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Conserved domains on  [gi|1488333082|ref|XP_026580415|]
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ATR-interacting protein [Pseudonaja textilis]

Protein Classification

OmpH family outer membrane protein( domain architecture ID 12048616)

OmpH family outer membrane protein may play an active role either as folding catalysts or as chaperones in extracytoplasmic compartments; similar to Flavobacterium psychrophilum outer membrane protein P18

Gene Ontology:  GO:0051082|GO:0016020
PubMed:  2318304

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 155-243 4.16e-06

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


:

Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 47.19  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 155 QYKEAMKKL----KEMQDEILIKNGEIKVLRDSMQQMESTVEDQRKsyillerEKAQCLNEKEKEFSRKLQSLQSELQ-F 229
Cdd:pfam03938  16 EGKAAQAQLekkfKKRQAELEAKQKELQKLYEELQKDGALLEEERE-------EKEQELQKKEQELQQLQQKAQQELQkK 88

                          90
                  ....*....|....
gi 1488333082 230 RDAEMNELRTKILN 243
Cdd:pfam03938  89 QQELLQPIQDKINK 102
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 94-322 2.54e-05

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


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.19  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082   94 SETNLLKTEPNVQLSIFPNSTNQFKTPDQwniTLTTETNPSENSMEEMklkgRFKFETLQAQYKEAMKKLKEMQDEILIK 173
Cdd:pfam15921  667 NELNSLSEDYEVLKRNFRNKSEEMETTTN---KLKMQLKSAQSELEQT----RNTLKSMEGSDGHAMKVAMGMQKQITAK 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082  174 NGEIKVLRDSMQQMESTVEDQRKSYILLEREKAQcLNEKEKEFSRKLQSLQSELQFRDAEMNELRTKILNCERIKPVALV 253
Cdd:pfam15921  740 RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNK-LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082  254 SYT------SPKKSPSNPMKIERSTHI---ENKSYPTEESFGSQILPIPSCSKTQSHVQAPH------QNNDSKTNALET 318
Cdd:pfam15921  819 QFAecqdiiQRQEQESVRLKLQHTLDVkelQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQstasflSHHSRKTNALKE 898


                   ....
gi 1488333082  319 EPVK 322
Cdd:pfam15921  899 DPTR 902
 
Name Accession Description Interval E-value
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 155-243 4.16e-06

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 47.19  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 155 QYKEAMKKL----KEMQDEILIKNGEIKVLRDSMQQMESTVEDQRKsyillerEKAQCLNEKEKEFSRKLQSLQSELQ-F 229
Cdd:pfam03938  16 EGKAAQAQLekkfKKRQAELEAKQKELQKLYEELQKDGALLEEERE-------EKEQELQKKEQELQQLQQKAQQELQkK 88

                          90
                  ....*....|....
gi 1488333082 230 RDAEMNELRTKILN 243
Cdd:pfam03938  89 QQELLQPIQDKINK 102
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 154-241 6.08e-06

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 46.42  E-value: 6.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082  154 AQYKEAMKKLKEMQDEiliKNGEIKVLRDSMQQMESTVEDQRKSYILLEREKAQC-LNEKEKEFSRKLQSLQSELQFRDA 232
Cdd:smart00935  14 PAGKAAQKQLEKEFKK---RQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKeLQKKVQEFQRKQQKLQQDLQKRQQ 90

                           90
                   ....*....|
gi 1488333082  233 E-MNELRTKI 241
Cdd:smart00935  91 EeLQKILDKI 100
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 94-322 2.54e-05

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: 48.19  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082   94 SETNLLKTEPNVQLSIFPNSTNQFKTPDQwniTLTTETNPSENSMEEMklkgRFKFETLQAQYKEAMKKLKEMQDEILIK 173
Cdd:pfam15921  667 NELNSLSEDYEVLKRNFRNKSEEMETTTN---KLKMQLKSAQSELEQT----RNTLKSMEGSDGHAMKVAMGMQKQITAK 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082  174 NGEIKVLRDSMQQMESTVEDQRKSYILLEREKAQcLNEKEKEFSRKLQSLQSELQFRDAEMNELRTKILNCERIKPVALV 253
Cdd:pfam15921  740 RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNK-LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082  254 SYT------SPKKSPSNPMKIERSTHI---ENKSYPTEESFGSQILPIPSCSKTQSHVQAPH------QNNDSKTNALET 318
Cdd:pfam15921  819 QFAecqdiiQRQEQESVRLKLQHTLDVkelQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQstasflSHHSRKTNALKE 898


