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Conserved domains on  [gi|242009598|ref|XP_002425570|]
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Optineurin, putative [Pediculus humanus corporis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
424-510 1.44e-26

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


:

Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 103.20  E-value: 1.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 424 GDINSLVIELNEKDEKLKSKEDECEKLKESIANLNLECEKIPVLKVQAELYESDFKDEREAREKLVGEKEKMAEQIRILQ 503
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80

                 ....*..
gi 242009598 504 TKLENLN 510
Cdd:cd09803   81 RENQELK 87
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
185-509 2.69e-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: 50.44  E-value: 2.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   185 EVHNLQKNILELERLQENAESNDECLSLDKYDLQKTIKKLKHEILNVSQKLKdfQCENDYLKNKMKEQNTKSQNGSsfvp 264
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS--ALRKDLARLEAEVEQLEERIAQ---- 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   265 VSLPNSEARVQISNLLKQLDDERRKVTILKKEIKKMKVLF------LSKNDNPSDELSicvDELNDMNDSVQNQNMRFDG 338
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeqlkeeLKALREALDELR---AELTLLNEEAANLRERLES 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   339 LNSWINLAEETVMGSNFQKEHQTQILSEISHlknyvmreekISKEKEESLKVMHYQFSKLLNDYKELQEKLNVLNESKME 418
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAA----------EIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   419 NDKmkgdinslviELNEKDEKLKSKEDECEKLKESIANLNLECEKIPVLKVQ-----AELYESDFKDEREAREKLVGEKE 493
Cdd:TIGR02168  899 LSE----------ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerlSEEYSLTLEEAEALENKIEDDEE 968
                          330
                   ....*....|....*.
gi 242009598   494 KMAEQIRILQTKLENL 509
Cdd:TIGR02168  969 EARRRLKRLENKIKEL 984
NEMO super family cl13089
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ...
77-136 7.97e-03

NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.


The actual alignment was detected with superfamily member pfam11577:

Pssm-ID: 431942 [Multi-domain]  Cd Length: 67  Bit Score: 35.15  E-value: 7.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   77 LNHLLQENQKLKETLNQNNLAIKSQLNTFFMWQQEVLKTHETHKQKFLETKDLILKLRLE 136
Cdd:pfam11577   8 MKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
 
Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
424-510 1.44e-26

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 103.20  E-value: 1.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 424 GDINSLVIELNEKDEKLKSKEDECEKLKESIANLNLECEKIPVLKVQAELYESDFKDEREAREKLVGEKEKMAEQIRILQ 503
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80

                 ....*..
gi 242009598 504 TKLENLN 510
Cdd:cd09803   81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
410-510 6.78e-26

