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Conserved domains on  [gi|25151215|ref|NP_741737|]
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DH domain-containing protein [Caenorhabditis elegans]

Protein Classification

rho guanine nucleotide exchange factor( domain architecture ID 10069502)

rho guanine nucleotide exchange factor containing a pleckstrin homology (PH) domain, similar to Mus musculus transforming protein Mcf-2 (Dbl)

CATH:  2.30.29.30|1.20.900.10
Gene Ontology:  GO:0005085|GO:0051056|GO:0005515
PubMed:  22728242|11738596
SCOP:  4002395|4001108

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 67-242 2.94e-35

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: 129.34  E-value: 2.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215  67 TNAFDEMIATEISYVADLKDIIIHYLEPFEATENQNSlpdtlRGKPDCLFGNVRELYKFHHRtVLEDLVAARSTAE---- 142
Cdd:cd00160   2 QEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLS-----PEEVELLFGNIEEIYEFHRI-FLKSLEERVEEWDksgp 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215 143 -MCRVLMQHRNQIYVtYRTYCQIHGSNQKVRDSVKNH-PFFKECQRNAN---HNMDMSSYLLKPIQRIMKYQLLLGNIMD 217
Cdd:cd00160  76 rIGDVFLKLAPFFKI-YSEYCSNHPDALELLKKLKKFnKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                       170       180
                ....*....|....*....|....*..
gi 25151215 218 DCPA--DVRDEVAMTRDSMVELLNQID 242
Cdd:cd00160 155 HTPDghEDREDLKKALEAIKEVASQVN 181
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 250-377 1.94e-14

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd01227:

Pssm-ID: 473070 [Multi-domain]  Cd Length: 126  Bit Score: 69.92  E-value: 1.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215 250 ISGYNGDLKSLGLLRLQTECDVFTYNRKKKAKLSRAQK---RFIFFFDGAVMFCKKRVSNpgttlnSEPEYFEHKFCIPI 326
Cdd:cd01227   2 ITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTKKLARFKpmqRHIFLYEKAVLFCKKRGEN------GEAPSYSYKNSLNT 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 25151215 327 ISLGYDTSSRTGASRFEVWDDAKTDAYVIETIDQTARTKWIQRLGKSETAQ 377
Cdd:cd01227  76 TAVGLTENVKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
 
Name Accession Description Interval E-value
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 67-242 2.94e-35

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: 129.34  E-value: 2.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215  67 TNAFDEMIATEISYVADLKDIIIHYLEPFEATENQNSlpdtlRGKPDCLFGNVRELYKFHHRtVLEDLVAARSTAE---- 142
Cdd:cd00160   2 QEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLS-----PEEVELLFGNIEEIYEFHRI-FLKSLEERVEEWDksgp 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215 143 -MCRVLMQHRNQIYVtYRTYCQIHGSNQKVRDSVKNH-PFFKECQRNAN---HNMDMSSYLLKPIQRIMKYQLLLGNIMD 217
Cdd:cd00160  76 rIGDVFLKLAPFFKI-YSEYCSNHPDALELLKKLKKFnKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                       170       180
                ....*....|....*....|....*..
gi 25151215 218 DCPA--DVRDEVAMTRDSMVELLNQID 242
Cdd:cd00160 155 HTPDghEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 69-243 4.93e-32

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: 120.48  E-value: 4.93e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215     69 AFDEMIATEISYVADLKDIIIHYLEPFeatenQNSLPDTLRGKPDCLFGNVRELYKFHhRTVLEDLVAARSTAE-----M 143
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPL-----KKELKLLSPNELETLFGNIEEIYEFH-RDFLDELEERIEEWDdsverI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215    144 CRVLMQHRNQIYVtYRTYCQIHGSNQKVRDSVKNHPFF----KECQRNANHN-MDMSSYLLKPIQRIMKYQLLLGNIMDD 218
Cdd:smart00325  75 GDVFLKLEEFFKI-YSEYCSNHPDALELLKKLKKNPRFqkflKEIESSPQCRrLTLESLLLKPVQRLTKYPLLLKELLKH 153

                          170       180
                   ....*....|....*....|....*..
gi 25151215    219 CPAD--VRDEVAMTRDSMVELLNQIDA 243
Cdd:smart00325 154 TPEDheDREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 72-242 3.91e-25

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: 101.61  E-value: 3.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215    72 EMIATEISYVADLKDIIIHYLEPFEatenqnslpDTLRGKPDC---LFGNVRELYKFHHRTVLEDLVAARSTAEMCRVLM 148
Cdd:pfam00621   4 ELLQTERSYVRDLEILVEVFLPPNS---------KPLSESEEEiktIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215   149 QHRNQIYVTYRTYCQIHGS-----NQKVRDSVKNHPFFKECQRNAN-HNMDMSSYLLKPIQRIMKYQLLLGNIMDDCPAD 222
Cdd:pfam00621  75 LKFAPGFKVYSTYCSNYPKalkllKKLLKKNPKFRAFLEELEANPEcRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPD 154

                         170       180
                  ....*....|....*....|..
gi 25151215   223 VRDEVAMTR--DSMVELLNQID 242
Cdd:pfam00621 155 HPDYEDLKKalEAIKEVAKQIN 176
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 250-377 1.94e-14

