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Conserved domains on  [gi|564366104|ref|XP_006244094|]
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5-azacytidine-induced protein 2 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TBD super family cl15118
TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, ...
227-277 4.23e-13

TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, has been found to be essential for poly(I:C)-induced IRF activation. The domain is found in SINTBAD, TANK and NAP1 protein. This domain is predicted to form an a-helix with residues essential for kinase binding clustering on one side.


The actual alignment was detected with superfamily member pfam12845:

Pssm-ID: 463729 [Multi-domain]  Cd Length: 56  Bit Score: 63.61  E-value: 4.23e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564366104  227 HHSDHMQHAYWELRREMANLHLVTRVQAELLRQLK----TAAAGKACTQVGCVED 277
Cdd:pfam12845   2 DSSVNLEKAYWELKEEMHRLCMLTRVQAEHLRKLKieqeTAGEIQFSMPIQCTDD 56
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
13-255 4.71e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.95  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   13 NHEKAHKREAVTPLSAYPGDESVASHFALVTAYEDIKKRLKDSEKENSFLKKRIRALEEKLVGARVEEETSsvgREQVNK 92
Cdd:pfam05483 266 SRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ---MEELNK 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   93 AYHAYREVCIDRDNLKSRLEKISK-------DNSESLRALTEQLQCKEVELLQL-----RTEVETQQVMRNLNPPSS--- 157
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRteqqrleKNEDQLKIITMELQKKSSELEEMtkfknNKEVELEELKKILAEDEKlld 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  158 -NWEVEKLSCDLKihGLEQELELL----RKECSDLRTELQKarqTGPSQEDILQDRDVIRPSLPREEHVPHQGPHHSDHM 232
Cdd:pfam05483 423 eKKQFEKIAEELK--GKEQELIFLlqarEKEIHDLEIQLTA---IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL 497
                         250       260
                  ....*....|....*....|...
gi 564366104  233 QHAYWELRREMANLHLVTRVQAE 255
Cdd:pfam05483 498 LLENKELTQEASDMTLELKKHQE 520
 
Name Accession Description Interval E-value
TBD pfam12845
TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, ...
227-277 4.23e-13

TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, has been found to be essential for poly(I:C)-induced IRF activation. The domain is found in SINTBAD, TANK and NAP1 protein. This domain is predicted to form an a-helix with residues essential for kinase binding clustering on one side.


Pssm-ID: 463729 [Multi-domain]  Cd Length: 56  Bit Score: 63.61  E-value: 4.23e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564366104  227 HHSDHMQHAYWELRREMANLHLVTRVQAELLRQLK----TAAAGKACTQVGCVED 277
Cdd:pfam12845   2 DSSVNLEKAYWELKEEMHRLCMLTRVQAEHLRKLKieqeTAGEIQFSMPIQCTDD 56
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
13-255 4.71e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.95  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   13 NHEKAHKREAVTPLSAYPGDESVASHFALVTAYEDIKKRLKDSEKENSFLKKRIRALEEKLVGARVEEETSsvgREQVNK 92
Cdd:pfam05483 266 SRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ---MEELNK 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   93 AYHAYREVCIDRDNLKSRLEKISK-------DNSESLRALTEQLQCKEVELLQL-----RTEVETQQVMRNLNPPSS--- 157
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRteqqrleKNEDQLKIITMELQKKSSELEEMtkfknNKEVELEELKKILAEDEKlld 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  158 -NWEVEKLSCDLKihGLEQELELL----RKECSDLRTELQKarqTGPSQEDILQDRDVIRPSLPREEHVPHQGPHHSDHM 232
Cdd:pfam05483 423 eKKQFEKIAEELK--GKEQELIFLlqarEKEIHDLEIQLTA---IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL 497
                         250       260
                  ....*....|....*....|...
gi 564366104  233 QHAYWELRREMANLHLVTRVQAE 255
Cdd:pfam05483 498 LLENKELTQEASDMTLELKKHQE 520
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
46-195 1.06e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  46 EDIKKRLKDSEKENSFLKKRIRALEEKLVGAR--------------VEEETSSVGREQVNKAYHAYREVCIDRDNLKSRL 111
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaeqlkeLEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104 112 EKISKDNSE------SLRALTEQLQCKEVELLQLRTEV---------ETQQVMRNLNPPSSNWeveklscdLKIHGLEQE 176
Cdd:PRK03918 542 KSLKKELEKleelkkKLAELEKKLDELEEELAELLKELeelgfesveELEERLKELEPFYNEY--------LELKDAEKE 613
                        170
                 ....*....|....*....
gi 564366104 177 LELLRKECSDLRTELQKAR 195
Cdd:PRK03918 614 LEREEKELKKLEEELDKAF 632
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
48-209 6.96e-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: 41.98  E-value: 6.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104    48 IKKRLKDSEKENSFLKKRIRALEEKLVGArveeetssvgREQVNKAYHAYREVCIDR-DNLKSRLEKISKDNSESLRALT 126
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKL----------EEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIE 818
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   127 EQLQCKEVELLQLRTEVETQQVMRNLnppssnweveklsCDLKIHGLEQELELLRKECSDLRTELQKA----RQTGPSQE 202
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRID-------------LKEQIKSIEKEIENLNGKKEELEEELEELeaalRDLESRLG 885

