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Conserved domains on  [gi|2030823680|ref|NP_001381613|]
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TNFAIP3-interacting protein 2 [Rattus norvegicus]

Protein Classification

kinesin family protein( domain architecture ID 13530685)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has ATPase-containing motor domain; similar to carboxy-terminal kinesins that contains a C-terminal domain responsible for the motor activity (it hydrolyzes ATP and binds microtubules)

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 ...
215-248 1.28e-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: 53.27  E-value: 1.28e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2030823680 215 KQKVIHVEDLNAKWQRYDASRDEYVKGLHAQLKR 248
Cdd:pfam12180   1 KQQVADVLELNQQWQVYDQSREEYVRGLLARLKE 34
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
73-335 3.95e-07

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: 52.37  E-value: 3.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680   73 ERFREQLRRQEDGASESQ-----LRQEVERLTECLEEKEREMQQlMSQPQHEQEKEVVLLRRSVvekEKARAASDILCRS 147
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEkalaeLRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEV---EQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  148 LTDETHQLRRTLAATAHMCQHLAKCLDERQRVQGDAGEkspAELEHTSRDTSGQSVIKKLQEENRLLKQKVIHVEDLnak 227
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ---LKEELKALREALDELRAELTLLNEEAANLRERLESL--- 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  228 wQRYDASRDEYVKGLHAQLKRRQvpLEPELMKKEISRLNRQLEEKISDCAEAKQELAAVKMARDTALERVQMLEQQILAY 307
Cdd:TIGR02168  830 -ERRIAATERRLEDLEEQIEELS--EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2030823680  308 KDDFKSERADRERA-------HSRIQELEEKVMSL 335
Cdd:TIGR02168  907 ESKRSELRRELEELreklaqlELRLEGLEVRIDNL 941
 
Name Accession Description Interval E-value
EABR pfam12180
TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is ...
215-248 1.28e-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: 53.27  E-value: 1.28e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2030823680 215 KQKVIHVEDLNAKWQRYDASRDEYVKGLHAQLKR 248
Cdd:pfam12180   1 KQQVADVLELNQQWQVYDQSREEYVRGLLARLKE 34
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
73-335 3.95e-07

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: 52.37  E-value: 3.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680   73 ERFREQLRRQEDGASESQ-----LRQEVERLTECLEEKEREMQQlMSQPQHEQEKEVVLLRRSVvekEKARAASDILCRS 147
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEkalaeLRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEV---EQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  148 LTDETHQLRRTLAATAHMCQHLAKCLDERQRVQGDAGEkspAELEHTSRDTSGQSVIKKLQEENRLLKQKVIHVEDLnak 227
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ---LKEELKALREALDELRAELTLLNEEAANLRERLESL--- 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  228 wQRYDASRDEYVKGLHAQLKRRQvpLEPELMKKEISRLNRQLEEKISDCAEAKQELAAVKMARDTALERVQMLEQQILAY 307
Cdd:TIGR02168  830 -ERRIAATERRLEDLEEQIEELS--EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2030823680  308 KDDFKSERADRERA-------HSRIQELEEKVMSL 335
Cdd:TIGR02168  907 ESKRSELRRELEELreklaqlELRLEGLEVRIDNL 941
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
65-347 5.50e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  65 VDALLDQVERFREQLRRQ--------------------EDGASESQLRQEVERLTECLEEKEREMQQLMSQpQHEQEKEV 124
Cdd:COG1196   191 LEDILGELERQLEPLERQaekaeryrelkeelkeleaeLLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAEL 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 125 VLLRRSVVEKEKARAASDILCRSLTDETHQLRRTLAATAHMCQHLAkclDERQRVQGDAGEKSPAELEHTSRDTSGQSVI 204
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE---ERLEELEEELAELEEELEELEEELEELEEEL 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 205 KKLQEENRLLKQKvihVEDLNAKWQRYDASRDEYVKGLHAQLKRRQVPLepelmkKEISRLNRQLEEKISDCAEAKQELA 284
Cdd:COG1196   347 EEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERLE 417
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2030823680 285 AVKMARDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKVMSLMYQVSQRQDSRE 347
Cdd:COG1196   418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
259-341 7.65e-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: 38.81  E-value: 7.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 259 KKEISRLNRQL---EEKISDCAEAKQELAAVKMARDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKVMSL 335
Cdd:pfam16516  13 KDEIDCLQAQLqaaEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYL 92