                   ....
gi 1488333082  319 EPVK 322
Cdd:pfam15921  899 DPTR 902
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 155-243 2.60e-05

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 45.60  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 155 QYKEAMKKLKEMQDEiliKNGEIKVLRDSMQQMESTVEDQRKSY---ILLEREKAqcLNEKEKEFSRKLQSLQSELQFRD 231
Cdd:COG2825    40 EGKAAQKKLEKEFKK---RQAELQKLEKELQALQEKLQKEAATLseeERQKKERE--LQKKQQELQRKQQEAQQDLQKRQ 114

                          90
                  ....*....|...
gi 1488333082 232 AE-MNELRTKILN 243
Cdd:COG2825   115 QElLQPILEKIQK 127
PRK12704 PRK12704
phosphodiesterase; Provisional
 134-247 4.73e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 134 SENSMEEMKlkgrfKFETLQAqyKEAMKKLK-EMQDEILIKNGEIKVLRDSMQQMESTVEDQRKsyiLLEREKAQcLNEK 212
Cdd:PRK12704   47 AKKEAEAIK-----KEALLEA--KEEIHKLRnEFEKELRERRNELQKLEKRLLQKEENLDRKLE---LLEKREEE-LEKK 115

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1488333082 213 EKEFSRKLQSLQSelqfRDAEMNELRTKILN-CERI 247
Cdd:PRK12704  116 EKELEQKQQELEK----KEEELEELIEEQLQeLERI 147
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 147-228 8.34e-03

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: 36.17  E-value: 8.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 147 FKFETLQAQYKEAMKKLKEMQDEILIKNGEIKVLRDSMQQME--STVEDQRKSYILLEREKAQCLNEKEKEFSRKLQSLQ 224
Cdd:cd09803     1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPvlKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                  ....
gi 1488333082 225 SELQ 228
Cdd:cd09803    81 RENQ 84
 
Name Accession Description Interval E-value
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 155-243 4.16e-06

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 47.19  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 155 QYKEAMKKL----KEMQDEILIKNGEIKVLRDSMQQMESTVEDQRKsyillerEKAQCLNEKEKEFSRKLQSLQSELQ-F 229
Cdd:pfam03938  16 EGKAAQAQLekkfKKRQAELEAKQKELQKLYEELQKDGALLEEERE-------EKEQELQKKEQELQQLQQKAQQELQkK 88

                          90
                  ....*....|....
gi 1488333082 230 RDAEMNELRTKILN 243
Cdd:pfam03938  89 QQELLQPIQDKINK 102
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 154-241 6.08e-06

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 46.42  E-value: 6.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082  154 AQYKEAMKKLKEMQDEiliKNGEIKVLRDSMQQMESTVEDQRKSYILLEREKAQC-LNEKEKEFSRKLQSLQSELQFRDA 232
Cdd:smart00935  14 PAGKAAQKQLEKEFKK---RQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKeLQKKVQEFQRKQQKLQQDLQKRQQ 90

                           90
                   ....*....|
gi 1488333082  233 E-MNELRTKI 241
Cdd:smart00935  91 EeLQKILDKI 100
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 94-322 2.54e-05

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: 48.19  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082   94 SETNLLKTEPNVQLSIFPNSTNQFKTPDQwniTLTTETNPSENSMEEMklkgRFKFETLQAQYKEAMKKLKEMQDEILIK 173
Cdd:pfam15921  667 NELNSLSEDYEVLKRNFRNKSEEMETTTN---KLKMQLKSAQSELEQT----RNTLKSMEGSDGHAMKVAMGMQKQITAK 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082  174 NGEIKVLRDSMQQMESTVEDQRKSYILLEREKAQcLNEKEKEFSRKLQSLQSELQFRDAEMNELRTKILNCERIKPVALV 253
Cdd:pfam15921  740 RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNK-LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082  254 SYT------SPKKSPSNPMKIERSTHI---ENKSYPTEESFGSQILPIPSCSKTQSHVQAPH------QNNDSKTNALET 318
Cdd:pfam15921  819 QFAecqdiiQRQEQESVRLKLQHTLDVkelQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQstasflSHHSRKTNALKE 898


                   ....
gi 1488333082  319 EPVK 322
Cdd:pfam15921  899 DPTR 902
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 155-243 2.60e-05

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 45.60  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 155 QYKEAMKKLKEMQDEiliKNGEIKVLRDSMQQMESTVEDQRKSY---ILLEREKAqcLNEKEKEFSRKLQSLQSELQFRD 231
Cdd:COG2825    40 EGKAAQKKLEKEFKK---RQAELQKLEKELQALQEKLQKEAATLseeERQKKERE--LQKKQQELQRKQQEAQQDLQKRQ 114

