKSLMKKVKTLES 140
Cdd:pfam15921  371 ESGNLDDQ---LQKLLADLHKREKELS--LEKEQNKRL-WDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAMKS 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   141 nqmECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQA---LTTMIKLKDKdIIEAVN 217
Cdd:pfam15921  441 ---ECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdLTASLQEKER-AIEATN 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   218 -HISDCSGKFkllehalrDAKMAETCVVKEKQDYkqkLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQ--------- 287
Cdd:pfam15921  517 aEITKLRSRV--------DLKLQELQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrta 585

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   288 -----EKSCLHDELiftverEKRKDEL--LDIAKSKQDRTNSELQnlrqiyvKQQSDLQFLNFNVEN--SQELIQIHGLK 358
Cdd:pfam15921  586 gamqvEKAQLEKEI------NDRRLELqeFKILKDKKDAKIRELE-------ARVSDLELEKVKLVNagSERLRAVKDIK 652

                          330       340
                   ....*....|....*....|
gi 564379397   359 MEEPKALECSRDmCLSDLDN 378
Cdd:pfam15921  653 QERDQLLNEVKT-SRNELNS 671
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
61-203 1.88e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  61 ESSTIEKQRKELQLLIGELKDRDKELNDMVAvHQRQLLSWEEDRQKVLTLEERCSKLEGELHKrtdiIKSLMKKVKTLES 140
Cdd:COG4717   96 ELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEA 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564379397 141 NQMECQTALQKTQQQLQEMAQKATHSALLS-EDLEARNENLSSTLVDLSAQVGQLQAREQALTT 203
Cdd:COG4717  171 ELAELQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 146-353 2.23e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 146 QTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGK 225
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 226 FKLLEHAL--------RDAKMAETCVVKEKQDYKQKLKALRIeVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELI 297
Cdd:COG4942   99 LEAQKEELaellralyRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564379397 298 FTVEREKRKDELLDIAKSKQDRTnseLQNLRQIYVKQQSDLQFLNFNVENSQELIQ 353
Cdd:COG4942  178 ALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIA 230
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
64-278 2.71e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   64 TIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWE------EDRQKVLTLEERCSKLEGELhkrtdiikslmkkvkt 137
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeysWDEIDVASAEREIAELEAEL---------------- 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  138 lesnqmecqTALQKTQQQLQEMAQKAthsallsEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKdKDIIEAVN 217
Cdd:COG4913   678 ---------ERLDASSDDLAALEEQL-------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL-QDRLEAAE 740

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564379397  218 HISDcSGKFKLLEHALRDAkMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQ 278
Cdd:COG4913   741 DLAR-LELRALLEERFAAA-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 128-325 2.74e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 128 IKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHsalLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKL 207
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE---LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 208 -----KDKDIIEAV---NHISDCSGKFKLLEHAL-RDAKMaetcvVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQ 278
Cdd:COG3883   95 lyrsgGSVSYLDVLlgsESFSDFLDRLSALSKIAdADADL-----LEELKADKAELEAKKAELEAKLAELEALKAELEAA 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564379397 279 REEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQ 325
Cdd:COG3883  170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
65-297 3.53e-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: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   65 IEKQRKELQLL--IGELKDRDKELNDMVAVHQ--RQLLSWEEDRQKVLTLEERCSKLEGELhkrtdiikslmkkvKTLES 140
Cdd:COG4913   244 LEDAREQIELLepIRELAERYAAARERLAELEylRAALRLWFAQRRLELLEAELEELRAEL--------------ARLEA 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  141 NQMECQTALQKTQQQLQEM-AQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAreqaLTTMIKLKDKDIIEAvnhi 219
Cdd:COG4913   310 ELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA----LLAALGLPLPASAEE---- 381

