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Conserved domains on  [gi|1039793568|ref|XP_017168930|]
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dixin isoform X8 [Mus musculus]

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 ...
 362-437 2.87e-38

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: 133.42  E-value: 2.87e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039793568 362 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 437
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 75-330 8.09e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 8.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568   75 EQQEHLEKEMEEAKKMISGLQALLlngSLPEDEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEAR 154
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSI---AEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  155 NLQGIKDALQQRLTQQDTSVLQLKQELlranmdkdelhnqnVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEAL 234
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDEL--------------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  235 RKLSDASYQQVDLERELEQKDVLLAhcmKGETDEPQTS-DLQLVRDALRSLRNsfsghdpqhhTIDSLEQGISSLMERLH 313
Cdd:TIGR02169  427 AAIAGIEAKINELEEEKEDKALEIK---KQEWKLEQLAaDLSKYEQELYDLKE----------EYDRVEKELSKLQRELA 493

                          250
                   ....*....|....*...
gi 1039793568  314 VVETQKKQ-ERKVGGRSP 330
Cdd:TIGR02169  494 EAEAQARAsEERVRGGRA 511
 
Name Accession Description Interval E-value
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 362-437 2.87e-38

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: 133.42  E-value: 2.87e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039793568 362 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 437
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
 362-438 1.85e-19

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


Pssm-ID: 197474  Cd Length: 83  Bit Score: 82.46  E-value: 1.85e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793568  362 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 438
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 75-330 8.09e-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: 51.61  E-value: 8.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568   75 EQQEHLEKEMEEAKKMISGLQALLlngSLPEDEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEAR 154
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSI---AEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  155 NLQGIKDALQQRLTQQDTSVLQLKQELlranmdkdelhnqnVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEAL 234
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDEL--------------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  235 RKLSDASYQQVDLERELEQKDVLLAhcmKGETDEPQTS-DLQLVRDALRSLRNsfsghdpqhhTIDSLEQGISSLMERLH 313
Cdd:TIGR02169  427 AAIAGIEAKINELEEEKEDKALEIK---KQEWKLEQLAaDLSKYEQELYDLKE----------EYDRVEKELSKLQRELA 493

                          250
                   ....*....|....*...
gi 1039793568  314 VVETQKKQ-ERKVGGRSP 330
Cdd:TIGR02169  494 EAEAQARAsEERVRGGRA 511
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 71-260 8.91e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 8.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  71 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 150
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 151 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 230
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039793568 231 EEALRKLSDASYQQVDLERELEQKDVLLAH 260
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 74-258 2.62e-04

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: 43.57  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568   74 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSVEENQDLKKE 145
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  146 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLEERNRLLGEYKKEL 216
Cdd:pfam15921  540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1039793568  217 GQKDRLFQQQQAK---LEEALRKLSDASYQQVDLERELEQ-KDVLL 258
Cdd:pfam15921  614 DKKDAKIRELEARvsdLELEKVKLVNAGSERLRAVKDIKQeRDQLL 659
 
Name Accession Description Interval E-value
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 362-437 2.87e-38

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: 133.42  E-value: 2.87e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039793568 362 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 437
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
 362-438 1.85e-19

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


Pssm-ID: 197474  Cd Length: 83  Bit Score: 82.46  E-value: 1.85e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793568  362 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 438
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 75-330 8.09e-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: 51.61  E-value: 8.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568   75 EQQEHLEKEMEEAKKMISGLQALLlngSLPEDEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEAR 154
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSI---AEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  155 NLQGIKDALQQRLTQQDTSVLQLKQELlranmdkdelhnqnVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEAL 234
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDEL--------------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  235 RKLSDASYQQVDLERELEQKDVLLAhcmKGETDEPQTS-DLQLVRDALRSLRNsfsghdpqhhTIDSLEQGISSLMERLH 313
Cdd:TIGR02169  427 AAIAGIEAKINELEEEKEDKALEIK---KQEWKLEQLAaDLSKYEQELYDLKE----------EYDRVEKELSKLQRELA 493

                          250
                   ....*....|....*...
gi 1039793568  314 VVETQKKQ-ERKVGGRSP 330
Cdd:TIGR02169  494 EAEAQARAsEERVRGGRA 511
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 71-260 8.91e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 8.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  71 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 150
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 151 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 230
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039793568 231 EEALRKLSDASYQQVDLERELEQKDVLLAH 260
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 71-259 1.14e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  71 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpEDEQERPVALcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 150
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAEL------EELRLELEEL-------ELELEEAQAEEYELLAELARLEQDIARLE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 151 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 230
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                         170       180
                  ....*....|....*....|....*....
gi 1039793568 231 EEALRKLSDASYQQVDLERELEQKDVLLA 259
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLE 417
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
71-254 2.18e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 2.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568   71 EQLLEQQEHL---EKEMEEAKKMISGLQALLLNGSLPEDEQERpvalcepgvnpEEQLIIIRSRLD--QSVEENQDLKKE 145
Cdd:COG4913    228 DALVEHFDDLeraHEALEDAREQIELLEPIRELAERYAAARER-----------LAELEYLRAALRlwFAQRRLELLEAE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  146 LLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD-KDELHNQNVDLQRKLEERNRLLGEYK---KELGQKD- 220
Cdd:COG4913    297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEallAALGLPLp 376

