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Conserved domains on  [gi|239787094|ref|NP_001154999|]
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TNFAIP3-interacting protein 2 isoform 2 [Homo sapiens]

Protein Classification

SMC_prok_B and EABR domain-containing protein( domain architecture ID 13530685)

SMC_prok_B and EABR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EABR pfam12180
TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is ...
 107-139 3.65e-09

TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. This domain is the active domain of CEP55. CEP55 is a protein involved in cytokinesis, specifically in abscission of the plasma membrane at the midbody. To perform this function, CEP55 complexes with ESCRT-I (by a Proline rich sequence in its TSG101 domain) and ALIX. This is the domain on CEP55 which binds to both TSG101 and ALIX. It also acts as a hinge between the N and C termini. This domain is called EABR.


:

Pssm-ID: 463486 [Multi-domain]  Cd Length: 34  Bit Score: 51.34  E-value: 3.65e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 239787094  107 KQKVTHVEDLNAKWQRYNASRDEYVRGLHAQLR 139
Cdd:pfam12180   1 KQQVADVLELNQQWQVYDQSREEYVRGLLARLK 33
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-263 5.59e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 5.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    13 EKEVVLLRRSMAEGERARAASDVLCRSLANETHQLRRTLTATAHMCQHLAKCLDERQHAQRNVGERSPDQS-EHTDGHTS 91
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    92 VQSVIEKLQEENRLLKQKVTHVEDLNAKWQRYNASRDEyvrgLHAQLRGLqiphepelmRKEISRLNRQLEEKINDCAEV 171
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDEL---------RAELTLLNEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094   172 KQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASLLHQVSWRQDSREPDAGRIHAGSKT 251
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909

                          250
                   ....*....|..
gi 239787094   252 AKYLAADALELM 263
Cdd:TIGR02168  910 RSELRRELEELR 921
 
Name Accession Description Interval E-value
EABR pfam12180
TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is ...
 107-139 3.65e-09

TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. This domain is the active domain of CEP55. CEP55 is a protein involved in cytokinesis, specifically in abscission of the plasma membrane at the midbody. To perform this function, CEP55 complexes with ESCRT-I (by a Proline rich sequence in its TSG101 domain) and ALIX. This is the domain on CEP55 which binds to both TSG101 and ALIX. It also acts as a hinge between the N and C termini. This domain is called EABR.


Pssm-ID: 463486 [Multi-domain]  Cd Length: 34  Bit Score: 51.34  E-value: 3.65e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 239787094  107 KQKVTHVEDLNAKWQRYNASRDEYVRGLHAQLR 139
Cdd:pfam12180   1 KQQVADVLELNQQWQVYDQSREEYVRGLLARLK 33
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-263 5.59e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 5.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    13 EKEVVLLRRSMAEGERARAASDVLCRSLANETHQLRRTLTATAHMCQHLAKCLDERQHAQRNVGERSPDQS-EHTDGHTS 91
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    92 VQSVIEKLQEENRLLKQKVTHVEDLNAKWQRYNASRDEyvrgLHAQLRGLqiphepelmRKEISRLNRQLEEKINDCAEV 171
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDEL---------RAELTLLNEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094   172 KQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASLLHQVSWRQDSREPDAGRIHAGSKT 251
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909

                          250
                   ....*....|..
gi 239787094   252 AKYLAADALELM 263
Cdd:TIGR02168  910 RSELRRELEELR 921
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
96-262 2.30e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094   96 IEKLQEENRLLKQKVTHVEDLNAKWQRYNASRDEYvrglhAQLRGLQIPHEPELMRKEISRLNRQLEEKINDCAEVKQEL 175
Cdd:COG4913   237 LERAHEALEDAREQIELLEPIRELAERYAAARERL-----AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094  176 AASRTARDAALERVQMLEQQILAYKDDFMSE-RADRERAQSRIQELEEKVASLLHQVSWRQDSREPDAGRIHAGSKTAKY 254
Cdd:COG4913   312 ERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391