                   ....*..
gi 564366104   203 DILQDRD 209
Cdd:TIGR02169  886 DLKKERD 892
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-203 8.26e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 8.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  50 KRLKDSEKENSFLKKRIRALEEKLVGARVEEETSSVGREQVNKAyHAYREVCIDRDNLKSRLEKIS------KDNSESLR 123
Cdd:COG4717   81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELPerleelEERLEELR 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104 124 ALTEQLQCKEVELLQLRTEVETQqvmRNLNPPSSNWEVEKLSCDL-----KIHGLEQELELLRKECSDLRTELQKARQTG 198
Cdd:COG4717  160 ELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELeelqqRLAELEEELEEAQEELEELEEELEQLENEL 236

                 ....*
gi 564366104 199 PSQED 203
Cdd:COG4717  237 EAAAL 241
 
Name Accession Description Interval E-value
TBD pfam12845
TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, ...
227-277 4.23e-13

TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, has been found to be essential for poly(I:C)-induced IRF activation. The domain is found in SINTBAD, TANK and NAP1 protein. This domain is predicted to form an a-helix with residues essential for kinase binding clustering on one side.


Pssm-ID: 463729 [Multi-domain]  Cd Length: 56  Bit Score: 63.61  E-value: 4.23e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564366104  227 HHSDHMQHAYWELRREMANLHLVTRVQAELLRQLK----TAAAGKACTQVGCVED 277
Cdd:pfam12845   2 DSSVNLEKAYWELKEEMHRLCMLTRVQAEHLRKLKieqeTAGEIQFSMPIQCTDD 56
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
13-255 4.71e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.95  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   13 NHEKAHKREAVTPLSAYPGDESVASHFALVTAYEDIKKRLKDSEKENSFLKKRIRALEEKLVGARVEEETSsvgREQVNK 92
Cdd:pfam05483 266 SRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ---MEELNK 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   93 AYHAYREVCIDRDNLKSRLEKISK-------DNSESLRALTEQLQCKEVELLQL-----RTEVETQQVMRNLNPPSS--- 157
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRteqqrleKNEDQLKIITMELQKKSSELEEMtkfknNKEVELEELKKILAEDEKlld 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  158 -NWEVEKLSCDLKihGLEQELELL----RKECSDLRTELQKarqTGPSQEDILQDRDVIRPSLPREEHVPHQGPHHSDHM 232
Cdd:pfam05483 423 eKKQFEKIAEELK--GKEQELIFLlqarEKEIHDLEIQLTA---IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL 497
                         250       260
                  ....*....|....*....|...
gi 564366104  233 QHAYWELRREMANLHLVTRVQAE 255
Cdd:pfam05483 498 LLENKELTQEASDMTLELKKHQE 520
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
46-195 1.06e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  46 EDIKKRLKDSEKENSFLKKRIRALEEKLVGAR--------------VEEETSSVGREQVNKAYHAYREVCIDRDNLKSRL 111
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelaeqlkeLEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104 112 EKISKDNSE------SLRALTEQLQCKEVELLQLRTEV---------ETQQVMRNLNPPSSNWeveklscdLKIHGLEQE 176
Cdd:PRK03918 542 KSLKKELEKleelkkKLAELEKKLDELEEELAELLKELeelgfesveELEERLKELEPFYNEY--------LELKDAEKE 613
                        170
                 ....*....|....*....
gi 564366104 177 LELLRKECSDLRTELQKAR 195
Cdd:PRK03918 614 LEREEKELKKLEEELDKAF 632
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
48-209 6.96e-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: 41.98  E-value: 6.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104    48 IKKRLKDSEKENSFLKKRIRALEEKLVGArveeetssvgREQVNKAYHAYREVCIDR-DNLKSRLEKISKDNSESLRALT 126
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKL----------EEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIE 818
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   127 EQLQCKEVELLQLRTEVETQQVMRNLnppssnweveklsCDLKIHGLEQELELLRKECSDLRTELQKA----RQTGPSQE 202
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRID-------------LKEQIKSIEKEIENLNGKKEELEEELEELeaalRDLESRLG 885

                   ....*..
gi 564366104   203 DILQDRD 209
Cdd:TIGR02169  886 DLKKERD 892
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
46-205 8.00e-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: 41.97  E-value: 8.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104    46 EDIKKRLKDSEKENSFLKKRIRALEEKLVGARVEEETSSVGREQVNKAYHAYREVCIDRDNLKSRLEKISKDNS---ESL 122
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeiEEL 864
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   123 RALTEQLQCKEVELLQLRTEVETQQVMRNLNPPSSNWEVEKLscDLKIHGLEQELELLRKECSDLRTELQKARQTGPSQE 202
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELREL--ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942

