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Conserved domains on  [gi|1958669645|ref|XP_038945711|]
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coiled-coil domain-containing protein 62 isoform X10 [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 ...
66-340 9.09e-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: 56.99  E-value: 9.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   66 EKQRKELQLLIGELKDRDKEL----------NDMVAVHQRQL----LSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELeelqeelkeaEEELEELTAELqeleEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  132 MKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  212 IIEAvnhisdcSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKttENNEQREEIIRLKQEKSC 291
Cdd:TIGR02168  381 LETL-------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE 451
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958669645  292 LHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKLEVSEEPNEN 340
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
66-340 9.09e-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: 56.99  E-value: 9.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   66 EKQRKELQLLIGELKDRDKEL----------NDMVAVHQRQL----LSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELeelqeelkeaEEELEELTAELqeleEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  132 MKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  212 IIEAvnhisdcSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKttENNEQREEIIRLKQEKSC 291
Cdd:TIGR02168  381 LETL-------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE 451
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958669645  292 LHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKLEVSEEPNEN 340
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
51-332 9.24e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 9.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  51 YRRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKS 130
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 131 LMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDK 210
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 211 DIIEAVNHISDcsgkfklLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKS 290
Cdd:COG1196   394 AAAELAAQLEE-------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958669645 291 CLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKLE 332
Cdd:COG1196   467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
71-287 9.92e-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: 37.79  E-value: 9.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   71 ELQLLIGELKDRDKELNDMVAVHQRQllsWEEDRQKVLTLEErcskLEGELHKRTDIIKSLMKKVKTLESnqmECQTALQ 150
Cdd:pfam15921  378 QLQKLLADLHKREKELSLEKEQNKRL---WDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAMKS---ECQGQME 447
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  151 KTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQA---LTTMIKLKDKDIIEAVNHISDCSGKFk 227
Cdd:pfam15921  448 RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdLTASLQEKERAIEATNAEITKLRSRV- 526
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  228 llehalrDAKMAETCVVKEKQDYkqkLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQ 287
Cdd:pfam15921  527 -------DLKLQELQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ 576
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
66-340 9.09e-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: 56.99  E-value: 9.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   66 EKQRKELQLLIGELKDRDKEL----------NDMVAVHQRQL----LSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELeelqeelkeaEEELEELTAELqeleEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  132 MKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  212 IIEAvnhisdcSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKttENNEQREEIIRLKQEKSC 291
Cdd:TIGR02168  381 LETL-------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE 451
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958669645  292 LHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKLEVSEEPNEN 340
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
51-332 9.24e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 9.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  51 YRRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKS 130
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 131 LMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDK 210
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 211 DIIEAVNHISDcsgkfklLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKS 290
Cdd:COG1196   394 AAAELAAQLEE-------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958669645 291 CLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKLE 332
Cdd:COG1196   467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
52-335 7.18e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 7.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   52 RRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEK 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  132 MKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  212 IIEAVNHISDCSGKFKLLEHALRDAKMaetcvvkEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQeksc 291
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSE-------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA---- 462
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1958669645  292 lhdeliftvEREKRKDELLDIaKSKQDRTNSELQNLRQKLEVSE 335
Cdd:TIGR02169  463 ---------DLSKYEQELYDL-KEEYDRVEKELSKLQRELAEAE 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
47-332 7.26e-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: 51.21  E-value: 7.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   47 STTLYRRQNI----------GSEVESSTIEKQ--RKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERC 114
Cdd:TIGR02168  670 SSILERRREIeeleekieelEEKIAELEKALAelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  115 SKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQL 194
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  195 QAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTE 274
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958669645  275 NNEQREEIIRLKQEKSCLHDELI-FTVEREKRKDEL-------LDIAKSKQDRTNSELQNLRQKLE 332
Cdd:TIGR02168  910 RSELRRELEELREKLAQLELRLEgLEVRIDNLQERLseeysltLEEAEALENKIEDDEEEARRRLK 975
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
37-288 2.66e-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: 49.28  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   37 VRERASSMNPSTTLYRRQNIGSEVESSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKV--------- 107
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqieqlke 796
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  108 --LTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLV 185
Cdd:TIGR02168  797 elKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  186 DLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETcvvKEKQDYKQKLKALRIEVNKLR 265
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTL 953
                          250       260
                   ....*....|....*....|....*..
gi 1958669645  266 EDL----NEKTTENNEQREEIIRLKQE 288
Cdd:TIGR02168  954 EEAealeNKIEDDEEEARRRLKRLENK 980
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
187-336 1.19e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 187 LSAQVGQL--QAR--EQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVN 262
Cdd:COG1196   198 LERQLEPLerQAEkaERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958669645 263 KLREDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKLEVSEE 336
Cdd:COG1196   278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
96-342 1.93e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  96 QLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKAthsALLSEDLEA 175
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL---AELEKEIAE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 176 RNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDcsgkFKLLEHALRDAkmaetcvVKEKQDYKQKLK 255
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARREQ-------AEELRADLAELA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 256 ALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELifTVEREKRKDELLDIAKSKQdrtnsELQNLRQKLEVSE 335
Cdd:COG4942   164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL--EKELAELAAELAELQQEAE-----ELEALIARLEAEA 236

