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Conserved domains on  [gi|755563793|ref|XP_011245687|]
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guanine nucleotide exchange factor for Rab-3A isoform X5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rab11BD_RAB3IP_like super family cl41767
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 ...
 198-359 3.76e-106

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 (RAB3IL1) and similar proteins; The family includes RAB3IP and RAB3IL1, as well as Rab guanine nucleotide exchange factor SEC2 from yeast. RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. RAB3IL1, also called guanine nucleotide exchange factor for Rab-3A (GRAB), or Rab3A-interacting-like protein 1, or Rabin3-like 1, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. As a dual Rab-binding protein, RAB3IL1 could potentially link Rab3 and Rab11 and/or Rab8 and Rab11-mediated intracellular trafficking processes. It may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. It may also activate RAB8A and RAB8B. In addition, RAB3IL1 interacts with InsP6K1 and plays a role for InsP7 in vesicle exocytosis. SEC2 is a guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis. SEC2 binds the Rab GTPase YPT32 but does not have exchange activity on YPT32. The model corresponds to the Rab11a/Rab11b-binding region of family members which lies within the carboxy-terminus, a region distinct from their GEF domain and Rab3a-binding region.


The actual alignment was detected with superfamily member cd21069:

Pssm-ID: 425398  Cd Length: 163  Bit Score: 308.33  E-value: 3.76e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793 198 SRQVDTTLFAEFQAWRASPTLDKSCPFLERVYREDVGPCLDFTVQELSALVRTAVEDNTLTIEPVASQTLPAVKVPTVEC 277
Cdd:cd21069    2 GKEVDTVLFAEFQAWKESPTLDRSCPFLSRIYREDIGPCLDFTKRELSDLVQSAVENNTLTIEPVASQALPVVKASAVEC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793 278 NNTNTCALSGLARTCHHRIRLGDSDSHYYISPSSRARITAVCNFFTYIRYIQQGLVRQDAEPMFWEIMRLRKGMSLAKLG 357
Cdd:cd21069   82 GGPKKCALSGLSRTCRHRIKLGDSGNYYYISPSCRARITAVCNFFTYIRYIQQGLVRQDAEQMFWEVMRLRREMSLAKLG 161


                 ..
gi 755563793 358 FF 359
Cdd:cd21069  162 FY 163
Sec2p super family cl05764
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 23-91 2.55e-10

GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.


The actual alignment was detected with superfamily member pfam06428:

Pssm-ID: 428938 [Multi-domain]  Cd Length: 92  Bit Score: 56.42  E-value: 2.55e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755563793   23 KLKDEECERLC--KVRAQLEQELEELTASLFEEAHKMVREANMKQATSEK-------QLKEAWGKIDMLQAEVTALKT 91
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVAAARREKHAVEIkndqlkeQLKEKETLLESLQEQLKELKQ 78
 
Name Accession Description Interval E-value
Rab11BD_RAB3IL1 cd21069
Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called ...
 198-359 3.76e-106

Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called guanine nucleotide exchange factor for Rab-3A (GRAB), or Rab3A-interacting-like protein 1, or Rabin3-like 1, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. As a dual Rab-binding protein, RAB3IL1 could potentially link Rab3 and Rab11 and/or Rab8 and Rab11-mediated intracellular trafficking processes. It may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. It may also activate RAB8A and RAB8B. In addition, RAB3IL1 interacts with InsP6K1 and plays a role for InsP7 in vesicle exocytosis. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IL1 lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411033  Cd Length: 163  Bit Score: 308.33  E-value: 3.76e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793 198 SRQVDTTLFAEFQAWRASPTLDKSCPFLERVYREDVGPCLDFTVQELSALVRTAVEDNTLTIEPVASQTLPAVKVPTVEC 277
Cdd:cd21069    2 GKEVDTVLFAEFQAWKESPTLDRSCPFLSRIYREDIGPCLDFTKRELSDLVQSAVENNTLTIEPVASQALPVVKASAVEC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793 278 NNTNTCALSGLARTCHHRIRLGDSDSHYYISPSSRARITAVCNFFTYIRYIQQGLVRQDAEPMFWEIMRLRKGMSLAKLG 357
Cdd:cd21069   82 GGPKKCALSGLSRTCRHRIKLGDSGNYYYISPSCRARITAVCNFFTYIRYIQQGLVRQDAEQMFWEVMRLRREMSLAKLG 161


                 ..
gi 755563793 358 FF 359
Cdd:cd21069  162 FY 163
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 23-91 2.55e-10

GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.


