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Conserved domains on  [gi|1958796896|ref|XP_038937658|]
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dixin isoform X8 [Rattus norvegicus]

Protein Classification

Smc and DIX domain-containing protein( domain architecture ID 10466383)

Smc and DIX domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 321-396 1.10e-37

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


:

Pssm-ID: 459936  Cd Length: 77  Bit Score: 130.72  E-value: 1.10e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958796896 321 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGSHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 396
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 51-189 1.53e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 130
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958796896 131 LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH 189
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
 
Name Accession Description Interval E-value
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 321-396 1.10e-37

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


Pssm-ID: 459936  Cd Length: 77  Bit Score: 130.72  E-value: 1.10e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958796896 321 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGSHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 396
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
 321-397 1.41e-19

Domain present in Dishevelled and axin; Domain of unknown function.


Pssm-ID: 197474  Cd Length: 83  Bit Score: 82.46  E-value: 1.41e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958796896  321 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGsHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 397
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTKKN-YKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 51-189 1.53e-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: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 130
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958796896 131 LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH 189
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 57-200 4.05e-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: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   57 IRSRLDQSMEENQDLKKEllkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDL 127
Cdd:pfam15921  522 LRSRVDLKLQELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQL 595

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958796896  128 QRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLED---ALRKLSDASYQQVDLERELEQKDVLLAHRVKGDTDEVTN 200
Cdd:pfam15921  596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDlelEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNS 671
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 34-184 6.57e-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: 45.06  E-value: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   34 EDEQERpvaLCEPGVNPEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlra 113
Cdd:TIGR02169  314 ERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL--- 387

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958796896  114 nmdkdelhnqnVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKD 184
Cdd:TIGR02169  388 -----------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
 
Name Accession Description Interval E-value
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 321-396 1.10e-37

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


Pssm-ID: 459936  Cd Length: 77  Bit Score: 130.72  E-value: 1.10e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958796896 321 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGSHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 396
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
 321-397 1.41e-19

Domain present in Dishevelled and axin; Domain of unknown function.


Pssm-ID: 197474  Cd Length: 83  Bit Score: 82.46  E-value: 1.41e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958796896  321 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGsHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 397
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTKKN-YKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 51-189 1.53e-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: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 130
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958796896 131 LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH 189
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
51-181 1.87e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRL---------TQQDTSVLQLKQELLRANMDKDEL- 120
Cdd:COG3206   204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAELAELs 283

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958796896 121 ------HNQNVDLQRKLD--------ERNRLLGEYKKD---LGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELE 181
Cdd:COG3206   284 arytpnHPDVIALRAQIAalraqlqqEAQRILASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
66-183 3.59e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 3.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   66 EENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD-KDELHNQNVDLQRKLDERNRLLGEYKKD 144
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEAL 367

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958796896  145 LGQKD--------------RLLQQQQAKLEDALRKLSDASYQQVDLERELEQK 183
Cdd:COG4913    368 LAALGlplpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 51-183 2.60e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 130
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958796896 131 LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQK 183
Cdd:COG1196   325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 41-188 2.90e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  41 VALCEPGVNPEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD---- 116
Cdd:COG3883     5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieer 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896 117 KDELHNQNVDLQRK-----------------------------LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLS 167
Cdd:COG3883    85 REELGERARALYRSggsvsyldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164

                         170       180
                  ....*....|....*....|.
gi 1958796896 168 DASYQQVDLERELEQKDVLLA 188
Cdd:COG3883   165 ELEAAKAELEAQQAEQEALLA 185
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 57-200 4.05e-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: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   57 IRSRLDQSMEENQDLKKEllkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDL 127
Cdd:pfam15921  522 LRSRVDLKLQELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQL 595

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958796896  128 QRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLED---ALRKLSDASYQQVDLERELEQKDVLLAHRVKGDTDEVTN 200
Cdd:pfam15921  596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDlelEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNS 671
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 34-184 6.57e-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: 45.06  E-value: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   34 EDEQERpvaLCEPGVNPEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlra 113
Cdd:TIGR02169  314 ERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL--- 387