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039793568  221 ----------RLFQQQQAKLEEALRKLSDASYQQVDLERELEQK 254
Cdd:COG4913    377 asaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 80-324 2.79e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 2.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568   80 LEKEMEEAKKMISGLQALLLNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGI 159
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREELEELQEELKEA--------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  160 KDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSD 239
Cdd:TIGR02168  290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  240 ASYQQVDLERELEQKDVLLAHCMKGETD--------EPQTSDLQLVRDALRS----LRNSFSGHDPQ--HHTIDSLEQGI 305
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASlnneierlEARLERLEDRRERLQQeieeLLKKLEEAELKelQAELEELEEEL 449

                          250
                   ....*....|....*....
gi 1039793568  306 SSLMERLHVVETQKKQERK 324
Cdd:TIGR02168  450 EELQEELERLEEALEELRE 468
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
122-252 4.86e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 122 EEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRL---------TQQDTSVLQLKQELLRANMDKDEL- 191
Cdd:COG3206   204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAELAELs 283

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793568 192 ------HNQNVDLQRKLE--------ERNRLLGEYKKE---LGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELE 252
Cdd:COG3206   284 arytpnHPDVIALRAQIAalraqlqqEAQRILASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 70-260 6.66e-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: 48.51  E-value: 6.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568   70 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERpVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELL 147
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  148 KCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQRKLEERNRLLGEYKKELGQKDRLFQQ 225
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1039793568  226 QQAKLEEALRKLSDASYQQVDLERELEQKDVLLAH 260
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ 926
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 75-259 1.08e-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: 44.37  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  75 EQQEHLEKEMEEAKKMISGLQALLlngslpEDEQERPVALcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCKQEAR 154
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKEL------AALKKEEKAL-------LKQLAALERRIAALARRIRALEQELAALEAELA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 155 NLQGIKDALQQRLTQQDT---SVLQLKQELLRANMDKDELHNQNVD--------LQRKLEERNRLLGEYKKELGQKDRLF 223
Cdd:COG4942    87 ELEKEIAELRAELEAQKEelaELLRALYRLGRQPPLALLLSPEDFLdavrrlqyLKYLAPARREQAEELRADLAELAALR 166

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039793568 224 QQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 259
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALEALKAERQKLLA 202
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 71-240 2.27e-04

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: 43.89  E-value: 2.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568   71 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpEDEQERPVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCK 150
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELI------EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  151 QEARNLQGIKDALQQRLTQQDTSVLQLKQELL-RANMDKD---ELHNQNVDLQRKLEERNRLLGEYKKELG--------- 217
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiee 994

                          170       180
                   ....*....|....*....|....*...
gi 1039793568  218 ---QKDRL--FQQQQAKLEEALRKLSDA 240
Cdd:TIGR02168  995 yeeLKERYdfLTAQKEDLTEAKETLEEA 1022
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
118-293 2.45e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  118 GVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSV---------LQLKQEL--LRANM 186
Cdd:COG4913    605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELerLDASS 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  187 DK--------DELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLL 258
Cdd:COG4913    685 DDlaaleeqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1039793568  259 AHCMK---GETDEpQTSDLQLVRDALRSLRNSFSGHDP 293
Cdd:COG4913    765 RELREnleERIDA-LRARLNRAEEELERAMRAFNREWP 801
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 74-258 2.62e-04

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: 43.57  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568   74 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSVEENQDLKKE 145
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  146 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLEERNRLLGEYKKEL 216
Cdd:pfam15921  540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1039793568  217 GQKDRLFQQQQAK---LEEALRKLSDASYQQVDLERELEQ-KDVLL 258
Cdd:pfam15921  614 DKKDAKIRELEARvsdLELEKVKLVNAGSERLRAVKDIKQeRDQLL 659
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 129-343 9.13e-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: 41.29  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 129 RSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRL 208
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 209 LGE-----YKKE--------LGQKD------------RLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLAhcmk 263
Cdd:COG4942   106 LAEllralYRLGrqpplallLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLA---- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 264 gETDEPQTSDLQLV---RDALRSLRNSFSGHDPQhhtIDSLEQGISSLMERLHVVETQKKQERKVGGRSPRNQASSEYRa 340
Cdd:COG4942   182 -ELEEERAALEALKaerQKLLARLEKELAELAAE---LAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP- 256


                  ...
gi 1039793568 341 sWP 343
Cdd:COG4942   257 -WP 258
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 139-263 9.61e-04