                   ...
gi 564366104   203 DIL 205
Cdd:TIGR02168  943 ERL 945
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-203 8.26e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 8.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  50 KRLKDSEKENSFLKKRIRALEEKLVGARVEEETSSVGREQVNKAyHAYREVCIDRDNLKSRLEKIS------KDNSESLR 123
Cdd:COG4717   81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELPerleelEERLEELR 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104 124 ALTEQLQCKEVELLQLRTEVETQqvmRNLNPPSSNWEVEKLSCDL-----KIHGLEQELELLRKECSDLRTELQKARQTG 198
Cdd:COG4717  160 ELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELeelqqRLAELEEELEEAQEELEELEEELEQLENEL 236

                 ....*
gi 564366104 199 PSQED 203
Cdd:COG4717  237 EAAAL 241
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
40-212 1.49e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  40 ALVTAY--EDIKKRLKDSEKENSFLKKRIRALEEKLVGARVE-------------EETSSVGREQVNKAYHAYREVCIDR 104
Cdd:COG3206  156 ALAEAYleQNLELRREEARKALEFLEEQLPELRKELEEAEAAleefrqknglvdlSEEAKLLLQQLSELESQLAEARAEL 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104 105 DNLKSRLEKISKD------------NSESLRALTEQLQCKEVELLQLRTE--------VETQQVMRNLNpPSSNWEVEKL 164
Cdd:COG3206  236 AEAEARLAALRAQlgsgpdalpellQSPVIQQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALR-AQLQQEAQRI 314
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564366104 165 SCDLK--IHGLEQELELLRKECSDLRTELQKARQTGPSQEDILQDRDVIR 212
Cdd:COG3206  315 LASLEaeLEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAR 364
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
45-196 3.69e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  45 YEDIKKRLKDSEKENSFLKKRIRALEEKLVG---------ARVEEETSSVGR-EQVNKAYHAYREVCIDRDNLKSRLEKI 114
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIREleerieelkKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREI 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104 115 SKDNS------ESLRALTEQLQCKEVELLQLRTE-VETQQVMRNLNPPSSNWE--------VEKLSCDLK---IHGLEQE 176
Cdd:PRK03918 313 EKRLSrleeeiNGIEERIKELEEKEERLEELKKKlKELEKRLEELEERHELYEeakakkeeLERLKKRLTgltPEKLEKE 392
                        170       180
                 ....*....|....*....|
gi 564366104 177 LELLRKECSDLRTELQKARQ 196
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITA 412
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
48-218 3.72e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  48 IKKRLKDSEKENSFLKKRIRALEEKLVGARVEEETSsvgREQVNKAYHAYREVCIDRDNLKSRLEKISkdNSESLRALTe 127
Cdd:COG1579   22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDL---EKEIKRLELEIEEVEARIKKYEEQLGNVR--NNKEYEALQ- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104 128 qlqcKEVELLQLR---TEVETQQVMRnlnppssnwEVEKLSCDLKihGLEQELELLRKECSDLRTELQKAR-QTGPSQED 203
Cdd:COG1579   96 ----KEIESLKRRisdLEDEILELME---------RIEELEEELA--ELEAELAELEAELEEKKAELDEELaELEAELEE 160
                        170
                 ....*....|....*
gi 564366104 204 ILQDRDVIRPSLPRE 218
Cdd:COG1579  161 LEAEREELAAKIPPE 175
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
40-191 3.85e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104  40 ALVTAYEDIKKRLKDSEKENSFLKKRIRALEEKLvgARVEEETSSVgreQVNKAYHAY-REVcidrDNLKSRLEKISKDn 118
Cdd:COG1579   42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARI--KKYEEQLGNV---RNNKEYEALqKEI----ESLKRRISDLEDE- 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564366104 119 sesLRALTEQLQCKEVELLQLRTEVETQQvmrnlnppsSNWEVEKLSCDLKIHGLEQELELLRKECSDLRTEL 191
Cdd:COG1579  112 ---ILELMERIEELEEELAELEAELAELE---------AELEEKKAELDEELAELEAELEELEAEREELAAKI 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-271 4.49e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 4.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104    32 DESVASHFALVTAYEDIKKRLKDSEKENSFLKKRIRALEEKLvgARVEEETSSVGREqvnkayhayrevcidRDNLKSRL 111
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL--ANLERQLEELEAQ---------------LEELESKL 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   112 EKIskdnSESLRALTEQLQCKEVELLQLRTEVET-QQVMRNLNPPSSNWEVEKLSCDLKIHGLEQELELLRKECSDLRTE 190
Cdd:TIGR02168  333 DEL----AEELAELEEKLEELKEELESLEAELEElEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564366104   191 L-------QKARQTGPSQEDILQ--DRDVIRPSLPREEHVPHQGPHHSDHMQHAYWELRREMAnlhLVTRVQAELLRQLK 261
Cdd:TIGR02168  409 LerledrrERLQQEIEELLKKLEeaELKELQAELEELEEELEELQEELERLEEALEELREELE---EAEQALDAAERELA 485
                          250
                   ....*....|
gi 564366104   262 TAAAGKACTQ 271
Cdd:TIGR02168  486 QLQARLDSLE 495
 
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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