Pssm-ID: 428938 [Multi-domain]  Cd Length: 92  Bit Score: 56.42  E-value: 2.55e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755563793   23 KLKDEECERLC--KVRAQLEQELEELTASLFEEAHKMVREANMKQATSEK-------QLKEAWGKIDMLQAEVTALKT 91
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVAAARREKHAVEIkndqlkeQLKEKETLLESLQEQLKELKQ 78
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 11-93 9.11e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793  11 LKEELYKAQKELKLKDEECERLCKVRAQLEQELEELTASLfEEAHKMVREANMKQATSEKQLKEAWGKIDMLQAEVTALK 90
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-AALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103


                 ...
gi 755563793  91 TLV 93
Cdd:COG4942  104 EEL 106
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-90 3.47e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 3.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793     9 EFLKEELYKAQKELKLKDEECERLCKVRAQLEQELEELTASLFEEAHKMVREANMKQATSEKQLKEAWGKIDMLQAEVTA 88
Cdd:TIGR02168  192 EDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271


                   ..
gi 755563793    89 LK 90
Cdd:TIGR02168  272 LR 273
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 11-90 6.97e-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: 35.40  E-value: 6.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793  11 LKEELYKAQKELKLKDEECERLCKVRAQLEQELEELT-----ASLFEEAHKMVREANMKQATSEKQLKEawgKIDMLQAE 85
Cdd:cd09803    6 LAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPvlkaqAEIYKSDFEAERAAREKLHQEKEQLAE---QLEYLQRE 82


                 ....*
gi 755563793  86 VTALK 90
Cdd:cd09803   83 NQELK 87
 
Name Accession Description Interval E-value
Rab11BD_RAB3IL1 cd21069
Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called ...
 198-359 3.76e-106

Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called guanine nucleotide exchange factor for Rab-3A (GRAB), or Rab3A-interacting-like protein 1, or Rabin3-like 1, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. As a dual Rab-binding protein, RAB3IL1 could potentially link Rab3 and Rab11 and/or Rab8 and Rab11-mediated intracellular trafficking processes. It may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. It may also activate RAB8A and RAB8B. In addition, RAB3IL1 interacts with InsP6K1 and plays a role for InsP7 in vesicle exocytosis. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IL1 lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411033  Cd Length: 163  Bit Score: 308.33  E-value: 3.76e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793 198 SRQVDTTLFAEFQAWRASPTLDKSCPFLERVYREDVGPCLDFTVQELSALVRTAVEDNTLTIEPVASQTLPAVKVPTVEC 277
Cdd:cd21069    2 GKEVDTVLFAEFQAWKESPTLDRSCPFLSRIYREDIGPCLDFTKRELSDLVQSAVENNTLTIEPVASQALPVVKASAVEC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793 278 NNTNTCALSGLARTCHHRIRLGDSDSHYYISPSSRARITAVCNFFTYIRYIQQGLVRQDAEPMFWEIMRLRKGMSLAKLG 357
Cdd:cd21069   82 GGPKKCALSGLSRTCRHRIKLGDSGNYYYISPSCRARITAVCNFFTYIRYIQQGLVRQDAEQMFWEVMRLRREMSLAKLG 161


                 ..
gi 755563793 358 FF 359
Cdd:cd21069  162 FY 163
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 198-359 4.90e-78

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IP lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411032  Cd Length: 193  Bit Score: 237.90  E-value: 4.90e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793 198 SRQVDTTLFAEFQAWRASPTLDKSCPFLERVYREDVGPCLDFTVQELSALVRTAVEDNTLTIEPVASQTLPAVKVPTVEC 277
Cdd:cd21068   29 CKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVLEAVENNTLSIEPVGLQPLRFVKASAVEC 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793 278 NNTNTCALSGLARTCHHRIRLGDSDSHYYISPSSRARITAVCNFFTYIRYIQQGLVR-QDAEPMFWEIMRLRKGMSLAKL 356
Cdd:cd21068  109 GGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQQGLVKqQDVDQMFWEVMQLRKEMSLAKL 188


                 ...
gi 755563793 357 GFF 359
Cdd:cd21068  189 GYY 191
Rab11BD_RAB3IP_like cd21044
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 ...
 201-357 1.12e-53

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 (RAB3IL1) and similar proteins; The family includes RAB3IP and RAB3IL1, as well as Rab guanine nucleotide exchange factor SEC2 from yeast. RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. RAB3IL1, also called guanine nucleotide exchange factor for Rab-3A (GRAB), or Rab3A-interacting-like protein 1, or Rabin3-like 1, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. As a dual Rab-binding protein, RAB3IL1 could potentially link Rab3 and Rab11 and/or Rab8 and Rab11-mediated intracellular trafficking processes. It may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. It may also activate RAB8A and RAB8B. In addition, RAB3IL1 interacts with InsP6K1 and plays a role for InsP7 in vesicle exocytosis. SEC2 is a guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis. SEC2 binds the Rab GTPase YPT32 but does not have exchange activity on YPT32. The model corresponds to the Rab11a/Rab11b-binding region of family members which lies within the carboxy-terminus, a region distinct from their GEF domain and Rab3a-binding region.