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: 101.60  E-value: 6.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598  410 NVLNESKMENDKmKGDINSLVIELNEKDEKLKSKEDECEKLKESIANLNLECEKIPVLKVQAELYESDFKDEREAREKLV 489
Cdd:pfam16516   1 EELKRKEMEKVY-KDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLH 79
                          90       100
                  ....*....|....*....|.
gi 242009598  490 GEKEKMAEQIRILQTKLENLN 510
Cdd:pfam16516  80 EEKEQLAAQLEYLQRQNQQLK 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
185-509 2.69e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 2.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   185 EVHNLQKNILELERLQENAESNDECLSLDKYDLQKTIKKLKHEILNVSQKLKdfQCENDYLKNKMKEQNTKSQNGSsfvp 264
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS--ALRKDLARLEAEVEQLEERIAQ---- 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   265 VSLPNSEARVQISNLLKQLDDERRKVTILKKEIKKMKVLF------LSKNDNPSDELSicvDELNDMNDSVQNQNMRFDG 338
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeqlkeeLKALREALDELR---AELTLLNEEAANLRERLES 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   339 LNSWINLAEETVMGSNFQKEHQTQILSEISHlknyvmreekISKEKEESLKVMHYQFSKLLNDYKELQEKLNVLNESKME 418
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAA----------EIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   419 NDKmkgdinslviELNEKDEKLKSKEDECEKLKESIANLNLECEKIPVLKVQ-----AELYESDFKDEREAREKLVGEKE 493
Cdd:TIGR02168  899 LSE----------ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerlSEEYSLTLEEAEALENKIEDDEE 968
                          330
                   ....*....|....*.
gi 242009598   494 KMAEQIRILQTKLENL 509
Cdd:TIGR02168  969 EARRRLKRLENKIKEL 984
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
396-515 1.01e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 396 SKLLNDYKELQEKLNVLNESKMENDKMKGDINSLVIELNEKDEKLKSKEDECEKLKESIanlnlecEKIPVLKVQAELYE 475
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-------KELKELKEKAEEYI 296
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 242009598 476 --SDFKDE-REAREKLVGEKEKMAEQIRILQTKLENLNSEKKE 515
Cdd:PRK03918 297 klSEFYEEyLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
126-463 2.77e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   126 TKDLILKLRLENANLKKQIENMTTTTTNDFSLLSNGDSNIKSNFSPGVDSINKPDLNIDEVHNLQKnilELERLQeNAES 205
Cdd:pfam15921  473 TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKN---EGDHLR-NVQT 548
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   206 NDECLSLDKYDLQKTIKKLKHEILNVSQKLKD-------FQCENDYLKNKMKEQNTKSQNgssfvpVSLPNSEARVQISN 278
Cdd:pfam15921  549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQE------FKILKDKKDAKIRE 622
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   279 LLKQLDD-ERRKVTILKKEIKKMKVL--FLSKNDNPSDELSICVDELNDMND--SVQNQNMRfdglnswiNLAEETVMGS 353
Cdd:pfam15921  623 LEARVSDlELEKVKLVNAGSERLRAVkdIKQERDQLLNEVKTSRNELNSLSEdyEVLKRNFR--------NKSEEMETTT 694
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   354 NFQKEHQTQILSEISHLKNYVMREEKISKEKEESLKVMHYQFSKLLNDYKELQEKLNVLNES-----------KMENDKM 422
Cdd:pfam15921  695 NKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAmtnankekhflKEEKNKL 774
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 242009598   423 KGDINSLVIELNEKDEKLKSKEDECEKLKESIANLNLECEK 463
Cdd:pfam15921  775 SQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
402-515 1.04e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 402 YKELQEKLNVL---------NESKMENDKMKGDINSLVIELNEKDEKLKSKEDECEKLKESIANLNLEcekipVLKVQAE 472
Cdd:COG1196  215 YRELKEELKELeaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-----LEEAQAE 289
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 242009598 473 LY---------ESDFKDEREAREKLVGEKEKMAEQIRILQTKLENLNSEKKE 515
Cdd:COG1196  290 EYellaelarlEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
398-517 1.34e-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: 41.97  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   398 LLNDYKELQEKLNVLNESKmenDKMKGDINSLVIELNEKDEKLKSKEDECEKLKESIANLnlecekipvlkvQAELYEsd 477
Cdd:TIGR02168  230 LVLRLEELREELEELQEEL---KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL------------QKELYA-- 292
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 242009598   478 fkderearekLVGEKEKMAEQIRILQTKLENLNSEKKEGN 517
Cdd:TIGR02168  293 ----------LANEISRLEQQKQILRERLANLERQLEELE 322
PRK01156 PRK01156
chromosome segregation protein; Provisional
193-513 1.86e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 193 ILELERLQENAESndeclsldkydLQKTIKKLKHEILNVsqklkdfqcenDYLKNKMKEQNTksqngssfvpvslpnsea 272
Cdd:PRK01156 158 ILEINSLERNYDK-----------LKDVIDMLRAEISNI-----------DYLEEKLKSSNL------------------ 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 273 rvQISNLLKQLDDERRKVTILKKEIKKMKVLFLSKNDNpSDELSICVDELNDMNDSVQNQNMRFDGLNSWINLAEETVMG 352
Cdd:PRK01156 198 --ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDD-YNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNY 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 353 SNFQKEHQTQILSEISHLKNYVMREEKISKEKEESLKVMHYQFSKLLNDYKELQEKLNVLNESKMENDKMKG---DINSL 429
Cdd:PRK01156 275 YKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSrydDLNNQ 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 430 VIELNEKDEKLKSKEDECEKLKESIANlnlecEKIPVLKVQAELYESDFKDEREArEKLVGEKEKMAEQIRILQTKLENL 509
Cdd:PRK01156 355 ILELEGYEMDYNSYLKSIESLKKKIEE-----YSKNIERMSAFISEILKIQEIDP-DAIKKELNEINVKLQDISSKVSSL 428

                 ....
gi 242009598 510 NSEK 513
Cdd:PRK01156 429 NQRI 432
NEMO pfam11577
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ...
77-136 7.97e-03

NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.


