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Conserved domains on  [gi|922581855|ref|NP_001300405|]
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DH domain-containing protein [Caenorhabditis elegans]

Protein Classification

RhoGEF domain-containing protein( domain architecture ID 1915843)

RhoGEF domain-containing protein contains guanine nucleotide exchange factor (GEF) activity to regulate small GTPases in the Rho family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGEF super family cl02571
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 852-1043 1.38e-16

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


The actual alignment was detected with superfamily member cd00160:

Pssm-ID: 470622 [Multi-domain]  Cd Length: 181  Bit Score: 79.26  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855  852 KQDAIFELYLMEKRHCANIAFLLHGYRRRMLDENI-ITKQDMDVLIPDvLEPLLIFHLNVLERITARMKE-NYEVGTISD 929
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGN-IEEIYEFHRIFLKSLEERVEEwDKSGPRIGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855  930 IISEELAIdggqhtklcCDAYTDFGVAKERSDVLYHHLMNKNAKFAEFfkkTYSEETFYKHYDFRPLITKIIGRATKYSL 1009
Cdd:cd00160    80 VFLKLAPF---------FKIYSEYCSNHPDALELLKKLKKFNKFFQEF---LEKAESECGRLKLESLLLKPVQRLTKYPL 147

                         170       180       190
                  ....*....|....*....|....*....|....
gi 922581855 1010 LLETILKNEQPFSEYHDLTKTALETARKFAHKID 1043
Cdd:cd00160   148 LLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
PH_16 super family cl39325
PH domain;
1095-1211 1.81e-05

PH domain;


The actual alignment was detected with superfamily member pfam17838:

Pssm-ID: 436083  Cd Length: 127  Bit Score: 45.85  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855  1095 TNRKLVHLGEALIKipvnpvgsgggthssssgKQVDKKDQCYIVLFDDIIVILIRKSSRQLIFMQDQG-----------V 1163
Cdd:pfam17838   13 TTRKLIHEGPLTWR------------------NSKGKLVEVHALLLEDILVLLQEKDQKLVLACLSTGsenvdqktqspI 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 922581855  1164 MPVQSLLIR-TAARGHSIMLISGAK--PVLFEISFHTSTDRKKWVTLLELA 1211
Cdd:pfam17838   75 ISLKKLIVReVATDKKAFFLISTSPsdPQMYELHASTKSERNTWTKLIQDA 125
HlpA super family cl34496
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 1540-1591 5.20e-04

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


The actual alignment was detected with superfamily member COG2825:

Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 42.52  E-value: 5.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581855 1540 LRKKEKEIRELQQKVLADR-----DELAEKQKAIDAQEEEIQTKWAALQaRSIEQQQ 1591
Cdd:COG2825    59 LQKLEKELQALQEKLQKEAatlseEERQKKERELQKKQQELQRKQQEAQ-QDLQKRQ 114
 
Name Accession Description Interval E-value
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 852-1043 1.38e-16

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 79.26  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855  852 KQDAIFELYLMEKRHCANIAFLLHGYRRRMLDENI-ITKQDMDVLIPDvLEPLLIFHLNVLERITARMKE-NYEVGTISD 929
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGN-IEEIYEFHRIFLKSLEERVEEwDKSGPRIGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855  930 IISEELAIdggqhtklcCDAYTDFGVAKERSDVLYHHLMNKNAKFAEFfkkTYSEETFYKHYDFRPLITKIIGRATKYSL 1009
Cdd:cd00160    80 VFLKLAPF---------FKIYSEYCSNHPDALELLKKLKKFNKFFQEF---LEKAESECGRLKLESLLLKPVQRLTKYPL 147

                         170       180       190
                  ....*....|....*....|....*....|....
gi 922581855 1010 LLETILKNEQPFSEYHDLTKTALETARKFAHKID 1043
Cdd:cd00160   148 LLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 855-1043 1.51e-14

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 73.49  E-value: 1.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855   855 AIFELYLMEKRHCANIAFLLHGYRRRMLDENIITKQDMDVLIPDvLEPLLIFHLNVLerITARMKENYEVGTISDIIsee 934
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSN-IEEIYELHRQLL--LEELLKEWISIQRIGDIF--- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855   935 LAIDGGQHTklccdaYTDFGVAKERSDVLYHHLMNKNAKFAEFFKKTYSEETFYKhYDFRPLITKIIGRATKYSLLLETI 1014
Cdd:pfam00621   75 LKFAPGFKV------YSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRG-LDLNSFLIKPVQRIPRYPLLLKEL 147