                  ....*.
gi 2030823680 336 MYQVSQ 341
Cdd:pfam16516  93 QRQNQQ 98
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
62-304 4.00e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.65  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680   62 PSLVDALLDQVERFREQLRRQEDGASESQLRQEVERLTECLEEKEREMQQlmsqpqheqekevvllrrsvvEKEKARAAS 141
Cdd:PRK10929    78 PKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ---------------------EQDRAREIS 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  142 DILCRsLTDETHQLRRTLAatahmcqhlakclDERQRVQGDAGEKSPAelehtsrdtsGQSVIKKLQEENRLLKQKV--I 219
Cdd:PRK10929   137 DSLSQ-LPQQQTEARRQLN-------------EIERRLQTLGTPNTPL----------AQAQLTALQAESAALKALVdeL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  220 HVEDLNAKwQRYDASRdeyvkglhaqlkrrqvpLEPELMKKEISRLNRQLEEKISDCAEAKQELAavkmarDTALERVQM 299
Cdd:PRK10929   193 ELAQLSAN-NRQELAR-----------------LRSELAKKRSQQLDAYLQALRNQLNSQRQREA------ERALESTEL 248

                   ....*
gi 2030823680  300 LEQQI 304
Cdd:PRK10929   249 LAEQS 253
 
Name Accession Description Interval E-value
EABR pfam12180
TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is ...
215-248 1.28e-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: 53.27  E-value: 1.28e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2030823680 215 KQKVIHVEDLNAKWQRYDASRDEYVKGLHAQLKR 248
Cdd:pfam12180   1 KQQVADVLELNQQWQVYDQSREEYVRGLLARLKE 34
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
73-335 3.95e-07

