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Conserved domains on  [gi|564379395|ref|XP_006249418|]
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coiled-coil domain-containing protein 62 isoform X2 [Rattus norvegicus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

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
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 62-298 1.26e-08

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 57.47  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  62 SSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESN 141
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 142 QMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDcsgKFKLLEHALRDAKMA 221
Cdd:COG4942   99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAE 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564379395 222 ETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSK 298
Cdd:COG4942  176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 62-298 1.26e-08

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: 57.47  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  62 SSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESN 141
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 142 QMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDcsgKFKLLEHALRDAKMA 221
Cdd:COG4942   99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAE 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564379395 222 ETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSK 298
Cdd:COG4942  176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 52-311 4.61e-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: 4.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395    52 RRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   132 MKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQ----DKDIIEAVNHISDCSGK 207
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevDKEFAETRDELKDYREK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   208 FKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELiftverEKR 287
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL------SKY 467

                          250       260
                   ....*....|....*....|....
gi 564379395   288 KDELLDIaKSKQDRTNSELQNLRQ 311
Cdd:TIGR02169  468 EQELYDL-KEEYDRVEKELSKLQR 490
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 61-247 1.75e-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: 48.19  E-value: 1.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395    61 ESSTIEKQrkeLQLLIGELKDRDKELNdmVAVHQRQLLsWEEDRQKVLTLEErcskLEGELHKRTDIIKSLMKKVKTLES 140
Cdd:pfam15921  371 ESGNLDDQ---LQKLLADLHKREKELS--LEKEQNKRL-WDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAMKS 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   141 nqmECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHALrDAKM 220
Cdd:pfam15921  441 ---ECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-EATN 516

                          170       180
                   ....*....|....*....|....*...
gi 564379395   221 AETCVVKEKQDYK-QKLKALRIEVNKLR 247
Cdd:pfam15921  517 AEITKLRSRVDLKlQELQHLKNEGDHLR 544
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-352 4.78e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  38 RERASS--MNPSTTLYRRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDmvavhqrQLLSWEEDR-QKVLTLEERC 114
Cdd:PRK02224 168 RERASDarLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDE-------EIERYEEQReQARETRDEAD 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 115 SKLEGELHKRTDIiKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKAthsallsEDLEARNENLSSTLvDLSAQDKDI 194
Cdd:PRK02224 241 EVLEEHEERREEL-ETLEAEIEDLRETIAETEREREELAEEVRDLRERL-------EELEEERDDLLAEA-GLDDADAEA 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 195 IEAvnHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCL 274
Cdd:PRK02224 312 VEA--RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379395 275 HDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNVENSQELiqihglkMEEPKALECSRD 352
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-------LEAGKCPECGQP 460
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 62-298 1.26e-08

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: 57.47  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  62 SSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESN 141
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 142 QMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDcsgKFKLLEHALRDAKMA 221
Cdd:COG4942   99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAE 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564379395 222 ETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSK 298
Cdd:COG4942  176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 51-321 1.98e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  51 YRRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKS 130
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 131 LMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQDKDIIEAvnhisdcsgkfkl 210
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE------------- 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 211 lEHALRDAKMAETcvvKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDE 290
Cdd:COG1196  381 -LEELAEELLEAL---RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                        250       260       270
                 ....*....|....*....|....*....|.
gi 564379395 291 LLDIAKSKQDRTNSELQNLRQIYVKQQSDLQ 321
Cdd:COG1196  457 EEEALLELLAELLEEAALLEAALAELLEELA 487
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 52-311 4.61e-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: 4.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395    52 RRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   132 MKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQ----DKDIIEAVNHISDCSGK 207
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevDKEFAETRDELKDYREK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   208 FKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELiftverEKR 287
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL------SKY 467

                          250       260
                   ....*....|....*....|....
gi 564379395   288 KDELLDIaKSKQDRTNSELQNLRQ 311
Cdd:TIGR02169  468 EQELYDL-KEEYDRVEKELSKLQR 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 37-312 9.78e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 9.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395    37 VRERASSMNPSTTLYRRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKV--------- 107
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqieqlke 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   108 --LTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLV 185
Cdd:TIGR02168  797 elKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   186 DLSAQDKDIIEAVnhisdcsgkfklleHALRDakmaetcvvkEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEII 265
Cdd:TIGR02168  877 ALLNERASLEEAL--------------ALLRS----------ELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 564379395   266 RLKQEKSCLHDELiftveREKRKDELLDIAKSKQDRTNSELQNLRQI 312
Cdd:TIGR02168  933 GLEVRIDNLQERL-----SEEYSLTLEEAEALENKIEDDEEEARRRL 974
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 61-247 1.75e-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: 48.19  E-value: 1.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395    61 ESSTIEKQrkeLQLLIGELKDRDKELNdmVAVHQRQLLsWEEDRQKVLTLEErcskLEGELHKRTDIIKSLMKKVKTLES 140
Cdd:pfam15921  371 ESGNLDDQ---LQKLLADLHKREKELS--LEKEQNKRL-WDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAMKS 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   141 nqmECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHALrDAKM 220
Cdd:pfam15921  441 ---ECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-EATN 516