                          170       180
                   ....*....|....*....|....*....
gi 922581855  1015 LKNEQPFSEYHDLTKTALETARKFAHKID 1043
Cdd:pfam00621  148 LKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 855-1043 1.24e-12

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 68.10  E-value: 1.24e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855    855 AIFELYLMEKRHCANIAFLLHGYRRRMLDEN-IITKQDMDVLIPDvLEPLLIFHLNVLERITARMKENYEVG-TISDIIS 932
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELkLLSPNELETLFGN-IEEIYEFHRDFLDELEERIEEWDDSVeRIGDVFL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855    933 EELAIdggqhtklcCDAYTDFGVAKERSDVLYHHLMnKNAKFAEFFKKTYSEETFYKhYDFRPLITKIIGRATKYSLLLE 1012
Cdd:smart00325   80 KLEEF---------FKIYSEYCSNHPDALELLKKLK-KNPRFQKFLKEIESSPQCRR-LTLESLLLKPVQRLTKYPLLLK 148

                           170       180       190
                    ....*....|....*....|....*....|.
gi 922581855   1013 TILKNEQPFSEYHDLTKTALETARKFAHKID 1043
Cdd:smart00325  149 ELLKHTPEDHEDREDLKKALKAIKELANQVN 179
PH_16 pfam17838
PH domain;
1095-1211 1.81e-05

PH domain;


Pssm-ID: 436083  Cd Length: 127  Bit Score: 45.85  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855  1095 TNRKLVHLGEALIKipvnpvgsgggthssssgKQVDKKDQCYIVLFDDIIVILIRKSSRQLIFMQDQG-----------V 1163
Cdd:pfam17838   13 TTRKLIHEGPLTWR------------------NSKGKLVEVHALLLEDILVLLQEKDQKLVLACLSTGsenvdqktqspI 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 922581855  1164 MPVQSLLIR-TAARGHSIMLISGAK--PVLFEISFHTSTDRKKWVTLLELA 1211
Cdd:pfam17838   75 ISLKKLIVReVATDKKAFFLISTSPsdPQMYELHASTKSERNTWTKLIQDA 125
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 1540-1591 5.20e-04

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: 42.52  E-value: 5.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581855 1540 LRKKEKEIRELQQKVLADR-----DELAEKQKAIDAQEEEIQTKWAALQaRSIEQQQ 1591
Cdd:COG2825    59 LQKLEKELQALQEKLQKEAatlseEERQKKERELQKKQQELQRKQQEAQ-QDLQKRQ 114
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1540-1591 5.24e-04

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: 41.80  E-value: 5.24e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581855   1540 LRKKEKEIRELQQKVLADR-----DELAEKQKAIDAQEEEIQTKWAALQARSIEQQQ 1591
Cdd:smart00935   34 LEKLEKELQKLKEKLQKDAatlseAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQ 90
PH_RhoGEF cd13329
Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to ...
 1130-1209 9.77e-03

Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275411  Cd Length: 109  Bit Score: 37.63  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855 1130 DKKDQCYIVLFDDIIVILIRKSSRQLIFMQDQG----------VMPVQSLLIR-TAARGHSIMLISGAK--PVLFEISFH 1196
Cdd:cd13329    14 GKLIEVHVLLLEDLLVLLQKQDDKYLLKLHLTGsfdskdtkspVIKLSTLLVReVATDKKAFFLISTSKngPQMYELVAN 93

                          90
                  ....*....|...
gi 922581855 1197 TSTDRKKWVTLLE 1209
Cdd:cd13329    94 SSSERKTWIKHIS 106
 
Name Accession Description Interval E-value
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 852-1043 1.38e-16

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 79.26  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855  852 KQDAIFELYLMEKRHCANIAFLLHGYRRRMLDENI-ITKQDMDVLIPDvLEPLLIFHLNVLERITARMKE-NYEVGTISD 929
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGN-IEEIYEFHRIFLKSLEERVEEwDKSGPRIGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855  930 IISEELAIdggqhtklcCDAYTDFGVAKERSDVLYHHLMNKNAKFAEFfkkTYSEETFYKHYDFRPLITKIIGRATKYSL 1009
Cdd:cd00160    80 VFLKLAPF---------FKIYSEYCSNHPDALELLKKLKKFNKFFQEF---LEKAESECGRLKLESLLLKPVQRLTKYPL 147

                         170       180       190
                  ....*....|....*....|....*....|....
gi 922581855 1010 LLETILKNEQPFSEYHDLTKTALETARKFAHKID 1043
Cdd:cd00160   148 LLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 855-1043 1.51e-14

