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Conserved domains on  [gi|771916200|ref|NP_571068|]
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crestin [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 81-220 2.31e-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: 53.92  E-value: 2.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    81 DRHSAQLQHKLTHVQSRINQLELEAQE----------RPEQPDETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANK 150
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDasrkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 771916200   151 LEY----IEQLLEEVNA-DSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELKHAYELTHNEKAE 220
Cdd:TIGR02169  767 IEEleedLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 81-220 2.31e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 2.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    81 DRHSAQLQHKLTHVQSRINQLELEAQE----------RPEQPDETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANK 150
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDasrkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 771916200   151 LEY----IEQLLEEVNA-DSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELKHAYELTHNEKAE 220
Cdd:TIGR02169  767 IEEleedLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 114-199 8.40e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 8.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200 114 ETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIKALETHLSEARHEVRRLTQQL 193
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99


                 ....*.
gi 771916200 194 DYIKEE 199
Cdd:COG4942  100 EAQKEE 105
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
97-194 3.22e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  97 RINQLELEAQERPEQPDETD---QAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIK 173
Cdd:PRK02224 350 DADDLEERAEELREEAAELEselEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429

                         90       100
                 ....*....|....*....|.
gi 771916200 174 ALETHLSEARHEVRRLTQQLD 194
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLE 450
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 39-201 1.11e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 44.62  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    39 DQLDENLNsLMKQDpsksYNH--KDLAKITGTLshvliatLKLSDRHSAqLQHKLTHVQsrinQLELEAQERPeqPDETD 116
Cdd:smart00787 147 EGLDENLE-GLKED----YKLlmKELELLNSIK-------PKLRDRKDA-LEEELRQLK----QLEDELEDCD--PTELD 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200   117 qAAKEEIDKLhetlaatTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIKALETHLSEARH----EVRRLTQQ 192
Cdd:smart00787 208 -RAKEKLKKL-------LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGftfkEIEKLKEQ 279


                   ....*....
gi 771916200   193 LDYIKEESN 201
Cdd:smart00787 280 LKLLQSLTG 288
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 23-197 6.06e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.45  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200   23 DSLLPKAAETLQHLTQDQLDENLNSLMKQDPSKSYNHKDLAKITGTLSHVliatlklsDRHSAQLQHKLTHVQSR--INQ 100
Cdd:pfam06160 254 ENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHA--------EEQNKELKEELERVQQSytLNE 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  101 LELEAQerpeqpdetdQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIKALETHLS 180
Cdd:pfam06160 326 NELERV----------RGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDEL 395

                         170
                  ....*....|....*..
gi 771916200  181 EARHEVRRLTQQLDYIK 197
Cdd:pfam06160 396 EAREKLDEFKLELREIK 412
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 81-220 2.31e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 2.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    81 DRHSAQLQHKLTHVQSRINQLELEAQE----------RPEQPDETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANK 150
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDasrkigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 771916200   151 LEY----IEQLLEEVNA-DSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELKHAYELTHNEKAE 220
Cdd:TIGR02169  767 IEEleedLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 85-210 6.07e-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: 52.76  E-value: 6.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    85 AQLQHKLTHVQSRINQLELEAQE-RPEQPDETDQ--AAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEV 161
Cdd:TIGR02169  360 AELKEELEDLRAELEEVDKEFAEtRDELKDYREKleKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 771916200   162 NADSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELKHA 210
Cdd:TIGR02169  440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-210 2.81e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    85 AQLQHKLTHVQSRINQLELE---AQERPEQPDETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEV 161
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 771916200   162 NADSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELKHA 210
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 114-199 8.40e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 8.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200 114 ETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIKALETHLSEARHEVRRLTQQL 193
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99


                 ....*.
gi 771916200 194 DYIKEE 199
Cdd:COG4942  100 EAQKEE 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 85-212 1.38e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  85 AQLQHKLTHVQSRINQLELE----AQERPEQpDETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEE 160
Cdd:COG1196  298 ARLEQDIARLEERRRELEERleelEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 771916200 161 VNADSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELKHAYE 212
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 90-210 2.53e-05

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: 46.07  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  90 KLTHVQSRINQLELEAQERPEQPDETDQ---AAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLL------EE 160
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKE 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 771916200 161 VNADSKDKDS---RIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELKHA 210
Cdd:COG1579   91 YEALQKEIESlkrRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
85-199 3.07e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  85 AQLQHKLTHVQSRINQLELEAQERPEQpdetDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNAD 164
Cdd:COG4372   69 EQARSELEQLEEELEELNEQLQAAQAE----LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE 144