                          170       180
                   ....*....|....*....|....*...
gi 564379395   221 AETCVVKEKQDYK-QKLKALRIEVNKLR 247
Cdd:pfam15921  517 AEITKLRSRVDLKlQELQHLKNEGDHLR 544
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
65-269 7.35e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 7.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  65 IEKQRKEL--------QLLIGELKDRDKELNDMvavhQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVK 136
Cdd:COG4717   51 LEKEADELfkpqgrkpELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 137 TLESNQmecqtALQKTQQQLQEMAQKAthsallsEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKL-LEHAL 215
Cdd:COG4717  127 LLPLYQ-----ELEALEAELAELPERL-------EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEEL 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564379395 216 RDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLN--EKTTENNEQREEIIRLKQ 269
Cdd:COG4717  195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARL 250
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-352 9.92e-05

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: 45.82  E-value: 9.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   117 LEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKAthsallsEDLEARNENLSSTLVDLSAQDKDIIE 196
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-------EELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   197 AvnhisdcsgkfklLEHALRDAKMAETcvvkEKQDYKQKLkalrievNKLREDLNEKTTENNEQREEIIRLKQEKSCLHD 276
Cdd:TIGR02168  310 R-------------LANLERQLEELEA----QLEELESKL-------DELAEELAELEEKLEELKEELESLEAELEELEA 365

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564379395   277 ELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNVENSQELIQIHGLKMEEPKALECSRD 352
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 65-311 1.50e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395    65 IEKQRKELQLLIGELKDRDKELNDMvavhqRQLLSWEEdrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQME 144
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDEL-----SQELSDAS--RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   145 CQTALQKTQQQLQEMAQKATHSALLSEDLEARN-----ENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHALRDAK 219
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   220 MAETCVVKE----KQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELiftVEREKRKDEL---L 292
Cdd:TIGR02169  836 QELQEQRIDlkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELeaqI 912

                          250
                   ....*....|....*....
gi 564379395   293 DIAKSKQDRTNSELQNLRQ 311
Cdd:TIGR02169  913 EKKRKRLSELKAKLEALEE 931
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 59-309 2.34e-04

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: 44.44  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395    59 EVESSTIEKQRKELQLLIGELKDrdkelndmvavHQRQllswEEDRQKVLtlEERCSKLEGELHKRTDIIKslmKKVKTL 138
Cdd:pfam12128  247 QQEFNTLESAELRLSHLHFGYKS-----------DETL----IASRQEER--QETSAELNQLLRTLDDQWK---EKRDEL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   139 ESNQMECQTALQKTQQQLQemAQKATHSALLSEDLEARN---ENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHAL 215
Cdd:pfam12128  307 NGELSAADAAVAKDRSELE--ALEDQHGAFLDADIETAAadqEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   216 RDAKMAETCVVKEKQDYKQKLKALRIEV---------NKLREDLNEKTTENNEQREEII-RLKQEKSCLHDELIF--TVE 283
Cdd:pfam12128  385 KEQNNRDIAGIKDKLAKIREARDRQLAVaeddlqaleSELREQLEAGKLEFNEEEYRLKsRLGELKLRLNQATATpeLLL 464

                          250       260
                   ....*....|....*....|....*.
gi 564379395   284 REKRKDELLDIAKSKQDRTNSELQNL 309
Cdd:pfam12128  465 QLENFDERIERAREEQEAANAEVERL 490
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
64-260 3.13e-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: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   64 TIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWE------EDRQKVLTLEERCSKLEGELHKrtdiIKSLMKKVKT 137
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeysWDEIDVASAEREIAELEAELER----LDASSDDLAA 689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  138 LESNQMECQTALQKTQQQLQEMAQKAthsALLSEDLEARNENLSSTLVDLSAQDKDIIEAVnhisdcsgkFKLLEHALRD 217
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELKGEI---GRLEKELEQAEEELDELQDRLEAAEDLARLEL---------RALLEERFAA 757