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379397  220 sdcsgkFKLLEHALRDAKmaetcvvkekQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELI 297
Cdd:COG4913   382 ------FAALRAEAAALL----------EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
61-217 3.53e-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: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   61 ESSTIEKQRKELQLLIGELKDRDKELNDmVAVHQRQLLSWEEDRQKVL-------TLEERCSKLEGELHKRTDIIKSLMK 133
Cdd:COG4913   635 ALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLDassddlaALEEQLEELEAELEELEEELDELKG 713

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  134 KVKTLESNQMECQTALQKTQQQLQEMAQKAthSALLSEDLEARNENLSSTlvDLSAQVG-QLQAREQALTTMIKLKDKDI 212
Cdd:COG4913   714 EIGRLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAALGD--AVERELReNLEERIDALRARLNRAEEEL 789


                  ....*
gi 564379397  213 IEAVN 217
Cdd:COG4913   790 ERAMR 794
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 63-353 3.73e-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: 43.86  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   63 STIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQ 142
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  143 MECQTALQKTQQQLQEMAQKAthsallsEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISdc 222
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKEL-------KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN-- 548

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  223 SGKFKLLEHALRDAKMAETcvvKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVER 302
Cdd:TIGR04523 549 KDDFELKKENLEKEIDEKN---KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564379397  303 EKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNVENSQELIQ 353
Cdd:TIGR04523 626 NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
61-361 6.68e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 6.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  61 ESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLtleERCSKLEGELHKRTDIIKSLMKKVKTLES 140
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL---AEAGLDDADAEAVEARREELEDRDEELRD 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 141 NQMECQTALQKTQQQLQEMAQKAthsallsEDLEARNEnlsstlvdlsaqvgqlQAREQALTTmiklkDKDIIEAVNHIS 220
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDA-------DDLEERAE----------------ELREEAAEL-----ESELEEAREAVE 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 221 DCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEII---RLKQEKSC------ 291
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaeALLEAGKCpecgqp 460

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564379397 292 LHDELIFTV--EREKRKDEL---LDIAKSKQDRTNSELQNLRQIyVKQQSDLQFLNFNVENSQELIQIHGLKMEE 361
Cdd:PRK02224 461 VEGSPHVETieEDRERVEELeaeLEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEE 534
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 84-364 7.06e-04

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 42.82  E-value: 7.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   84 KELNDMVAVHQRQLLSWEEDRQKVL-TLEERCSKLEGELH----KRTDIIKSLMKKVKtlESNQMECQtaLQKTQQQLQ- 157
Cdd:pfam07111 140 RELEEIQRLHQEQLSSLTQAHEEALsSLTSKAEGLEKSLNsletKRAGEAKQLAEAQK--EAELLRKQ--LSKTQEELEa 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  158 -----EMAQKATHSALLSE----DLEARNENLSSTL-------VDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISD 221
Cdd:pfam07111 216 qvtlvESLRKYVGEQVPPEvhsqTWELERQELLDTMqhlqedrADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDS 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  222 CSGKF----KLLEHALRDAKMAETCVVKEKQ-DYKQKLKALRIEVnklrEDLNEKTTENNEQREEIIRLKQEKSCLhdel 296
Cdd:pfam07111 296 LEPEFpkkcRSLLNRWREKVFALMVQLKAQDlEHRDSVKQLRGQV----AELQEQVTSQSQEQAILQRALQDKAAE---- 367

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379397  297 iFTVEREKRKDELLDIAKSKQDRTNSELQNlrqiyVKQQSDLQFLNFNVENSQELIQIHGLKMEEPKA 364
Cdd:pfam07111 368 -VEVERMSAKGLQMELSRAQEARRRQQQQT-----ASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVA 429
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 22-391 7.75e-04

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: 42.79  E-value: 7.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   22 TYGVSEVTRSWHQLSVRERASSMNPSTTLYRRQNIGSEVESSTIEKQR---------KELQL-------LIGELKDRDKE 85
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmstqkaleEDLQIatkticqLTEEKEAQMEE 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   86 LNDMVAVHQrqlLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLmkkvkTLEsnqmecqtaLQKTQQQLQEMAQKATH 165
Cdd:pfam05483 340 LNKAKAAHS---FVVTEFEATTCSLEELLRTEQQRLEKNEDQLKII-----TME---------LQKKSSELEEMTKFKNN 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  166 SALLSEDLE---ARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEavnhisdcsgkfklLEHALRDAKMAETC 242
Cdd:pfam05483 403 KEVELEELKkilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD--------------LEIQLTAIKTSEEH 468