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: 41.88  E-value: 9.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  139 NQDLKKELLKCKQEARNLQGIKDALQQRLTQQDtsvlqLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQ 218
Cdd:TIGR00618  627 LQDVRLHLQQCSQELALKLTALHALQLTLTQER-----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1039793568  219 KDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLAHCMK 263
Cdd:TIGR00618  702 CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
122-253 1.33e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 122 EEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 201
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039793568 202 LEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQ 253
Cdd:COG4372   124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 70-323 1.39e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.09  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568   70 EEQLLEQQEHLEKEMEEAKKMISGL----QALllngslpeDEQ--------------ERPVALCE-PGVNPE---EQLII 127
Cdd:COG3096    374 AEQLAEAEARLEAAEEEVDSLKSQLadyqQAL--------DVQqtraiqyqqavqalEKARALCGlPDLTPEnaeDYLAA 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  128 IRSRLDQSVEENQDLKKEL---------------LKCK-----------QEARNLqgIKDALQQRLTQQDTSVLQLKQEL 181
Cdd:COG3096    446 FRAKEQQATEEVLELEQKLsvadaarrqfekayeLVCKiageversqawQTAREL--LRRYRSQQALAQRLQQLRAQLAE 523

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  182 LRanmdkdelhnQNVDLQRKLEernRLLGEYKKELGQK-------DRLFQQQQAKLEEALRKLSDASYQQVDLERELEQk 254
Cdd:COG3096    524 LE----------QRLRQQQNAE---RLLEEFCQRIGQQldaaeelEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ- 589

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039793568  255 dvLLAHCMKGETDEPQTSDLQlvrDALRSLRNsfsghdpqhHTIDSLE--QGISSLMERLHVVETQKKQER 323
Cdd:COG3096    590 --LRARIKELAARAPAWLAAQ---DALERLRE---------QSGEALAdsQEVTAAMQQLLEREREATVER 646
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 145-361 2.56e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 145 ELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQ 224
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 225 QQQAKLE------------------EALRKLSDASY----QQVDLERELEQKDVLLAHcmKGETDEPQTSDLQLVRDALR 282
Cdd:COG3883    97 RSGGSVSyldvllgsesfsdfldrlSALSKIADADAdlleELKADKAELEAKKAELEA--KLAELEALKAELEAAKAELE 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039793568 283 SLRNSfsghdpQHHTIDSLEQGISSLMERLHVVETQKKQERKVGGRSPRNQASSEYRASWPPNSTLPHSQSSPAVSSTC 361
Cdd:COG3883   175 AQQAE------QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 122-259 2.85e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 122 EEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELH--------- 192
Cdd:COG3883    36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgsesfs 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 193 --NQNVDLQRKLEERNR-LLGEYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 259
Cdd:COG3883   116 dfLDRLSALSKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
70-253 3.27e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  70 EEQLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLiiiRSRLDQsVEENQDLKKELLKC 149
Cdd:COG4717   332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL---RAALEQ-AEEYQELKEELEEL 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 150 KQEarnLQGIKDALQQRLTQQDTSvlQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKK--ELGQKDRLFQQQQ 227
Cdd:COG4717   408 EEQ---LEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELK 482

                         170       180
                  ....*....|....*....|....*.
gi 1039793568 228 AKLEEALRKLSDASYQQVDLERELEQ 253
Cdd:COG4717   483 AELRELAEEWAALKLALELLEEAREE 508
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 71-252 5.77e-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: 5.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  71 EQLLEQQEHLEKEMEEAKKMISGLQalllngslpEDEQERPVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCK 150
Cdd:pfam10174 404 ENLQEQLRDKDKQLAGLKERVKSLQ---------TDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLK 474

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568 151 QEARNLQGIKDALQQRLTQQDTSVLQLKQEL--LRANMDKDELHNQNVD--LQRKLEERNRLLGEYKK-----ELGQKDR 221
Cdd:pfam10174 475 KENKDLKEKVSALQPELTEKESSLIDLKEHAssLASSGLKKDSKLKSLEiaVEQKKEECSKLENQLKKahnaeEAVRTNP 554

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039793568 222 LFQQQQAKLE-EALRKLSDASYQQVDLERELE 252
Cdd:pfam10174 555 EINDRIRLLEqEVARYKEESGKAQAEVERLLG 586
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 128-312 6.15e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.05  E-value: 6.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  128 IRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANmdkDELHNQNVDLQRKLEERNR 207
Cdd:pfam12128  602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLF---DEKQSEKDKKNKALAERKD 678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  208 LLGEYKKEL-GQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELE-QKDVLLAHCMKGETDEPQTSDLQLvrDALRSLR 285
Cdd:pfam12128  679 SANERLNSLeAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEgALDAQLALLKAAIAARRSGAKAEL--KALETWY 756

                          170       180
                   ....*....|....*....|....*...
gi 1039793568  286 -NSFSGHDPQHHTIDSLEQGISSLMERL 312
Cdd:pfam12128  757 kRDLASLGVDPDVIAKLKREIRTLERKI 784
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 143-324 6.16e-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: 6.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  143 KKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDE----LHNQNVDLQRKLEERNRLLGEY---KKE 215
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEAEVEQLEERIaqlSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793568  216 LGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQkdvllahcMKGETDEpQTSDLQLVRDALRSLRNSFsghDPQH 295
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ--------LKEELKA-LREALDELRAELTLLNEEA---ANLR 823

                          170       180
                   ....*....|....*....|....*....
gi 1039793568  296 HTIDSLEQGISSLMERLHVVETQKKQERK 324
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSE 852
 
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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