Pssm-ID: 431942 [Multi-domain]  Cd Length: 67  Bit Score: 35.15  E-value: 7.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   77 LNHLLQENQKLKETLNQNNLAIKSQLNTFFMWQQEVLKTHETHKQKFLETKDLILKLRLE 136
Cdd:pfam11577   8 MKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
 
Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
424-510 1.44e-26

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 103.20  E-value: 1.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 424 GDINSLVIELNEKDEKLKSKEDECEKLKESIANLNLECEKIPVLKVQAELYESDFKDEREAREKLVGEKEKMAEQIRILQ 503
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80

                 ....*..
gi 242009598 504 TKLENLN 510
Cdd:cd09803   81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
410-510 6.78e-26

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: 101.60  E-value: 6.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598  410 NVLNESKMENDKmKGDINSLVIELNEKDEKLKSKEDECEKLKESIANLNLECEKIPVLKVQAELYESDFKDEREAREKLV 489
Cdd:pfam16516   1 EELKRKEMEKVY-KDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLH 79
                          90       100
                  ....*....|....*....|.
gi 242009598  490 GEKEKMAEQIRILQTKLENLN 510
Cdd:pfam16516  80 EEKEQLAAQLEYLQRQNQQLK 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
185-509 2.69e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 2.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   185 EVHNLQKNILELERLQENAESNDECLSLDKYDLQKTIKKLKHEILNVSQKLKdfQCENDYLKNKMKEQNTKSQNGSsfvp 264
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS--ALRKDLARLEAEVEQLEERIAQ---- 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   265 VSLPNSEARVQISNLLKQLDDERRKVTILKKEIKKMKVLF------LSKNDNPSDELSicvDELNDMNDSVQNQNMRFDG 338
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeqlkeeLKALREALDELR---AELTLLNEEAANLRERLES 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   339 LNSWINLAEETVMGSNFQKEHQTQILSEISHlknyvmreekISKEKEESLKVMHYQFSKLLNDYKELQEKLNVLNESKME 418
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAA----------EIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   419 NDKmkgdinslviELNEKDEKLKSKEDECEKLKESIANLNLECEKIPVLKVQ-----AELYESDFKDEREAREKLVGEKE 493
Cdd:TIGR02168  899 LSE----------ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerlSEEYSLTLEEAEALENKIEDDEE 968
                          330
                   ....*....|....*.
gi 242009598   494 KMAEQIRILQTKLENL 509
Cdd:TIGR02168  969 EARRRLKRLENKIKEL 984
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
396-515 1.01e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 396 SKLLNDYKELQEKLNVLNESKMENDKMKGDINSLVIELNEKDEKLKSKEDECEKLKESIanlnlecEKIPVLKVQAELYE 475
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-------KELKELKEKAEEYI 296
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 242009598 476 --SDFKDE-REAREKLVGEKEKMAEQIRILQTKLENLNSEKKE 515
Cdd:PRK03918 297 klSEFYEEyLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
126-463 2.77e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   126 TKDLILKLRLENANLKKQIENMTTTTTNDFSLLSNGDSNIKSNFSPGVDSINKPDLNIDEVHNLQKnilELERLQeNAES 205
Cdd:pfam15921  473 TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKN---EGDHLR-NVQT 548
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   206 NDECLSLDKYDLQKTIKKLKHEILNVSQKLKD-------FQCENDYLKNKMKEQNTKSQNgssfvpVSLPNSEARVQISN 278
Cdd:pfam15921  549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQE------FKILKDKKDAKIRE 622
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   279 LLKQLDD-ERRKVTILKKEIKKMKVL--FLSKNDNPSDELSICVDELNDMND--SVQNQNMRfdglnswiNLAEETVMGS 353
Cdd:pfam15921  623 LEARVSDlELEKVKLVNAGSERLRAVkdIKQERDQLLNEVKTSRNELNSLSEdyEVLKRNFR--------NKSEEMETTT 694
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   354 NFQKEHQTQILSEISHLKNYVMREEKISKEKEESLKVMHYQFSKLLNDYKELQEKLNVLNES-----------KMENDKM 422
Cdd:pfam15921  695 NKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAmtnankekhflKEEKNKL 774
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 242009598   423 KGDINSLVIELNEKDEKLKSKEDECEKLKESIANLNLECEK 463
Cdd:pfam15921  775 SQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
402-515 1.04e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 402 YKELQEKLNVL---------NESKMENDKMKGDINSLVIELNEKDEKLKSKEDECEKLKESIANLNLEcekipVLKVQAE 472
Cdd:COG1196  215 YRELKEELKELeaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-----LEEAQAE 289
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 242009598 473 LY---------ESDFKDEREAREKLVGEKEKMAEQIRILQTKLENLNSEKKE 515
Cdd:COG1196  290 EYellaelarlEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
398-517 1.34e-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: 41.97  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   398 LLNDYKELQEKLNVLNESKmenDKMKGDINSLVIELNEKDEKLKSKEDECEKLKESIANLnlecekipvlkvQAELYEsd 477
Cdd:TIGR02168  230 LVLRLEELREELEELQEEL---KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL------------QKELYA-- 292
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 242009598   478 fkderearekLVGEKEKMAEQIRILQTKLENLNSEKKEGN 517
Cdd:TIGR02168  293 ----------LANEISRLEQQKQILRERLANLERQLEELE 322
PRK01156 PRK01156
chromosome segregation protein; Provisional
193-513 1.86e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 193 ILELERLQENAESndeclsldkydLQKTIKKLKHEILNVsqklkdfqcenDYLKNKMKEQNTksqngssfvpvslpnsea 272
Cdd:PRK01156 158 ILEINSLERNYDK-----------LKDVIDMLRAEISNI-----------DYLEEKLKSSNL------------------ 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 273 rvQISNLLKQLDDERRKVTILKKEIKKMKVLFLSKNDNpSDELSICVDELNDMNDSVQNQNMRFDGLNSWINLAEETVMG 352
Cdd:PRK01156 198 --ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDD-YNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNY 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 353 SNFQKEHQTQILSEISHLKNYVMREEKISKEKEESLKVMHYQFSKLLNDYKELQEKLNVLNESKMENDKMKG---DINSL 429
Cdd:PRK01156 275 YKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSrydDLNNQ 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 430 VIELNEKDEKLKSKEDECEKLKESIANlnlecEKIPVLKVQAELYESDFKDEREArEKLVGEKEKMAEQIRILQTKLENL 509
Cdd:PRK01156 355 ILELEGYEMDYNSYLKSIESLKKKIEE-----YSKNIERMSAFISEILKIQEIDP-DAIKKELNEINVKLQDISSKVSSL 428

