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Conserved domains on  [gi|68163569|ref|NP_001020236|]
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angiopoietin-related protein 3 isoform 2 precursor [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FReD super family cl00085
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 241-311 6.06e-31

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


The actual alignment was detected with superfamily member cd00087:

Pssm-ID: 412152 [Multi-domain]  Cd Length: 215  Bit Score: 115.80  E-value: 6.06e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68163569 241 DLPADCSAIYNRGEHTSGVYTIRP-SSSQVFNVYCDTQS-GTPRTLIQHRKDGSQNFNQTWENYEKGFGRLDG 311
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPpGSNEPFQVYCDMDTdGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDG 73
GumC super family cl34566
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
90-205 1.19e-05

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


The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  90 NEIKEEEKELRRTTSKLQ--------VKNEEVKNMSL----ELNSKLESLLEEKMALQHRVRALEEQLTSLVQNPPGARE 157
Cdd:COG3206 182 EQLPELRKELEEAEAALEefrqknglVDLSEEAKLLLqqlsELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 68163569 158 HPEVTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ 309
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 241-311 6.06e-31

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 115.80  E-value: 6.06e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68163569 241 DLPADCSAIYNRGEHTSGVYTIRP-SSSQVFNVYCDTQS-GTPRTLIQHRKDGSQNFNQTWENYEKGFGRLDG 311
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPpGSNEPFQVYCDMDTdGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDG 73
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 242-311 1.31e-22

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548 [Multi-domain]  Cd Length: 212  Bit Score: 93.50  E-value: 1.31e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68163569    242 LPADCSAIYNRGEHTSGVYTIRP-SSSQVFNVYCDTQ-SGTPRTLIQHRKDGSQNFNQTWENYEKGFGRLDG 311
Cdd:smart00186   1 LPRDCSDVLQNGGKTSGLYTIYPdGSSRPLKVYCDMEtDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAG 72
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
243-309 5.50e-17

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 78.33  E-value: 5.50e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68163569   243 PADCSAIYNRGEHTSGVYTIRPS-SSQVFNVYCD-TQSGTPRTLIQHRKDGSQNFNQTWENYEKGFGRL 309
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPDgATKPFEVYCDmETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNL 70
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
90-205 1.19e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  90 NEIKEEEKELRRTTSKLQ--------VKNEEVKNMSL----ELNSKLESLLEEKMALQHRVRALEEQLTSLVQNPPGARE 157
Cdd:COG3206 182 EQLPELRKELEEAEAALEefrqknglVDLSEEAKLLLqqlsELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 68163569 158 HPEVTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ 309
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 84-242 7.12e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 7.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569    84 DLSLQTNEIKEEEKELRRTTSKLQVKNEEVKNMSLELNSKLESLLEEKMALQHRVRALEEQLTSLVQNppGAREHPEVTS 163
Cdd:pfam07888  77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQR--VLERETELER 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68163569   164 LKSFVEQQDNSIREllqsvEEQYKQLSQQHIQIKEIENQLRKTGIQEpTENSLyskprAPRTTPPLHLKEAKNIEQDDL 242
Cdd:pfam07888 155 MKERAKKAGAQRKE-----EEAERKQLQAKLQQTEEELRSLSKEFQE-LRNSL-----AQRDTQVLQLQDTITTLTQKL 222
PRK12704 PRK12704
phosphodiesterase; Provisional
 90-207 1.85e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569   90 NEIKEEEKELRRTTSKLQVKNEEVKNMSLELNSKLESLLEEKMALQHR---VRALEEQLTSLVQNppgAREHPE-VTSLk 165
Cdd:PRK12704  75 KELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKqqeLEKKEEELEELIEE---QLQELErISGL- 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 68163569  166 sfveQQDNSIRELLQSVEEQYKQlsQQHIQIKEIENQLRKTG 207
Cdd:PRK12704 151 ----TAEEAKEILLEKVEEEARH--EAAVLIKEIEEEAKEEA 186
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 91-205 8.44e-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: 38.11  E-value: 8.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569     91 EIKEEEKELRRTTSKLQVKnEEVKNMSlELNSKLESLLEEKMALQHRVRALEEQLTSLVqnppgaREHPEVTslKSFVEQ 170
Cdd:TIGR02168  217 ELKAELRELELALLVLRLE-ELREELE-ELQEELKEAEEELEELTAELQELEEKLEELR------LEVSELE--EEIEEL 286

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 68163569    171 QD------NSIRELLQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:TIGR02168  287 QKelyalaNEISRLEQQKQILRERLANLERQLEELEAQLEE 327
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 241-311 6.06e-31