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 771916200 165 SKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEE 199
Cdd:COG4372  145 IAEREEELKELEEQLESLQEELAALEQELQALSEA 179
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
97-194 3.22e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  97 RINQLELEAQERPEQPDETD---QAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIK 173
Cdd:PRK02224 350 DADDLEERAEELREEAAELEselEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429

                         90       100
                 ....*....|....*....|.
gi 771916200 174 ALETHLSEARHEVRRLTQQLD 194
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLE 450
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
86-191 8.84e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 8.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  86 QLQHKLTHVQSRINQLELEAQERPEQPDETD------------QAAKEEIDKLHETLAATTQEMEQAKAEHAdVANKLEY 153
Cdd:COG4717  399 ELKEELEELEEQLEELLGELEELLEALDEEEleeeleeleeelEELEEELEELREELAELEAELEQLEEDGE-LAELLQE 477

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 771916200 154 IEQLLEEVNADSKDkDSRIKALETHLSEARHEVRRLTQ 191
Cdd:COG4717  478 LEELKAELRELAEE-WAALKLALELLEEAREEYREERL 514
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 39-201 1.11e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 44.62  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    39 DQLDENLNsLMKQDpsksYNH--KDLAKITGTLshvliatLKLSDRHSAqLQHKLTHVQsrinQLELEAQERPeqPDETD 116
Cdd:smart00787 147 EGLDENLE-GLKED----YKLlmKELELLNSIK-------PKLRDRKDA-LEEELRQLK----QLEDELEDCD--PTELD 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200   117 qAAKEEIDKLhetlaatTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIKALETHLSEARH----EVRRLTQQ 192
Cdd:smart00787 208 -RAKEKLKKL-------LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGftfkEIEKLKEQ 279


                   ....*....
gi 771916200   193 LDYIKEESN 201
Cdd:smart00787 280 LKLLQSLTG 288
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
85-206 2.32e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  85 AQLQHKLTHVQSRINQLELEAQERpeqpdetdQAAKEEIDKLHETLAATTQEMEQAKAEHAdvANKLEYIEQLLEEVNad 164
Cdd:COG4717  135 EALEAELAELPERLEELEERLEEL--------RELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELE-- 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 771916200 165 skDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDE 206
Cdd:COG4717  203 --ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 86-220 3.36e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  86 QLQHKLTHVQSRINQLELEAQErpeqpdETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADS 165
Cdd:COG1196  217 ELKEELKELEAELLLLKLRELE------AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 771916200 166 KDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELKHAYELTHNEKAE 220
Cdd:COG1196  291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 77-214 3.63e-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: 43.51  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    77 LKLSDRHSAQLQHKLTHVQSRINQLELEAQERPEQPDETDQ---AAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEY 153
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELIEELESELEALLNERASLEEALAL 891

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 771916200   154 IEQLLEEVNADSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELKHAYELT 214
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 26-217 4.03e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.29  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  26 LPKAAETLQHLtQDQLDENLNSLMKQDPSKSYNHKDLAKITGTLSHVLiatlklsdRHSAQLQHKLTHVQS--RINQLEL 103
Cdd:PRK04778 277 LDEAEEKNEEI-QERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAK--------EQNKELKEEIDRVKQsyTLNESEL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200 104 EAQerpeqpdetdQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIKALETHLSEAR 183
Cdd:PRK04778 348 ESV----------RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR 417

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 771916200 184 HEVRRLTQQLDYIK---EESN--SIKDELKHAYELTHNE 217
Cdd:PRK04778 418 EKLERYRNKLHEIKrylEKSNlpGLPEDYLEMFFEVSDE 456
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 28-207 4.13e-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: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    28 KAAETLQHLTQDQLDENLNSLMKQDPSKSYNHKDLAKITGTLSHVLIATLKLSDRHSAQLQHKLTHVQSRINQLE---LE 104
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLErsiAE 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200   105 AQERPEQPDETDQAAKEEIDKLHETLAATTQEMEQ-----------------------------------AKAEHADVAN 149
Cdd:TIGR02169  313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklteeyaelkeeledlraeleevdkefaeTRDELKDYRE 392

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 771916200   150 KLE---------------------YIEQLLEEVNADSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDEL 207
Cdd:TIGR02169  393 KLEklkreinelkreldrlqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
85-194 9.46e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200   85 AQLQHKLTHVQSRINQLELEAQERPEQPDETDQAAK---EEID--KLHETLAATTQEMEQAKAEHADVAN---KLEYIEQ 156
Cdd:COG4913   620 AELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDvaSAEREIAELEAELERLDASSDDLAAleeQLEELEA 699