                  ....*..
gi 1958669645 336 EPNENTT 342
Cdd:COG4942   237 AAAAERT 243
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
62-316 2.73e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  62 SSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESN 141
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 142 QMECQTALQKTQQQLQEMAQKATHSALLS----EDLEARNENLSSTLVDLSAQVGQLQAREQALTTmiklkdkdiieavn 217
Cdd:COG4942    99 LEAQKEELAELLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRADLAELAA-------------- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 218 hisdcsgkfklLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKSCLHDELI 297
Cdd:COG4942   165 -----------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
                         250
                  ....*....|....*....
gi 1958669645 298 FTVEREKRKDELLDIAKSK 316
Cdd:COG4942   234 AEAAAAAERTPAAGFAALK 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
125-336 1.04e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 125 TDIIKSLMKKVKTLESnqmECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTM 204
Cdd:COG1196   192 EDILGELERQLEPLER---QAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 205 IKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIR 284
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958669645 285 LKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKLEVSEE 336
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
65-336 3.72e-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: 42.36  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   65 IEKQRKELQLLIGELKDRDKELNDMvavhqRQLLSWEEdrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQME 144
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDEL-----SQELSDAS--RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  145 CQTALQKTQQQLQEMAQKATHSALLSEDLEAR------------NENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDI 212
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  213 IEAVNHISDCSGKFKLLEHALRDAKmaetcvvKEKQDYKQKLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQEKscl 292
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLN-------GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI--- 905
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1958669645  293 hDELIFTVEREKRKDELLDIAKSKQDRTNSELQ-NLRQKLEVSEE 336
Cdd:TIGR02169  906 -EELEAQIEKKRKRLSELKAKLEALEEELSEIEdPKGEDEEIPEE 949
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
85-288 1.54e-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: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   85 ELNDMVAVHQRQLLSWEeDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQtALQKTQQQLQEMAQKAT 164
Cdd:COG4913    591 EKDDRRRIRSRYVLGFD-NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAER 668
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  165 HSALLSEDLEARNENlSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAkmAETCVV 244
Cdd:COG4913    669 EIAELEAELERLDAS-SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARL 745
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958669645  245 KEKQDYKQKLKALRIE--VNKLREDLNEK----TTENNEQREEIIRLKQE 288
Cdd:COG4913    746 ELRALLEERFAAALGDavERELRENLEERidalRARLNRAEEELERAMRA 795
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
61-217 5.07e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 5.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   61 ESSTIEKQRKELQLLIGELKDRDKELNDmVAVHQRQLLSWEEDRQKVL-------TLEERCSKLEGELHKRTDIIKSLMK 133
Cdd:COG4913    635 ALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLDassddlaALEEQLEELEAELEELEEELDELKG 713
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  134 KVKTLESNQMECQTALQKTQQQLQEMAQKAthSALLSEDLEARNENLSSTLVdLSAQVGQLQAREQALTTMIKLKDKDII 213
Cdd:COG4913    714 EIGRLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELE 790

                   ....
gi 1958669645  214 EAVN 217
Cdd:COG4913    791 RAMR 794
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
106-332 5.07e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 106 KVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQMECQTALQKTQQQLQEMAQKATHSALLSEDLEARNENLSSTLV 185
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645 186 DLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVKEKQDYKQKLKALRIEVNKLR 265
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958669645 266 EDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQKLE 332
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
71-287 9.92e-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: 37.79  E-value: 9.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645   71 ELQLLIGELKDRDKELNDMVAVHQRQllsWEEDRQKVLTLEErcskLEGELHKRTDIIKSLMKKVKTLESnqmECQTALQ 150
Cdd:pfam15921  378 QLQKLLADLHKREKELSLEKEQNKRL---WDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAMKS---ECQGQME 447
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  151 KTQQQLQEMAQKATHSALLSEDLEARNENLSSTLVDLSAQVGQLQAREQA---LTTMIKLKDKDIIEAVNHISDCSGKFk 227
Cdd:pfam15921  448 RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdLTASLQEKERAIEATNAEITKLRSRV- 526
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669645  228 llehalrDAKMAETCVVKEKQDYkqkLKALRIEVNKLREDLNEKTTENNEQREEIIRLKQ 287
Cdd:pfam15921  527 -------DLKLQELQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ 576
 
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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