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 115.80  E-value: 6.06e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68163569 241 DLPADCSAIYNRGEHTSGVYTIRP-SSSQVFNVYCDTQS-GTPRTLIQHRKDGSQNFNQTWENYEKGFGRLDG 311
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPpGSNEPFQVYCDMDTdGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDG 73
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 242-311 1.31e-22

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548 [Multi-domain]  Cd Length: 212  Bit Score: 93.50  E-value: 1.31e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68163569    242 LPADCSAIYNRGEHTSGVYTIRP-SSSQVFNVYCDTQ-SGTPRTLIQHRKDGSQNFNQTWENYEKGFGRLDG 311
Cdd:smart00186   1 LPRDCSDVLQNGGKTSGLYTIYPdGSSRPLKVYCDMEtDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAG 72
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
243-309 5.50e-17

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 78.33  E-value: 5.50e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68163569   243 PADCSAIYNRGEHTSGVYTIRPS-SSQVFNVYCD-TQSGTPRTLIQHRKDGSQNFNQTWENYEKGFGRL 309
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPDgATKPFEVYCDmETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNL 70
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
90-205 1.19e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  90 NEIKEEEKELRRTTSKLQ--------VKNEEVKNMSL----ELNSKLESLLEEKMALQHRVRALEEQLTSLVQNPPGARE 157
Cdd:COG3206 182 EQLPELRKELEEAEAALEefrqknglVDLSEEAKLLLqqlsELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 68163569 158 HPEVTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ 309
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-205 1.08e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 1.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  91 EIKEEEKELRRTTSKLQVKNEEvknmslELNSKLEsLLEEKMALQHRVRALEEQLTSLvqnpPGAREHPEVTSLKSFVEQ 170
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEE------ELRAALE-QAEEYQELKEELEELEEQLEEL----LGELEELLEALDEEELEE 432

                        90       100       110
                ....*....|....*....|....*....|....*
gi 68163569 171 QDNSIRELLQSVEEQYKQLSQqhiQIKEIENQLRK 205
Cdd:COG4717 433 ELEELEEELEELEEELEELRE---ELAELEAELEQ 464
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
87-205 4.48e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 4.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  87 LQTNEI-KEEEKELRRTTSKLQVKNEEVKNMsLELNSKLESLLEEKMALQHRVRALEEQLTSLVQNppgARE-HPEVTSL 164
Cdd:COG1340 125 QQTEVLsPEEEKELVEKIKELEKELEKAKKA-LEKNEKLKELRAELKELRKEAEEIHKKIKELAEE---AQElHEEMIEL 200

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 68163569 165 KSFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:COG1340 201 YKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 84-242 7.12e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 7.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569    84 DLSLQTNEIKEEEKELRRTTSKLQVKNEEVKNMSLELNSKLESLLEEKMALQHRVRALEEQLTSLVQNppGAREHPEVTS 163
Cdd:pfam07888  77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQR--VLERETELER 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68163569   164 LKSFVEQQDNSIREllqsvEEQYKQLSQQHIQIKEIENQLRKTGIQEpTENSLyskprAPRTTPPLHLKEAKNIEQDDL 242
Cdd:pfam07888 155 MKERAKKAGAQRKE-----EEAERKQLQAKLQQTEEELRSLSKEFQE-LRNSL-----AQRDTQVLQLQDTITTLTQKL 222
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 84-204 7.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 7.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  84 DLSLQTNEIKEEEKELRRTTSKLQVKNEEVKNMSL---ELNSKLESLLEEKMALQHRVRALEEQLTSLVQnppgarehpE 160
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLeleELELELEEAQAEEYELLAELARLEQDIARLEE---------R 310

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 68163569 161 VTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLR 204
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
87-206 8.72e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 8.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  87 LQTNEIKEEEKELRRTTSKLQvKNEEVKNMSLELNSKLESLLEEKMALQHRVRALEEQLtslvqnppgarEHPEVTSLKS 166
Cdd:COG4717  68 LNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLL-----------QLLPLYQELE 135

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 68163569 167 FVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRKT 206
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAEL 175
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
91-205 9.17e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 9.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  91 EIKEEEKELRRTTSKLQVKNEEVKNmsleLNSKLESLLEEKMALQHRVRALEEQLTSLVQNPPGAREhpevtSLKSfVEQ 170
Cdd:COG4372  39 ELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-----ELES-LQE 108