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958796896  114 nmdkdelhnqnVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKD 184
Cdd:TIGR02169  388 -----------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 51-182 6.81e-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: 45.05  E-value: 6.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 130
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958796896  131 LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQ 182
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
51-182 1.94e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 130
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958796896 131 LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQ 182
Cdd:COG4372   124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 34-183 2.32e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 2.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   34 EDEQERPVALCEPGVNPEEQLIIIRSRLDQ-------SMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQL 106
Cdd:TIGR02169  346 EEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaeTRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958796896  107 KQELLRANMDKDELHNQNVDLQRKLDErnrllgeykkdlgqKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQK 183
Cdd:TIGR02169  426 NAAIAGIEAKINELEEEKEDKALEIKK--------------QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
47-200 2.58e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   47 GVNPEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSV---------LQLKQEL--LRANM 115
Cdd:COG4913    605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELerLDASS 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  116 DK--------DELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDA-------LRKLSDASYQQVDLEREL 180
Cdd:COG4913    685 DDlaaleeqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlarleLRALLEERFAAALGDAVE 764

                          170       180
                   ....*....|....*....|
gi 1958796896  181 EQKDVLLAHRVKGDTDEVTN 200
Cdd:COG4913    765 RELRENLEERIDALRARLNR 784
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 51-218 2.66e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNL------QGIKDALQQRLTQQDTS------------VLQLKQELLR 112
Cdd:COG4942    75 EQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrLGRQPPLALLLSPEDFLdavrrlqylkylAPARREQAEE 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896 113 ANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH--R 190
Cdd:COG4942   155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleA 234

                         170       180
                  ....*....|....*....|....*...
gi 1958796896 191 VKGDTDEVTNYNSHSSQRNGFVLPVAGR 218
Cdd:COG4942   235 EAAAAAERTPAAGFAALKGKLPWPVSGR 262
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 58-188 6.42e-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: 41.67  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  58 RSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRL 137
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958796896 138 LGE-----YK-------------KDLGQKDR-------LLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLA 188
Cdd:COG4942   106 LAEllralYRlgrqpplalllspEDFLDAVRrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 68-192 1.19e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   68 NQDLKKELLKCKQEARNLQGIKDALQQRLTQQDtsvlqLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQ 147
Cdd:TIGR00618  627 LQDVRLHLQQCSQELALKLTALHALQLTLTQER-----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958796896  148 KDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAHRVK 192
Cdd:TIGR00618  702 CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
51-188 1.25e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 130
Cdd:COG4372    51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896 131 LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLS--DASYQQVDLERELEQKDVLLA 188
Cdd:COG4372   131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAalEQELQALSEAEAEQALDELLK 190
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 64-188 1.89e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  64 SMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKK 143
Cdd:COG1579     1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958796896 144 DLGQ--KDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLA 188
Cdd:COG1579    81 QLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELA 127
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-169 2.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   58 RSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDEL-HNQNVDLQRKLDERNR 136
Cdd:COG4913    677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFA 756

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958796896  137 LLGEYKKdLGQKDRLLQQQQAKLEDALRKLSDA 169
Cdd:COG4913    757 AALGDAV-ERELRENLEERIDALRARLNRAEEE 788
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
52-182 3.01e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  52 EQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQ--QDTSVLQLKQELLRANMDKDELHNQNVDLQR 129
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEE 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958796896 130 KLDERNRLLGEYKkdlgQKDRLLQQQQAKLEDALRKLSDASYQQV-DLERELEQ 182
Cdd:COG4717   154 RLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELqDLAEELEE 203
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
51-173 3.67e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.12  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSmEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQEL--LRANMDkdELHNQNVDLQ 128
Cdd:COG1340   146 EKELEKAKKALEKN-EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAdeLRKEAD--ELHKEIVEAQ 222

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958796896 129 RKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQ 173
Cdd:COG1340   223 EKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEE 267
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 51-189 4.38e-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: 39.27  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQ 128
Cdd:TIGR02168  795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELE 865