                  ....*...
gi 239787094  255 LAADALEL 262
Cdd:COG4913   392 LLEALEEE 399
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 151-230 3.55e-04

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 39.20  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094  151 RKEISRLNRQL---EEKINDCAEVKQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASL 227
Cdd:pfam16516  13 KDEIDCLQAQLqaaEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYL 92


                  ...
gi 239787094  228 LHQ 230
Cdd:pfam16516  93 QRQ 95
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 95-234 5.78e-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: 41.16  E-value: 5.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    95 VIEKLQEENRLLKQKVTHVEDLNAKWQ-RYNASRDEyvrglHAQLRGLQI------PHEPELMRKEISRLNRQLEEKIND 167
Cdd:smart00787 152 NLEGLKEDYKLLMKELELLNSIKPKLRdRKDALEEE-----LRQLKQLEDeledcdPTELDRAKEKLKKLLQEIMIKVKK 226

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239787094   168 CAEVKQELAASRTArdaalerVQMLEQQILAYKDDFMSERADRERAQ----SRIQELEEKVASLLHQVSWR 234
Cdd:smart00787 227 LEELEEELQELESK-------IEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLKLLQSLTGWK 290
 
Name Accession Description Interval E-value
EABR pfam12180
TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is ...
 107-139 3.65e-09

TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. This domain is the active domain of CEP55. CEP55 is a protein involved in cytokinesis, specifically in abscission of the plasma membrane at the midbody. To perform this function, CEP55 complexes with ESCRT-I (by a Proline rich sequence in its TSG101 domain) and ALIX. This is the domain on CEP55 which binds to both TSG101 and ALIX. It also acts as a hinge between the N and C termini. This domain is called EABR.


Pssm-ID: 463486 [Multi-domain]  Cd Length: 34  Bit Score: 51.34  E-value: 3.65e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 239787094  107 KQKVTHVEDLNAKWQRYNASRDEYVRGLHAQLR 139
Cdd:pfam12180   1 KQQVADVLELNQQWQVYDQSREEYVRGLLARLK 33
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-263 5.59e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 5.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    13 EKEVVLLRRSMAEGERARAASDVLCRSLANETHQLRRTLTATAHMCQHLAKCLDERQHAQRNVGERSPDQS-EHTDGHTS 91
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    92 VQSVIEKLQEENRLLKQKVTHVEDLNAKWQRYNASRDEyvrgLHAQLRGLqiphepelmRKEISRLNRQLEEKINDCAEV 171
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDEL---------RAELTLLNEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094   172 KQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASLLHQVSWRQDSREPDAGRIHAGSKT 251
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909

                          250
                   ....*....|..
gi 239787094   252 AKYLAADALELM 263
Cdd:TIGR02168  910 RSELRRELEELR 921
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-262 1.40e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094   151 RKEISRLNRQLEEKINDCAEVKQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASLLHQ 230
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110
                   ....*....|....*....|....*....|..
gi 239787094   231 VSWRQDSREPDAGRIHAGSKTAKYLAADALEL 262
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
96-262 2.30e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094   96 IEKLQEENRLLKQKVTHVEDLNAKWQRYNASRDEYvrglhAQLRGLQIPHEPELMRKEISRLNRQLEEKINDCAEVKQEL 175
Cdd:COG4913   237 LERAHEALEDAREQIELLEPIRELAERYAAARERL-----AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094  176 AASRTARDAALERVQMLEQQILAYKDDFMSE-RADRERAQSRIQELEEKVASLLHQVSWRQDSREPDAGRIHAGSKTAKY 254
Cdd:COG4913   312 ERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391