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 771916200  157 LLEEVNADSKDKDSRIKALETHLSEARHEVRRLTQQLD 194
Cdd:COG4913   700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 91-187 2.50e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  91 LTHVQSRINQLELEAQERPEqpdETDQAAKEEIDKLHETLAATTQEMEQAKAEHA---DVANKLEYIEQLLEEVNADSKD 167
Cdd:COG0542  413 LDELERRLEQLEIEKEALKK---EQDEASFERLAELRDELAELEEELEALKARWEaekELIEEIQELKEELEQRYGKIPE 489

                         90       100
                 ....*....|....*....|
gi 771916200 168 KDSRIKALETHLSEARHEVR 187
Cdd:COG0542  490 LEKELAELEEELAELAPLLR 509
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
113-208 2.60e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200 113 DETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIKALETHLSEARHEVRRLTQQ 192
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                         90
                 ....*....|....*.
gi 771916200 193 LDYIKEESNSIKDELK 208
Cdd:COG4372  110 AEELQEELEELQKERQ 125
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 117-220 3.49e-03

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: 40.44  E-value: 3.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200   117 QAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDK-DSRIKALETHLSEARHEVRRLTQQLDY 195
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAE 312

                           90       100
                   ....*....|....*....|....*
gi 771916200   196 IKEESNSIKDELKHAYELTHNEKAE 220
Cdd:TIGR02169  313 KERELEDAEERLAKLEAEIDKLLAE 337
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 86-161 4.47e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 36.49  E-value: 4.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 771916200  86 QLQHKLTHVQSRINQLELEAqerpEQPDETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEV 161
Cdd:COG3074    8 ELEAKVQQAVDTIELLQMEV----EELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSLLGKIDEV 79
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
85-192 5.83e-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: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200   85 AQLQHKLTHVQSRINQLEL------EAQERPEQPDETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLE------ 152
Cdd:COG4913   664 ASAEREIAELEAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaaedla 743

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 771916200  153 ------YIEQLLEEVNAD------SKDKDSRIKALETHLSEARHEVRRLTQQ 192
Cdd:COG4913   744 rlelraLLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAMRA 795
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 23-197 6.06e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.45  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200   23 DSLLPKAAETLQHLTQDQLDENLNSLMKQDPSKSYNHKDLAKITGTLSHVliatlklsDRHSAQLQHKLTHVQSR--INQ 100
Cdd:pfam06160 254 ENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHA--------EEQNKELKEELERVQQSytLNE 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200  101 LELEAQerpeqpdetdQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIKALETHLS 180
Cdd:pfam06160 326 NELERV----------RGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDEL 395

                         170
                  ....*....|....*..
gi 771916200  181 EARHEVRRLTQQLDYIK 197
Cdd:pfam06160 396 EAREKLDEFKLELREIK 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-213 6.08e-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: 39.65  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    85 AQLQHKLTHVQSRINQLELE----AQERPEQPDETDQAAKEEidkLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEE 160
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRrerlQQEIEELLKKLEEAELKE---LQAELEELEEELEELQEELERLEEALEELREELEE 472

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 771916200   161 VNadskdkdSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELKHAYEL 213
Cdd:TIGR02168  473 AE-------QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
86-204 6.08e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 6.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200   86 QLQHKLTHVQSRINQLELEAQERPEQPDETDQ---AAKEEIDKLHE--------TLAATTQEMEQAKAEHADVANKLEYI 154
Cdd:COG4913   285 FAQRRLELLEAELEELRAELARLEAELERLEArldALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARL 364

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 771916200  155 EQLL------------------EEVNADSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIK 204
Cdd:COG4913   365 EALLaalglplpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 104-173 7.30e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 7.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200 104 EAQERPEQPDETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIK 173
Cdd:COG3883   20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
117-208 8.01e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200 117 QAAKEEIDKLHETLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIKALETHLSEARHEVRRLTQQLDYI 196
Cdd:COG4372   48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127

                         90
                 ....*....|..
gi 771916200 197 KEESNSIKDELK 208
Cdd:COG4372  128 EQQRKQLEAQIA 139
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 129-210 8.89e-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: 8.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200 129 TLAATTQEMEQAKAEHADVANKLEYIEQLLEEVNADSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKDELK 208
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93


                 ..
gi 771916200 209 HA 210
Cdd:COG4942   94 EL 95
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 75-205 9.87e-03

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: 38.90  E-value: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771916200    75 ATLKLSDRHSAQLQHKLTHVQSRINQLELEA---QERPEQPDETDQAAKEEIDKLHETLAATTQEMEQAKAEHADVANKL 151
Cdd:TIGR02169  378 KEFAETRDELKDYREKLEKLKREINELKRELdrlQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 771916200   152 EYIEQLLEEVNADSKDKDSRIKALETHLSEARHEVRRLTQQLDYIKEESNSIKD 205
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
 
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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