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958796896  129 RKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH 189
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 58-181 5.19e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.03  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  58 RSRLDQS-MEENQDLKKELLKCKQEArnlqgikDALQQRLTQQDTSVLQLKQEL--LRANMDKDELHNQNVD--LQRKLD 132
Cdd:pfam10174 459 REREDRErLEELESLKKENKDLKEKV-------SALQPELTEKESSLIDLKEHAssLASSGLKKDSKLKSLEiaVEQKKE 531

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958796896 133 ERNRLLGEYKK------------DLGQKDRLLQQQQAkledalRKLSDASYQQVDLERELE 181
Cdd:pfam10174 532 ECSKLENQLKKahnaeeavrtnpEINDRIRLLEQEVA------RYKEESGKAQAEVERLLG 586
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
51-182 5.49e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQdtsvlQLKQELLRANMDKDELHNQNVDLQRK 130
Cdd:COG4717    87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE-----ALEAELAELPERLEELEERLEELREL 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958796896 131 LDERNRLLGEYKKDLGQKDRLLQQ----QQAKLEDALRKLSDASYQQVDLERELEQ 182
Cdd:COG4717   162 EEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEE 217
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 51-184 5.72e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQ----------------DTSVLQL-------- 106
Cdd:COG3883    36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelgeraralyrsggSVSYLDVllgsesfs 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896 107 ----------------KQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDAS 170
Cdd:COG3883   116 dfldrlsalskiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195

                         170
                  ....*....|....
gi 1958796896 171 YQQVDLERELEQKD 184
Cdd:COG3883   196 AQLAELEAELAAAE 209
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 51-174 5.78e-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: 38.88  E-value: 5.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   51 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELL-RANMDKD---ELHNQNVD 126
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIED 965

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958796896  127 LQRKLDERNRLLGEYKKDLG------------QKDRL--LQQQQAKLEDALRKLSDA--------------SYQQV 174
Cdd:TIGR02168  966 DEEEARRRLKRLENKIKELGpvnlaaieeyeeLKERYdfLTAQKEDLTEAKETLEEAieeidrearerfkdTFDQV 1041
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 51-182 6.47e-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: 39.00  E-value: 6.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896   51 EEQLIIIRSRLDQSMEENQDLKKelLKCKQEARnlqgIKDaLQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 130
Cdd:pfam01576  158 EERISEFTSNLAEEEEKAKSLSK--LKNKHEAM----ISD-LEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958796896  131 LDErnrllgeYKKDLGQKDRLLQQQQAKLED-------ALRKLSDASYQQVDLERELEQ 182
Cdd:pfam01576  231 IAE-------LRAQLAKKEEELQAALARLEEetaqknnALKKIRELEAQISELQEDLES 282
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 89-283 6.54e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  89 KDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLgeykkdlgqkdRLLQQQQAKLEDALRKLSD 168
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----------RALEQELAALEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896 169 asyQQVDLERELEQKDVLLAHRVkgdtdeVTNYNshSSQRNGFVLPVAGRAATTATHRgpqssdLQLVRDALRSLRNSFS 248
Cdd:COG4942    91 ---EIAELRAELEAQKEELAELL------RALYR--LGRQPPLALLLSPEDFLDAVRR------LQYLKYLAPARREQAE 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958796896 249 GHDPQHHTIDSLEQGISSLIERLHVIETQKKQERK 283
Cdd:COG4942   154 ELRADLAELAALRAELEAERAELEALLAELEEERA 188
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 59-161 7.81e-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: 38.46  E-value: 7.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  59 SRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLL 138
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283

                          90       100
                  ....*....|....*....|...
gi 1958796896 139 GEYKKDLgqkdrllQQQQAKLED 161
Cdd:TIGR04523 284 KELEKQL-------NQLKSEISD 299
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 49-183 9.53e-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: 38.08  E-value: 9.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796896  49 NPEEQLIIIRSRL-DQSMEENQDLKKELlkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDL 127
Cdd:TIGR04523 285 ELEKQLNQLKSEIsDLNNQKEQDWNKEL---KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958796896 128 QRKLDERNRLLGEYKKdlgQKDRLLQQQQaKLEDALRKLSDASYQQVDLERELEQK 183
Cdd:TIGR04523 362 QRELEEKQNEIEKLKK---ENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQ 413
 
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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