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  243 VVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNS 322
Cdd:pfam05483 469 YLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRD 548

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  323 ELQNLRQIYVKQQSDLQF-LNFNVENSQELIQIHGLKMEEPKALECSRDMCLSDLDNNYPKIDIKRERNQ 391
Cdd:pfam05483 549 ELESVREEFIQKGDEVKCkLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENK 618
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
65-281 9.99e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 9.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  65 IEKQRKEL--------QLLIGELKDRDKELNDMvavhQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVK 136
Cdd:COG4717   51 LEKEADELfkpqgrkpELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 137 TLESNQmecqtALQKTQQQLQEMAQKAthsallsEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAv 216
Cdd:COG4717  127 LLPLYQ-----ELEALEAELAELPERL-------EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE- 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564379397 217 nhisdcsgkfklLEHALRDAKMAEtcvvKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREE 281
Cdd:COG4717  194 ------------LQDLAEELEELQ----QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
146-354 2.11e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 146 QTALQKTQQQLQEMAQKatHSALlseDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDcsgk 225
Cdd:COG3206  188 RKELEEAEAALEEFRQK--NGLV---DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE---- 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 226 fkllehALRDAKMaetcvvkekQDYKQKLKALRIEVNKLREDLnektTENNEQreeIIRLKQEKSCLHDELiftverEKR 305
Cdd:COG3206  259 ------LLQSPVI---------QQLRAQLAELEAELAELSARY----TPNHPD---VIALRAQIAALRAQL------QQE 310

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564379397 306 KDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNfnvENSQELIQI 354
Cdd:COG3206  311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELP---ELEAELRRL 356
PRK12704 PRK12704
phosphodiesterase; Provisional
 65-243 2.69e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397  65 IEKQRKELQlliGELKDRDKELNDMvavhQRQLLsweedrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQME 144
Cdd:PRK12704  66 IHKLRNEFE---KELRERRNELQKL----EKRLL------QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 145 CQTALQKTQQQLQEMAQkathsalLSEDlEARNENLSSTLVDLSAQVGQL------QAREQAlttmiKLKDKDIIeaVNH 218
Cdd:PRK12704 133 LEELIEEQLQELERISG-------LTAE-EAKEILLEKVEEEARHEAAVLikeieeEAKEEA-----DKKAKEIL--AQA 197

                        170       180
                 ....*....|....*....|....*
gi 564379397 219 ISDCSGkfkllEHAlrdakmAETCV 243
Cdd:PRK12704 198 IQRCAA-----DHV------AETTV 211
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
110-370 3.53e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 110 LEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEA---RNENLSSTLVD 186
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterEREELAEEVRD 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 187 LSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLRE 266
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 267 DLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNVE 346
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE 443

                        250       260
                 ....*....|....*....|....
gi 564379397 347 NSQELiqihglkMEEPKALECSRD 370
Cdd:PRK02224 444 EAEAL-------LEAGKCPECGQP 460
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 92-327 3.63e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.59  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    92 VHQRQLLS-WEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQL-QEMAQKATHSALL 169
Cdd:pfam12128  227 IRDIQAIAgIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLrTLDDQWKEKRDEL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   170 SEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRD---------AKMAE 240
Cdd:pfam12128  307 NGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDvtakynrrrSKIKE 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   241 TCV-----VKEKQDYKQKLKALRIEV---------NKLREDLNEKTTENNEQREEII-RLKQEKSCLHDELIF--TVERE 303
Cdd:pfam12128  387 QNNrdiagIKDKLAKIREARDRQLAVaeddlqaleSELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATpeLLLQL 466