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: 52.37  E-value: 3.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680   73 ERFREQLRRQEDGASESQ-----LRQEVERLTECLEEKEREMQQlMSQPQHEQEKEVVLLRRSVvekEKARAASDILCRS 147
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEkalaeLRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEV---EQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  148 LTDETHQLRRTLAATAHMCQHLAKCLDERQRVQGDAGEkspAELEHTSRDTSGQSVIKKLQEENRLLKQKVIHVEDLnak 227
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ---LKEELKALREALDELRAELTLLNEEAANLRERLESL--- 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  228 wQRYDASRDEYVKGLHAQLKRRQvpLEPELMKKEISRLNRQLEEKISDCAEAKQELAAVKMARDTALERVQMLEQQILAY 307
Cdd:TIGR02168  830 -ERRIAATERRLEDLEEQIEELS--EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2030823680  308 KDDFKSERADRERA-------HSRIQELEEKVMSL 335
Cdd:TIGR02168  907 ESKRSELRRELEELreklaqlELRLEGLEVRIDNL 941
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
65-347 5.50e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  65 VDALLDQVERFREQLRRQ--------------------EDGASESQLRQEVERLTECLEEKEREMQQLMSQpQHEQEKEV 124
Cdd:COG1196   191 LEDILGELERQLEPLERQaekaeryrelkeelkeleaeLLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAEL 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 125 VLLRRSVVEKEKARAASDILCRSLTDETHQLRRTLAATAHMCQHLAkclDERQRVQGDAGEKSPAELEHTSRDTSGQSVI 204
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE---ERLEELEEELAELEEELEELEEELEELEEEL 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 205 KKLQEENRLLKQKvihVEDLNAKWQRYDASRDEYVKGLHAQLKRRQVPLepelmkKEISRLNRQLEEKISDCAEAKQELA 284
Cdd:COG1196   347 EEAEEELEEAEAE---LAEAEEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERLE 417
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2030823680 285 AVKMARDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKVMSLMYQVSQRQDSRE 347
Cdd:COG1196   418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
72-348 6.11e-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: 45.43  E-value: 6.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680   72 VERFREqlRRQEdgaSESQL---RQEVERLTECLEEKEREMQQLmsQPQHEQEKEVVLLRRSVVEKEKARAASDIlcRSL 148
Cdd:TIGR02168  167 ISKYKE--RRKE---TERKLertRENLDRLEDILNELERQLKSL--ERQAEKAERYKELKAELRELELALLVLRL--EEL 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  149 TDETHQLRRTLAATAHMCQHLAKCLDERQrvqgdaGEKSPAELEHTSRDTSGQSVIKKLQEENRLLKQKVIHVEDLNAKW 228
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELE------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  229 QRYDASRDEYVKGLhAQLKRRQVPLEPEL---------MKKEISRLNRQLEEKISDCAEAKQELAAVKMARDTALERVQM 299
Cdd:TIGR02168  312 ANLERQLEELEAQL-EELESKLDELAEELaeleekleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2030823680  300 LEQQIlaykddfKSERADRERAHSRIQELEEKVMSLMYQVSQRQDSREP 348
Cdd:TIGR02168  391 LELQI-------ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
69-335 1.35e-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: 44.29  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680   69 LDQVERFREQLRRQEdgASESQLRQEVERLTECLEEKEReMQQLMSQpqhEQEKEVVLLRRSVVEKEKARAASDILCRSL 148
Cdd:TIGR02169  176 LEELEEVEENIERLD--LIIDEKRQQLERLRREREKAER-YQALLKE---KREYEGYELLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  149 TDETHQLRRTLAATAHMCQHLAKCLDERQRVQGDAGEKSPAELEHTSRDTSGQsvIKKLQEENRLLKQKvihVEDLNAKW 228
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERE---LEDAEERL 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  229 QRYDASRDEY------VKGLHAQLKRRQVPLEPEL--MKKEISRLNRQLEEKISDCAEAKQELAAVKMARDTALERVQML 300
Cdd:TIGR02169  325 AKLEAEIDKLlaeieeLEREIEEERKRRDKLTEEYaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2030823680  301 EQQILAYKDDFKSERADRERAHSRIQELEEKVMSL 335
Cdd:TIGR02169  405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
42-330 1.40e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  42 RDALIASLRTRLAALEGHTAPSLVDALLDQVERFREQLRRQEdgASESQLRQEVERLTECLEEK-EREMQQLMSQPQHEQ 120
Cdd:COG1196   225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE--AELEELRLELEELELELEEAqAEEYELLAELARLEQ 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 121 EKEVVLLRRSVVEKEKARAASDIlcRSLTDETHQLRRTLAATAHMCQHLAKCLDERQRVQGDAGEKSPAELEhtSRDTSG 200
Cdd:COG1196   303 DIARLEERRRELEERLEELEEEL--AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA--ELAEAE 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 201 QSVIKKLQEENRLLKQKVIHVEDLNAKwqrydASRDEYVKGLHAQLKRRQVPLEPELMKKEISRLNRQLEEkisdcAEAK 280
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEEL-----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL-----EEAA 448
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2030823680 281 QELAAVKMARDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEE 330
Cdd:COG1196   449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
44-335 3.43e-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: 43.12  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680   44 ALIASLRTRLAALEghTAPSLVDALLDQVERFREQLRRQEDGASES--QLRQEVERLTECLEEKEREMQQLMSQPQ---- 117
Cdd:TIGR02168  691 EKIAELEKALAELR--KELEELEEELEQLRKELEELSRQISALRKDlaRLEAEVEQLEERIAQLSKELTELEAEIEelee 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  118 ---------HEQEKEVVLLRRSVVEKEKARAASDILCRSLTDETHQLRRTLAATAHMCQHLAKCLDERQRVQGDAGEKSP 188
Cdd:TIGR02168  769 rleeaeeelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  189 AELEHTSRDTSgqsVIKKLQEENRLLKQKVIHVEDLNAKWQRYDASRDEYVKGLHAQLKRrqvplepelMKKEISRLNRQ 268
Cdd:TIGR02168  849 ELSEDIESLAA---EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE---------LESKRSELRRE 916
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2030823680  269 LEEKISDCAEAKQELAAVKMARDTALERV----QMLEQQILAYKDDFKserADRERAHSRIQELEEKVMSL 335
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIE---DDEEEARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
247-347 5.32e-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: 42.35  E-value: 5.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  247 KRRQVPLEPelmKKEISRLNRQLEEKISDCAEAKQELAAVKMARDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQ 326
Cdd:TIGR02168  667 KTNSSILER---RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
                           90       100
                   ....*....|....*....|.
gi 2030823680  327 ELEEKVMSLMYQVSQRQDSRE 347
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIE 764
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
214-335 7.13e-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: 7.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  214 LKQKVIHVEDLNAKWQRYDASRDEYvkglhAQLKRRQVPLEPELMKKEISRLNRQLEEKISDCAEAKQELAAVKMARDTA 293
Cdd:COG4913    247 AREQIELLEPIRELAERYAAARERL-----AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2030823680  294 LERVQMLEQQILAY----KDDFKSERADRERAHSRIQELEEKVMSL 335
Cdd:COG4913    322 REELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEAL 367
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
259-341 7.65e-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: 38.81  E-value: 7.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 259 KKEISRLNRQL---EEKISDCAEAKQELAAVKMARDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKVMSL 335
Cdd:pfam16516  13 KDEIDCLQAQLqaaEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYL 92