                 ....
gi 242009598 510 NSEK 513
Cdd:PRK01156 429 NQRI 432
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
181-520 5.32e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 181 LNIDEVHNLQKNILELERLQENAESNDECLSLDKYDLQKTIKKLK-------HEILNVSQKLKDFQCENDYLKNKMKE-Q 252
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEkeleevlREINEISSELPELREELEKLEKEVKElE 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 253 NTKSQNGSSFVPVSLPNSEAR---VQISNLLKQLDDERRKVTILKKEIKKMKVLflsknDNPSDELSICVDELNDMNDSV 329
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRkleEKIRELEERIEELKKEIEELEEKVKELKEL-----KEKAEEYIKLSEFYEEYLDEL 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 330 QNQNMRFDGLNSWINLAEETVMGSNFQKEHQTQILSEISHLKNYVMREEKISKEKEESLKVMH-----------YQFSKL 398
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEelerlkkrltgLTPEKL 389
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598 399 LNDYKELQEKLNVLNESKMENDKMKGDINSLVIELNEKDEKLKSKEDEC---------EKLKESIANLNLECEKIPVLKV 469
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELK 469
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 242009598 470 QAELYESDFKDE-REAREKLVGEKE-----KMAEQIRILQTKLENLNSEKKEGNSND 520
Cdd:PRK03918 470 EIEEKERKLRKElRELEKVLKKESEliklkELAEQLKELEEKLKKYNLEELEKKAEE 526
NEMO pfam11577
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ...
77-136 7.97e-03

NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.


Pssm-ID: 431942 [Multi-domain]  Cd Length: 67  Bit Score: 35.15  E-value: 7.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 242009598   77 LNHLLQENQKLKETLNQNNLAIKSQLNTFFMWQQEVLKTHETHKQKFLETKDLILKLRLE 136
Cdd:pfam11577   8 MKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
 
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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