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 564379395  218 AkMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQ 260
Cdd:COG4913   758 A-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-352 4.78e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  38 RERASS--MNPSTTLYRRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDmvavhqrQLLSWEEDR-QKVLTLEERC 114
Cdd:PRK02224 168 RERASDarLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDE-------EIERYEEQReQARETRDEAD 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 115 SKLEGELHKRTDIiKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKAthsallsEDLEARNENLSSTLvDLSAQDKDI 194
Cdd:PRK02224 241 EVLEEHEERREEL-ETLEAEIEDLRETIAETEREREELAEEVRDLRERL-------EELEEERDDLLAEA-GLDDADAEA 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 195 IEAvnHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCL 274
Cdd:PRK02224 312 VEA--RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564379395 275 HDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNVENSQELiqihglkMEEPKALECSRD 352
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-------LEAGKCPECGQP 460
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 189-321 5.78e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 189 AQDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLK 268
Cdd:COG1196  222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564379395 269 QEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQ 321
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
 21-335 6.29e-04

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 43.22  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   21 STYGVSEVTRSWHQLSVRERASSMNPSTTLYRRQNIGSEVESSTIEKQrkELQLLIGELKDRDKELNDMvAVHQRQLLSW 100
Cdd:pfam18971 526 ATNGVSHLEAGFNKVAVFNLPDLNNLAITSFVRRNLENKLTAKGLSLQ--EANKLIKDFLSSNKELAGK-ALNFNKAVAE 602

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  101 EEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQ------LQEMAQKATHSALLSEDLE 174
Cdd:pfam18971 603 AKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKdeifalINKEANRDARAIAYTQNLK 682

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  175 ARNENLSSTLVDLSAQDKDIIEAVNHISDcsGKFKllehalrDAKMAEtcvvkekqdykQKLKALRIEVNKLR------- 247
Cdd:pfam18971 683 GIKRELSDKLEKISKDLKDFSKSFDEFKN--GKNK-------DFSKAE-----------ETLKALKGSVKDLGinpewis 742

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  248 --EDLNEKTTE-NNEQREEIIRLKQEKSCLHDELIFTVEREKRKDEL------LDIAK-----SKQDRTNSELQNLRQIY 313
Cdd:pfam18971 743 kvENLNAALNEfKNGKNKDFSKVTQAKSDLENSVKDVIINQKVTDKVdnlnqaVSVAKamgdfSRVEQVLADLKNFSKEQ 822

                         330       340
                  ....*....|....*....|..
gi 564379395  314 VKQQSDlQFLNFNVENSQELIQ 335
Cdd:pfam18971 823 LAQQAQ-KNEDFNTGKNSELYQ 843
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 125-335 1.35e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   125 TDIIKSLMKKVKTLESnQMECQTALQKTQQQLqemaqKATHSALLSEDLEARNENLSSTLVDLSAQDKDIIEAVNhisdc 204
Cdd:TIGR02168  192 EDILNELERQLKSLER-QAEKAERYKELKAEL-----RELELALLVLRLEELREELEELQEELKEAEEELEELTA----- 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   205 sgkfkllehalrdakmaetcvvkEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVER 284
Cdd:TIGR02168  261 -----------------------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564379395   285 EKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNVENSQELIQ 335
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
COG5022 COG5022
Myosin heavy chain [General function prediction only];
77-343 1.91e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.60  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   77 GELKDRDKELNDmvavhqrqlLSWEEDRQKVL-TLEERCSKLEGEL-----------HKRTdiikSLMKKVKTLESNQME 144
Cdd:COG5022   810 KEYRSYLACIIK---------LQKTIKREKKLrETEEVEFSLKAEVliqkfgrslkaKKRF----SLLKKETIYLQSAQR 876

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  145 CQTALQKTQQqLQEMAQKATHSALLSEDLEARNENLSSTLvdlsaqDKDIIEAVNHISDCSGKFK--LLEHALRDAKMAE 222
Cdd:COG5022   877 VELAERQLQE-LKIDVKSISSLKLVNLELESEIIELKKSL------SSDLIENLEFKTELIARLKklLNNIDLEEGPSIE 949

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  223 TCVVKEKQDYKQKLKALRiEVNKLREDLNEKTT----ENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELldiaksk 298
Cdd:COG5022   950 YVKLPELNKLHEVESKLK-ETSEEYEDLLKKSTilvrEGNKANSELKNFKKELAELSKQYGALQESTKQLKEL------- 1021