                          90
                  ....*....|...
gi 1488333082 232 AE-MNELRTKILN 243
Cdd:COG2825   115 QElLQPILEKIQK 127
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
127-241 2.03e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 127 LTTETNPSENSMEEMKLKGRFKFETLQAQYKEAMKKLKEMQDEILIKNGEIKVLRDSMQQMESTVEDQRKSYILLEREKA 206
Cdd:COG4372     4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1488333082 207 QcLNEKEKEFSRKLQSLQSELQFRDAEMNELRTKI 241
Cdd:COG4372    84 E-LNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
150-241 2.35e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 150 ETLQAQYKEAMKKLKEMQDEILIKNGEIKVLRDSMQQMESTVEDqrksyilLEREKAQcLNEKEKEFSRKLQSLQSELQF 229
Cdd:COG4372    76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQD-LEQQRKQLEAQIAELQSEIAE 147

                          90
                  ....*....|..
gi 1488333082 230 RDAEMNELRTKI 241
Cdd:COG4372   148 REEELKELEEQL 159
PRK12704 PRK12704
phosphodiesterase; Provisional
 134-247 4.73e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 134 SENSMEEMKlkgrfKFETLQAqyKEAMKKLK-EMQDEILIKNGEIKVLRDSMQQMESTVEDQRKsyiLLEREKAQcLNEK 212
Cdd:PRK12704   47 AKKEAEAIK-----KEALLEA--KEEIHKLRnEFEKELRERRNELQKLEKRLLQKEENLDRKLE---LLEKREEE-LEKK 115

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1488333082 213 EKEFSRKLQSLQSelqfRDAEMNELRTKILN-CERI 247
Cdd:PRK12704  116 EKELEQKQQELEK----KEEELEELIEEQLQeLERI 147
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 150-246 1.23e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.52  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 150 ETLQAQYKEAMKKLKEMQDEILIKNGEikvLRDSmQQMESTVEDQRKSY----ILLEREKAQCLNEKEK----------- 214
Cdd:pfam20492   2 EEAEREKQELEERLKQYEEETKKAQEE---LEES-EETAEELEEERRQAeeeaERLEQKRQEAEEEKERleesaemeaee 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1488333082 215 ---------EFSRKLQSLQSELQFRDAEMNELRTKILNCER 246
Cdd:pfam20492  78 keqleaelaEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 150-243 2.86e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 150 ETLQAQYKEAMKKLKEMQDEILIKNGEIKVLRDSMQQMESTVEDQRKsyiLLEREKAQcLNE--KEKEFsrklQSLQSEL 227
Cdd:COG1579    27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQ-LGNvrNNKEY----EALQKEI 98

                          90
                  ....*....|....*.
gi 1488333082 228 QFRDAEMNELRTKILN 243
Cdd:COG1579    99 ESLKRRISDLEDEILE 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 150-245 5.83e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 150 ETLQAQYKEAMKKLKEMQDEILIKNGEIKVLRDSMQQMESTVEDQRKSYILLEREKAQC------LNEKEKEFSRKLQSL 223
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarLEERRRELEERLEEL 321

                          90       100
                  ....*....|....*....|..
gi 1488333082 224 QSELQFRDAEMNELRTKILNCE 245
Cdd:COG1196   322 EEELAELEEELEELEEELEELE 343
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
150-241 6.45e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 150 ETLQAQYKEAMKKLKEMQDEIliknGEIKVLRDSMQQMESTVEDQRKSYILL---EREKAQCLNEKEKEFSRKLQSLQSE 226
Cdd:COG1340     4 DELSSSLEELEEKIEELREEI----EELKEKRDELNEELKELAEKRDELNAQvkeLREEAQELREKRDELNEKVKELKEE 79

                          90
                  ....*....|....*
gi 1488333082 227 LQFRDAEMNELRTKI 241
Cdd:COG1340    80 RDELNEKLNELREEL 94
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 147-228 8.34e-03

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: 36.17  E-value: 8.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488333082 147 FKFETLQAQYKEAMKKLKEMQDEILIKNGEIKVLRDSMQQME--STVEDQRKSYILLEREKAQCLNEKEKEFSRKLQSLQ 224
Cdd:cd09803     1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPvlKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                  ....
gi 1488333082 225 SELQ 228
Cdd:cd09803    81 RENQ 84
 
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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