Pssm-ID: 411031  Cd Length: 178  Bit Score: 174.86  E-value: 1.12e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793 201 VDTTLFAEFQAWRASP-----TLDKSCPFLERVYREDVGPCLDFTVQELSAL----VRTAVEDNTLTIEPVASQTLPAVK 271
Cdd:cd21044    3 VDLVLFEEFQEFLKAPsslslSLLKSSPFLKRILAEDIEPCLRFDPALLNWLlkkrLLAAILENTLEIEPISGSTETSSS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793 272 ------VPTVECNNTNTCALSGLART--CHHRIRLGDSDSH-YYISPSSRARITAVCNFFTYIRYIQQGLVRQ-DAEPMF 341
Cdd:cd21044   83 snntapVSSPPPASPKKCALCGESRLdaCLYRLRLSDSDSEwYPICSYCRNRLRAVCDFFAYLRYIRQGLVKSrSIEKLY 162

                        170
                 ....*....|....*.
gi 755563793 342 WEIMRLRKGMSLAKLG 357
Cdd:cd21044  163 LEILRLRLRMFLARLG 178
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
 23-91 2.55e-10

GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.


Pssm-ID: 428938 [Multi-domain]  Cd Length: 92  Bit Score: 56.42  E-value: 2.55e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755563793   23 KLKDEECERLC--KVRAQLEQELEELTASLFEEAHKMVREANMKQATSEK-------QLKEAWGKIDMLQAEVTALKT 91
Cdd:pfam06428   1 ELKEEKKKRLEaeKEKKKLEKELEDLTASLFEEANKMVAAARREKHAVEIkndqlkeQLKEKETLLESLQEQLKELKQ 78
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 11-93 9.11e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793  11 LKEELYKAQKELKLKDEECERLCKVRAQLEQELEELTASLfEEAHKMVREANMKQATSEKQLKEAWGKIDMLQAEVTALK 90
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-AALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103


                 ...
gi 755563793  91 TLV 93
Cdd:COG4942  104 EEL 106
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
11-91 9.58e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 9.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793  11 LKEELYKAQKELKLKDEECERLCKVRAQLEQELEELTASLfEEAHKMVREANMKQATSEKQLKEAWGKIDMLQAEVTALK 90
Cdd:COG4372   43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121


                 .
gi 755563793  91 T 91
Cdd:COG4372  122 K 122
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2-105 5.33e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793   2 EIREKGSEF--LKEELYKAQKELKLKDEECERLCKVRAQLEQELEELTASLfEEAHKMVREANMKQATSEKQLKEAWGKI 79
Cdd:COG4372   81 ELEELNEQLqaAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR-KQLEAQIAELQSEIAEREEELKELEEQL 159

                         90       100
                 ....*....|....*....|....*.
gi 755563793  80 DMLQAEVTALKTLVITSTPASPNREL 105
Cdd:COG4372  160 ESLQEELAALEQELQALSEAEAEQAL 185
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
11-91 3.38e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793  11 LKEELYKAQKELKLKDEECERL---CKVRAQLEQELEELTASLFEEAHKMVREANMKQATSEKQLKEAWGKIDMLQAEVT 87
Cdd:COG4717  130 LYQELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209


                 ....
gi 755563793  88 ALKT 91
Cdd:COG4717  210 ELEE 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-90 3.47e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 3.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793     9 EFLKEELYKAQKELKLKDEECERLCKVRAQLEQELEELTASLFEEAHKMVREANMKQATSEKQLKEAWGKIDMLQAEVTA 88
Cdd:TIGR02168  192 EDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271


                   ..
gi 755563793    89 LK 90
Cdd:TIGR02168  272 LR 273
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 11-90 6.97e-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: 35.40  E-value: 6.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563793  11 LKEELYKAQKELKLKDEECERLCKVRAQLEQELEELT-----ASLFEEAHKMVREANMKQATSEKQLKEawgKIDMLQAE 85
Cdd:cd09803    6 LAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPvlkaqAEIYKSDFEAERAAREKLHQEKEQLAE---QLEYLQRE 82


                 ....*
gi 755563793  86 VTALK 90
Cdd:cd09803   83 NQELK 87
 
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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