                        90       100       110
                ....*....|....*....|....*....|....*
gi 68163569 171 QDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143
PRK12704 PRK12704
phosphodiesterase; Provisional
 90-207 1.85e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569   90 NEIKEEEKELRRTTSKLQVKNEEVKNMSLELNSKLESLLEEKMALQHR---VRALEEQLTSLVQNppgAREHPE-VTSLk 165
Cdd:PRK12704  75 KELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKqqeLEKKEEELEELIEE---QLQELErISGL- 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 68163569  166 sfveQQDNSIRELLQSVEEQYKQlsQQHIQIKEIENQLRKTG 207
Cdd:PRK12704 151 ----TAEEAKEILLEKVEEEARH--EAAVLIKEIEEEAKEEA 186
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 67-205 2.21e-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: 39.36  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  67 QINDIFQKLNIFDQcfyDLSLQTNEIKEEEKELRRTTSKLQVKNEEVKNM-----SLELNSKLESLLEEK---------M 132
Cdd:COG4942  63 RIAALARRIRALEQ---ELAALEAELAELEKEIAELRAELEAQKEELAELlralyRLGRQPPLALLLSPEdfldavrrlQ 139

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68163569 133 ALQHRVRALEEQLTSLvqnppgAREHPEVTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:COG4942 140 YLKYLAPARREQAEEL------RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 84-206 2.73e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 2.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  84 DLSLQTNEIKEEEKELRRTTSKLQVKNEEVKNMSLELNSKLESLLEEKMALQHRVRALEEQLTSLVQNppgAREHPEVTS 163
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA---LRAAAELAA 400

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 68163569 164 LKSFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRKT 206
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 85-205 3.88e-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: 39.17  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569   85 LSLQTNEIKEEEKELRRTTSKLQVKNEEVKNmSLELNSKLE---SLLEEKmALQHRVRALEEQLTSLVQNppgarehpev 161
Cdd:COG3096  841 LRQRRSELERELAQHRAQEQQLRQQLDQLKE-QLQLLNKLLpqaNLLADE-TLADRLEELREELDAAQEA---------- 908

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 68163569  162 tslKSFVEQQDNSIREL------LQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:COG3096  909 ---QAFIQQHGKALAQLeplvavLQSDPEQFEQLQADYLQAKEQQRRLKQ 955
mukB PRK04863
chromosome partition protein MukB;
84-205 4.95e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.78  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569    84 DLSLQTNEIKEEEKELRRTTSKLQVKNEEVKNMSLELNsKLE---SLLEEKmALQHRVRALEEQLTSLVQNppgarehpe 160
Cdd:PRK04863  841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALN-RLLprlNLLADE-TLADRVEEIREQLDEAEEA--------- 909

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 68163569   161 vtslKSFVEQQDNSIREL------LQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:PRK04863  910 ----KRFVQQHGNALAQLepivsvLQSDPEQFEQLKQDYQQAQQTQRDAKQ 956
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
88-216 6.03e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 37.97  E-value: 6.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  88 QTNEIKEEEKELRRTTSKLQVKNEEVKNMSLELNSKLESLLEEKMALQHRVRALEEQltslvqnppgAREHPEvtSLKSF 167
Cdd:COG1340   2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE----------AQELRE--KRDEL 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 68163569 168 VEQqdnsIRELLQSVEEQYKQLSQQHIQIKEIENQLRKTGIQEPTENSL 216
Cdd:COG1340  70 NEK----VKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKL 114
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
91-205 6.79e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569   91 EIKEEEKELRRTTSKLQVKNEEVKNMS--LELNSKLESLLEEK---MALQHRVRALEEQLTSLVQNPpgarehPEVTSLK 165
Cdd:COG4913  618 ELAELEEELAEAEERLEALEAELDALQerREALQRLAEYSWDEidvASAEREIAELEAELERLDASS------DDLAALE 691

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 68163569  166 SFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:COG4913  692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 81-211 8.35e-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: 37.44  E-value: 8.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569  81 CFYDLSLQTNEIKEEEKELRRTTSKLQvkneevknmslELNSKLESLLEEKMALQHRVRALEEQLTSLVQnppgarehpE 160
Cdd:COG4942  11 LALAAAAQADAAAEAEAELEQLQQEIA-----------ELEKELAALKKEEKALLKQLAALERRIAALAR---------R 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 68163569 161 VTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRKTGIQEP 211
Cdd:COG4942  71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPP 121
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 91-205 8.44e-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: 38.11  E-value: 8.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68163569     91 EIKEEEKELRRTTSKLQVKnEEVKNMSlELNSKLESLLEEKMALQHRVRALEEQLTSLVqnppgaREHPEVTslKSFVEQ 170
Cdd:TIGR02168  217 ELKAELRELELALLVLRLE-ELREELE-ELQEELKEAEEELEELTAELQELEEKLEELR------LEVSELE--EEIEEL 286

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 68163569    171 QD------NSIRELLQSVEEQYKQLSQQHIQIKEIENQLRK 205
Cdd:TIGR02168  287 QKelyalaNEISRLEQQKQILRERLANLERQLEELEAQLEE 327
 
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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