                          250       260
                   ....*....|....*....|....
gi 564379397   304 KRKDELLDIAKSKQDRTNSELQNL 327
Cdd:pfam12128  467 ENFDERIERAREEQEAANAEVERL 490
PRK12704 PRK12704
phosphodiesterase; Provisional
 245-365 3.67e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397 245 KEKQDYKQ-KLKALRIEVNKLREDLnEKttENNEQREEIIRLKQeksclhdeliftveREKRKDELLDIAKSKQDRTNSE 323
Cdd:PRK12704  49 KEAEAIKKeALLEAKEEIHKLRNEF-EK--ELRERRNELQKLEK--------------RLLQKEENLDRKLELLEKREEE 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564379397 324 LQNLRQIYVKQQSDLQFLNFNVENS-----QELIQIHGLKMEEPKAL 365
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELieeqlQELERISGLTAEEAKEI 158
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 110-326 4.90e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 4.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   110 LEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQkathsalLSEDLEARNENLSSTLVDLSA 189
Cdd:pfam01576  157 LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK-------AKRKLEGESTDLQEQIAELQA 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   190 QV----GQLQAREQALTTMIKLKD----------KDIIEAVNHISDcsgkfklLEHALRDAKMAETCVVKEKQDYKQKLK 255
Cdd:pfam01576  230 QIaelrAQLAKKEEELQAALARLEeetaqknnalKKIRELEAQISE-------LQEDLESERAARNKAEKQRRDLGEELE 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   256 ALRI---------------------EVNKLREDLNEKTTENNEQREEiirLKQEKSCLHDELIFTVEREKRKDELLDIAK 314
Cdd:pfam01576  303 ALKTeledtldttaaqqelrskreqEVTELKKALEEETRSHEAQLQE---MRQKHTQALEELTEQLEQAKRNKANLEKAK 379

                          250
                   ....*....|..
gi 564379397   315 SKQDRTNSELQN 326
Cdd:pfam01576  380 QALESENAELQA 391
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 52-366 8.39e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.64  E-value: 8.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    52 RRQNIGSEV--ESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvltLEERCSKLEGELHKRTdiIK 129
Cdd:TIGR00606  752 KLQKVNRDIqrLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERK----IAQQAAKLQGSDLDRT--VQ 825

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   130 SLMKKVktlesnqmecqtalQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSA---QVGQLQAREQALTTMIK 206
Cdd:TIGR00606  826 QVNQEK--------------QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLV 891

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   207 LKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKalrIEVNKLREDLNE-----KTTENNEQREE 281
Cdd:TIGR00606  892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ---DKVNDIKEKVKNihgymKDIENKIQDGK 968

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   282 IIRLKQEKSCLHDELIFTVEREKRKDELLDiaKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNVENSQELIQIHGLKMEE 361
Cdd:TIGR00606  969 DDYLKQKETELNTVNAQLEECEKHQEKINE--DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQ 1046


                   ....*
gi 564379397   362 PKALE 366
Cdd:TIGR00606 1047 MQVLQ 1051
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 37-286 9.35e-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: 39.33  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397    37 VRERASSMNPSTTLYRRQNIGSEVESSTIEKqrkelqlligELKDRDKELNDMvavhqrQLLSWEEDrQKVLTLEERCSK 116
Cdd:pfam15921  567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEK----------EINDRRLELQEF------KILKDKKD-AKIRELEARVSD 629

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   117 LEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKathSALLSEDLEARNENLSSTLVDLSAQVGQLQA 196
Cdd:pfam15921  630 LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED---YEVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379397   197 R-EQALTTMIKLKDKD-------------IIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVN 262
Cdd:pfam15921  707 ElEQTRNTLKSMEGSDghamkvamgmqkqITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786

                          250       260
                   ....*....|....*....|....
gi 564379397   263 KLREDLNEKTTENNEQREEIIRLK 286
Cdd:pfam15921  787 KMAGELEVLRSQERRLKEKVANME 810
 
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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