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 564379395  299 qDRTNSELQNLRQIYVKQQSDLQFLNfnveNSQELIQIHGLKMEE 343
Cdd:COG5022  1022 -PVEVAELQSASKIISSESTELSILK----PLQKLKGLLLLENNQ 1061
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
146-336 2.22e-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: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 146 QTALQKTQQQLQEMAQKatHSALlseDLEARNENLSSTLVDLSAQdkdIIEAVNHISDCSGKFKLLEHALRDAKMAETCV 225
Cdd:COG3206  188 RKELEEAEAALEEFRQK--NGLV---DLSEEAKLLLQQLSELESQ---LAEARAELAEAEARLAALRAQLGSGPDALPEL 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 226 VK--EKQDYKQKLKALRIEVNKLREDLnektTENNEQreeIIRLKQEKSCLHDELiftverEKRKDELLDIAKSKQDRTN 303
Cdd:COG3206  260 LQspVIQQLRAQLAELEAELAELSARY----TPNHPD---VIALRAQIAALRAQL------QQEAQRILASLEAELEALQ 326

                        170       180       190
                 ....*....|....*....|....*....|...
gi 564379395 304 SELQNLRQIYVKQQSDLQFLNfnvENSQELIQI 336
Cdd:COG3206  327 AREASLQAQLAQLEARLAELP---ELEAELRRL 356
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
61-203 2.27e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  61 ESSTIEKQRKELQLLIGELKDRDKELNDMVAvHQRQLLSWEEDRQKVLTLEERCSKLEGELHKrtdiIKSLMKKVKTLES 140
Cdd:COG4717   96 ELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEA 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564379395 141 NQMECQTALQKTQQQLQEMAQKATHSALLS-EDLEARNENLSSTLVDLSAQDKDIIEAVNHISD 203
Cdd:COG4717  171 ELAELQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 63-335 2.30e-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: 41.16  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   63 STIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQ 142
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  143 MECQTALQKTQQQL----QEMAQKATHSALLSEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGKFKLLEHALRDA 218
Cdd:TIGR04523 478 NKIKQNLEQKQKELkskeKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  219 KMAEtcVVKEKQ----DYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDI 294
Cdd:TIGR04523 558 NLEK--EIDEKNkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 564379395  295 AKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNVENSQELIQ 335
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
PRK12704 PRK12704
phosphodiesterase; Provisional
 227-347 2.53e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 227 KEKQDYKQ-KLKALRIEVNKLREDLnEKttENNEQREEIIRLKQeksclhdeliftveREKRKDELLDIAKSKQDRTNSE 305
Cdd:PRK12704  49 KEAEAIKKeALLEAKEEIHKLRNEF-EK--ELRERRNELQKLEK--------------RLLQKEENLDRKLELLEKREEE 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564379395 306 LQNLRQIYVKQQSDLQFLNFNVENS-----QELIQIHGLKMEEPKAL 347
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELieeqlQELERISGLTAEEAKEI 158
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 59-373 3.04e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   59 EVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQrQLLSWEEDRQKVLTLEercsklegeLHKRTDIIKSLMKKVKTL 138
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITME---------LQKKSSELEEMTKFKNNK 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  139 ESNQMECQTALQKTQQQLQEMAQKAThsalLSEDLEARNENLSSTLvdlSAQDKDIIEavnhisdcsgkfklLEHALRDA 218
Cdd:pfam05483 404 EVELEELKKILAEDEKLLDEKKQFEK----IAEELKGKEQELIFLL---QAREKEIHD--------------LEIQLTAI 462

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  219 KMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSK 298
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564379395  299 QDRTNSELQNLRQIYVKQQSDLQF-LNFNVENSQELIQIHGLKMEEPKALECSRDMCLSDLDNNYPKIDIKRERNQ 373
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDEVKCkLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENK 618
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
61-272 3.28e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   61 ESSTIEKQRKELQLLIGELKDRDKELNDmVAVHQRQLLSWEEDRQKVL-------TLEERCSKLEGELHKRTDIIKSLMK 133
Cdd:COG4913   635 ALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLDassddlaALEEQLEELEAELEELEEELDELKG 713

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  134 KVKTLESNQMECQTALQKTQQQLQEMAQKAthSALLSEDLEARNENLsstlvDLSAQDKDIIEAV-NHISDCSGKFKLLE 212
Cdd:COG4913   714 EIGRLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAA-----LGDAVERELRENLeERIDALRARLNRAE 786