                  ....*.
gi 2030823680 336 MYQVSQ 341
Cdd:pfam16516  93 QRQNQQ 98
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
188-346 3.16e-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: 40.05  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  188 PAELEHTSRDtsgqsvIKKLQEENRLLKQKVIHVEdlnakwQRYDASRDEyVKGLHAQLKRRQvpLEPELMKKEISRLNR 267
Cdd:TIGR02169  673 PAELQRLRER------LEGLKRELSSLQSELRRIE------NRLDELSQE-LSDASRKIGEIE--KEIEQLEQEEEKLKE 737
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030823680  268 QLEEKISDCAEAKQELAAVKMARDTALERVQMLEQQILAYKDdfKSERADRERAHSRIQELEEKVMSLMYQVSqRQDSR 346
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE--ALNDLEARLSHSRIPEIQAELSKLEEEVS-RIEAR 813
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
62-304 4.00e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.65  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680   62 PSLVDALLDQVERFREQLRRQEDGASESQLRQEVERLTECLEEKEREMQQlmsqpqheqekevvllrrsvvEKEKARAAS 141
Cdd:PRK10929    78 PKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ---------------------EQDRAREIS 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  142 DILCRsLTDETHQLRRTLAatahmcqhlakclDERQRVQGDAGEKSPAelehtsrdtsGQSVIKKLQEENRLLKQKV--I 219
Cdd:PRK10929   137 DSLSQ-LPQQQTEARRQLN-------------EIERRLQTLGTPNTPL----------AQAQLTALQAESAALKALVdeL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  220 HVEDLNAKwQRYDASRdeyvkglhaqlkrrqvpLEPELMKKEISRLNRQLEEKISDCAEAKQELAavkmarDTALERVQM 299
Cdd:PRK10929   193 ELAQLSAN-NRQELAR-----------------LRSELAKKRSQQLDAYLQALRNQLNSQRQREA------ERALESTEL 248

                   ....*
gi 2030823680  300 LEQQI 304
Cdd:PRK10929   249 LAEQS 253
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
71-327 7.89e-03

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: 38.55  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680  71 QVERFREQLRRQEDgaSESQLRQEVERLTECLEEKEREMQQLMSQpqheQEKEVVLLRRSVVEKEKARAASDILCRSLTD 150
Cdd:pfam05483 528 QEERMLKQIENLEE--KEMNLRDELESVREEFIQKGDEVKCKLDK----SEENARSIEYEVLKKEKQMKILENKCNNLKK 601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 151 ETHQLRRTLAATAHMCQHLAK-CLDERQRVQGDAGEKSPAELEHTSRDTSGQSVIKKLQEEnrlLKQKVIHVEDLNAKWQ 229
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKKkGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE---IEDKKISEEKLLEEVE 678
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 230 RYDASRDEYVKgLHAQLKRR---QVPLEPELMKKEISRLNRQLEEKISDCAEAK---QELAAVKMARDTALERvqmLEQQ 303
Cdd:pfam05483 679 KAKAIADEAVK-LQKEIDKRcqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKnkeQEQSSAKAALEIELSN---IKAE 754
                         250       260
                  ....*....|....*....|....
gi 2030823680 304 ILAYKDDFKSERADRERAHSRIQE 327
Cdd:pfam05483 755 LLSLKKQLEIEKEEKEKLKMEAKE 778
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
174-287 8.42e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030823680 174 DERQRVQGDAGEKSPAELEHTSRDTSG--------QSVIKKLQEENRLLKQKVihvedlnakwqrydASRDEYVKGLHAQ 245
Cdd:COG2433   384 ELIEKELPEEEPEAEREKEHEERELTEeeeeirrlEEQVERLEAEVEELEAEL--------------EEKDERIERLERE 449
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2030823680 246 LK------RRQVPLEPEL--MKKEISRLNRQLEEKISDCAEAKQELAAVK 287
Cdd:COG2433   450 LSearseeRREIRKDREIsrLDREIERLERELEEERERIEELKRKLERLK 499
 
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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