                  ....*...
gi 239787094  255 LAADALEL 262
Cdd:COG4913   392 LLEALEEE 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-232 8.70e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 8.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094     5 LSQPQHEREKEvvlLRRSMAEGERARAASDVLCRSLANETHQLRRTLTATAHMCQHLAKCLDERQHAQRNVGERSPDQSE 84
Cdd:TIGR02168  724 LSRQISALRKD---LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    85 HTDGHTSVQSVIEKLQEENRLLKQKVTHVEDLNAKWQRYNASRDEYVRGLHAQLRGLQipHEPELMRKEISRLNRQLEEK 164
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA--AEIEELEELIEELESELEAL 878

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239787094   165 INDCAEVKQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASLLHQVS 232
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 98-227 3.11e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094  98 KLQEENRLLKQKVT--HVEDLNAKWQRYNASRDEY---VRGLHAQLRGLQipHEPELMRKEISRLNRQLEEKINDCAEVK 172
Cdd:COG1196  217 ELKEELKELEAELLllKLRELEAELEELEAELEELeaeLEELEAELAELE--AELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 239787094 173 QELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASL 227
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 151-230 3.55e-04

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 39.20  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094  151 RKEISRLNRQL---EEKINDCAEVKQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASL 227
Cdd:pfam16516  13 KDEIDCLQAQLqaaEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYL 92


                  ...
gi 239787094  228 LHQ 230
Cdd:pfam16516  93 QRQ 95
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 95-234 5.78e-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: 41.16  E-value: 5.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    95 VIEKLQEENRLLKQKVTHVEDLNAKWQ-RYNASRDEyvrglHAQLRGLQI------PHEPELMRKEISRLNRQLEEKIND 167
Cdd:smart00787 152 NLEGLKEDYKLLMKELELLNSIKPKLRdRKDALEEE-----LRQLKQLEDeledcdPTELDRAKEKLKKLLQEIMIKVKK 226

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239787094   168 CAEVKQELAASRTArdaalerVQMLEQQILAYKDDFMSERADRERAQ----SRIQELEEKVASLLHQVSWR 234
Cdd:smart00787 227 LEELEEELQELESK-------IEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLKLLQSLTGWK 290
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 91-238 9.18e-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: 41.21  E-value: 9.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    91 SVQSVIEKLQEENRLLKQKVTHVEdlnakwQRYNASRDEyVRGLHAQLRGLQipHEPELMRKEISRLNRQLEEKINDCAE 170
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIE------NRLDELSQE-LSDASRKIGEIE--KEIEQLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239787094   171 VKQELAASRTARDAALERVQMLEQQILAYKDDFmsERADRERAQSRIQELEEKVASLLHQVSwRQDSR 238
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVS-RIEAR 813
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 38-228 1.07e-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: 40.81  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094    38 RSLANETHQLRRTLTATAHMCQHLAKCLDERQHaqrnvgerspDQSEHTDGHTSVQSVIEKLQEENRLLKQKVthvEDLN 117
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEE----------KLEELRLEVSELEEEIEELQKELYALANEI---SRLE 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094   118 AKWQRYNASRDEYVRGL-HAQLRGLQIPHEPELMRKEISRLNRQLEEKINDCAEVKQELAASRTARDAALERVQMLEQQI 196
Cdd:TIGR02168  302 QQKQILRERLANLERQLeELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 239787094   197 LAYKDDFMSERADR--------------ERAQSRIQELEEKVASLL 228
Cdd:TIGR02168  382 ETLRSKVAQLELQIaslnneierlearlERLEDRRERLQQEIEELL 427
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
96-227 6.80e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787094  96 IEKLQEENRLLKQKVTHVEDLNAKWQRYNASRD--EYVRGLHAQLRGLQIPHEP-ELMRKEISRLNRQLEEKINDCAEVK 172
Cdd:COG4717  104 LEELEAELEELREELEKLEKLLQLLPLYQELEAleAELAELPERLEELEERLEElRELEEELEELEAELAELQEELEELL 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 239787094 173 QEL-AASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASL 227
Cdd:COG4717  184 EQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 151-228 6.81e-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: 37.82  E-value: 6.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239787094 151 RKEISRLNRQLEEKINDCAEVKQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASLL 228
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
 
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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