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 73.49  E-value: 1.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855   855 AIFELYLMEKRHCANIAFLLHGYRRRMLDENIITKQDMDVLIPDvLEPLLIFHLNVLerITARMKENYEVGTISDIIsee 934
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSN-IEEIYELHRQLL--LEELLKEWISIQRIGDIF--- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855   935 LAIDGGQHTklccdaYTDFGVAKERSDVLYHHLMNKNAKFAEFFKKTYSEETFYKhYDFRPLITKIIGRATKYSLLLETI 1014
Cdd:pfam00621   75 LKFAPGFKV------YSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRG-LDLNSFLIKPVQRIPRYPLLLKEL 147

                          170       180
                   ....*....|....*....|....*....
gi 922581855  1015 LKNEQPFSEYHDLTKTALETARKFAHKID 1043
Cdd:pfam00621  148 LKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 855-1043 1.24e-12

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 68.10  E-value: 1.24e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855    855 AIFELYLMEKRHCANIAFLLHGYRRRMLDEN-IITKQDMDVLIPDvLEPLLIFHLNVLERITARMKENYEVG-TISDIIS 932
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELkLLSPNELETLFGN-IEEIYEFHRDFLDELEERIEEWDDSVeRIGDVFL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855    933 EELAIdggqhtklcCDAYTDFGVAKERSDVLYHHLMnKNAKFAEFFKKTYSEETFYKhYDFRPLITKIIGRATKYSLLLE 1012
Cdd:smart00325   80 KLEEF---------FKIYSEYCSNHPDALELLKKLK-KNPRFQKFLKEIESSPQCRR-LTLESLLLKPVQRLTKYPLLLK 148

                           170       180       190
                    ....*....|....*....|....*....|.
gi 922581855   1013 TILKNEQPFSEYHDLTKTALETARKFAHKID 1043
Cdd:smart00325  149 ELLKHTPEDHEDREDLKKALKAIKELANQVN 179
PH_16 pfam17838
PH domain;
1095-1211 1.81e-05

PH domain;


Pssm-ID: 436083  Cd Length: 127  Bit Score: 45.85  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855  1095 TNRKLVHLGEALIKipvnpvgsgggthssssgKQVDKKDQCYIVLFDDIIVILIRKSSRQLIFMQDQG-----------V 1163
Cdd:pfam17838   13 TTRKLIHEGPLTWR------------------NSKGKLVEVHALLLEDILVLLQEKDQKLVLACLSTGsenvdqktqspI 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 922581855  1164 MPVQSLLIR-TAARGHSIMLISGAK--PVLFEISFHTSTDRKKWVTLLELA 1211
Cdd:pfam17838   75 ISLKKLIVReVATDKKAFFLISTSPsdPQMYELHASTKSERNTWTKLIQDA 125
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 1540-1591 5.20e-04

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: 42.52  E-value: 5.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581855 1540 LRKKEKEIRELQQKVLADR-----DELAEKQKAIDAQEEEIQTKWAALQaRSIEQQQ 1591
Cdd:COG2825    59 LQKLEKELQALQEKLQKEAatlseEERQKKERELQKKQQELQRKQQEAQ-QDLQKRQ 114
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1540-1591 5.24e-04

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: 41.80  E-value: 5.24e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 922581855   1540 LRKKEKEIRELQQKVLADR-----DELAEKQKAIDAQEEEIQTKWAALQARSIEQQQ 1591
Cdd:smart00935   34 LEKLEKELQKLKEKLQKDAatlseAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQ 90
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1515-1591 3.06e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855 1515 LLERVRGGGAMMTSTATAVDD---SMEMLRKKEKEIRELQQKVLADRDELAEKQKAIDAQEEEIQTKWAALQARSIEQQQ 1591
Cdd:COG3883   117 FLDRLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1537-1585 4.30e-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: 40.68  E-value: 4.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 922581855 1537 MEMLRKKEKEIRELQQKVLADRDELAEKQKAIDAQEEEIQTKWAALQAR 1585
Cdd:COG1579   116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
PH_RhoGEF cd13329
Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to ...
 1130-1209 9.77e-03

Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275411  Cd Length: 109  Bit Score: 37.63  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581855 1130 DKKDQCYIVLFDDIIVILIRKSSRQLIFMQDQG----------VMPVQSLLIR-TAARGHSIMLISGAK--PVLFEISFH 1196
Cdd:cd13329    14 GKLIEVHVLLLEDLLVLLQKQDDKYLLKLHLTGsfdskdtkspVIKLSTLLVReVATDKKAFFLISTSKngPQMYELVAN 93

                          90
                  ....*....|...
gi 922581855 1197 TSTDRKKWVTLLE 1209
Cdd:cd13329    94 SSSERKTWIKHIS 106
 
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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