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564379395  213 HALRDAkMAETcvvkeKQDYKQKLKALRIEVNKLRE--DLNEKTTENN--EQREEIIRLKQEKS 272
Cdd:COG4913   787 EELERA-MRAF-----NREWPAETADLDADLESLPEylALLDRLEEDGlpEYEERFKELLNENS 844
PRK12704 PRK12704
phosphodiesterase; Provisional
 65-183 3.73e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  65 IEKQRKELQlliGELKDRDKELNDMvavhQRQLLsweedrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQME 144
Cdd:PRK12704  66 IHKLRNEFE---KELRERRNELQKL----EKRLL------QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEE 132

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564379395 145 CQTALQKTQQQLQEMAQkathsalLSEDlEARNENLSST 183
Cdd:PRK12704 133 LEELIEEQLQELERISG-------LTAE-EAKEILLEKV 163
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
85-316 3.93e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395   85 ELNDMVAVHQRQLLSWEeDRQKVLTLEERCSKLEGELHkrtdiikslmkkvktlesnqmECQTALQKTQQQLQEMAQKAT 164
Cdd:COG4913   591 EKDDRRRIRSRYVLGFD-NRAKLAALEAELAELEEELA---------------------EAEERLEALEAELDALQERRE 648

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  165 HSALLSEdlearnenLSSTLVDLSAQDKDIIEAVNHISDC---SGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRI 241
Cdd:COG4913   649 ALQRLAE--------YSWDEIDVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK 720

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  242 EVNKLREDLnEKTTENNEQREEIIRLKQEKSC---LHDELIFTVEREKRK--DELLDIAKSKQDRTNSELQNLRQIYVKQ 316
Cdd:COG4913   721 ELEQAEEEL-DELQDRLEAAEDLARLELRALLeerFAAALGDAVERELREnlEERIDALRARLNRAEEELERAMRAFNRE 799
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
59-332 4.67e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  59 EVESSTIEKQRKELQLLIGELKDRDKELNDMVA----------VHQRQLLswEEDRQKVL---TLEerCSKLEGELHKRT 125
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpVCGRELT--EEHRKELLeeyTAE--LKRIEKELKEIE 472

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 126 DIIKSLMKKVKTLES--NQMECQTALQKTQQQLQEMAQKAthSALLSEDLEARN---ENLSSTLVDLSAQDKDIIEAVNH 200
Cdd:PRK03918 473 EKERKLRKELRELEKvlKKESELIKLKELAEQLKELEEKL--KKYNLEELEKKAeeyEKLKEKLIKLKGEIKSLKKELEK 550

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 201 ISDCSGKFKLLEHALRDA--KMAE---------------------------------TCVVKEKQDYKQKLKALRIEVNK 245
Cdd:PRK03918 551 LEELKKKLAELEKKLDELeeELAEllkeleelgfesveeleerlkelepfyneylelKDAEKELEREEKELKKLEEELDK 630

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 246 LREDLNEKTTENNEQREEIIRLKQEksclhdeliFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNF 325
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKK---------YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701


                 ....*..
gi 564379395 326 NVENSQE 332
Cdd:PRK03918 702 ELEEREK 708
46 PHA02562
endonuclease subunit; Provisional
 128-321 6.31e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 128 IKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSAllsEDLEARNENLSSTLVDLSAQDKDIIEAVNHISDCSGK 207
Cdd:PHA02562 190 IDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAK 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 208 -------FKLLEHALRDAKMAETCV------VKEKQDYKQKLKALRIEVNKL---REDLNEKTTENNEQREEIIRLKQEK 271
Cdd:PHA02562 267 ikskieqFQKVIKMYEKGGVCPTCTqqisegPDRITKIKDKLKELQHSLEKLdtaIDELEEIMDEFNEQSKKLLELKNKI 346

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564379395 272 SCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQ 321
Cdd:PHA02562 347 STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 63-271 8.95e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 8.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395  63 STIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKkvktlesnq 142
Cdd:COG3883   23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR--------- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564379395 143 mecqtALQKTQQQLQEMaqkathSALLS----EDLEARNENLSstlvDLSAQDKDIIEAVNHISDcsgKFKLLEHALRDA 218
Cdd:COG3883   94 -----ALYRSGGSVSYL------DVLLGsesfSDFLDRLSALS----KIADADADLLEELKADKA---ELEAKKAELEAK 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564379395 219 KMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEK 271
Cdd:COG3883  156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
 
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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