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. 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: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 69.92  E-value: 1.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215 250 ISGYNGDLKSLGLLRLQTECDVFTYNRKKKAKLSRAQK---RFIFFFDGAVMFCKKRVSNpgttlnSEPEYFEHKFCIPI 326
Cdd:cd01227   2 ITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTKKLARFKpmqRHIFLYEKAVLFCKKRGEN------GEAPSYSYKNSLNT 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 25151215 327 ISLGYDTSSRTGASRFEVWDDAKTDAYVIETIDQTARTKWIQRLGKSETAQ 377
Cdd:cd01227  76 TAVGLTENVKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 276-370 3.93e-03

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 36.76  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215    276 RKKKAKLSRAQKRFIFFFDGAVMFCKKRVSNPGTTlnsepeyfeHKFCIPI----ISLGYDTSSRTGASRFEVW-DDAKT 350
Cdd:smart00233   9 KKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYK---------PKGSIDLsgctVREAPDPDSSKKPHCFEIKtSDRKT 79

                           90       100
                   ....*....|....*....|
gi 25151215    351 daYVIETIDQTARTKWIQRL 370
Cdd:smart00233  80 --LLLQAESEEEREKWVEAL 97
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 276-370 8.99e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 36.00  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215   276 RKKKAKLSRAQKRFIFFFDGAVMFCKKRvsnpgttlnSEPEYFEHKFCIPIISLGY----DTSSRTGASRFEVW--DDAK 349
Cdd:pfam00169   9 KKGGGKKKSWKKRYFVLFDGSLLYYKDD---------KSGKSKEPKGSISLSGCEVvevvASDSPKRKFCFELRtgERTG 79

                          90       100
                  ....*....|....*....|.
gi 25151215   350 TDAYVIETIDQTARTKWIQRL 370
Cdd:pfam00169  80 KRTYLLQAESEEERKDWIKAI 100
 
Name Accession Description Interval E-value
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 67-242 2.94e-35

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: 129.34  E-value: 2.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215  67 TNAFDEMIATEISYVADLKDIIIHYLEPFEATENQNSlpdtlRGKPDCLFGNVRELYKFHHRtVLEDLVAARSTAE---- 142
Cdd:cd00160   2 QEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLPLS-----PEEVELLFGNIEEIYEFHRI-FLKSLEERVEEWDksgp 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215 143 -MCRVLMQHRNQIYVtYRTYCQIHGSNQKVRDSVKNH-PFFKECQRNAN---HNMDMSSYLLKPIQRIMKYQLLLGNIMD 217
Cdd:cd00160  76 rIGDVFLKLAPFFKI-YSEYCSNHPDALELLKKLKKFnKFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLK 154

                       170       180
                ....*....|....*....|....*..
gi 25151215 218 DCPA--DVRDEVAMTRDSMVELLNQID 242
Cdd:cd00160 155 HTPDghEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 69-243 4.93e-32

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: 120.48  E-value: 4.93e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215     69 AFDEMIATEISYVADLKDIIIHYLEPFeatenQNSLPDTLRGKPDCLFGNVRELYKFHhRTVLEDLVAARSTAE-----M 143
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPL-----KKELKLLSPNELETLFGNIEEIYEFH-RDFLDELEERIEEWDdsverI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215    144 CRVLMQHRNQIYVtYRTYCQIHGSNQKVRDSVKNHPFF----KECQRNANHN-MDMSSYLLKPIQRIMKYQLLLGNIMDD 218
Cdd:smart00325  75 GDVFLKLEEFFKI-YSEYCSNHPDALELLKKLKKNPRFqkflKEIESSPQCRrLTLESLLLKPVQRLTKYPLLLKELLKH 153

                          170       180
                   ....*....|....*....|....*..
gi 25151215    219 CPAD--VRDEVAMTRDSMVELLNQIDA 243
Cdd:smart00325 154 TPEDheDREDLKKALKAIKELANQVNE 180
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 72-242 3.91e-25

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: 101.61  E-value: 3.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215    72 EMIATEISYVADLKDIIIHYLEPFEatenqnslpDTLRGKPDC---LFGNVRELYKFHHRTVLEDLVAARSTAEMCRVLM 148
Cdd:pfam00621   4 ELLQTERSYVRDLEILVEVFLPPNS---------KPLSESEEEiktIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215   149 QHRNQIYVTYRTYCQIHGS-----NQKVRDSVKNHPFFKECQRNAN-HNMDMSSYLLKPIQRIMKYQLLLGNIMDDCPAD 222
Cdd:pfam00621  75 LKFAPGFKVYSTYCSNYPKalkllKKLLKKNPKFRAFLEELEANPEcRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPD 154

                         170       180
                  ....*....|....*....|..
gi 25151215   223 VRDEVAMTR--DSMVELLNQID 242
Cdd:pfam00621 155 HPDYEDLKKalEAIKEVAKQIN 176
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
 250-377 1.94e-14

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. 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: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 69.92  E-value: 1.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215 250 ISGYNGDLKSLGLLRLQTECDVFTYNRKKKAKLSRAQK---RFIFFFDGAVMFCKKRVSNpgttlnSEPEYFEHKFCIPI 326
Cdd:cd01227   2 ITGYDGNLGDLGKLLMQGSFNVWTEHKKGHTKKLARFKpmqRHIFLYEKAVLFCKKRGEN------GEAPSYSYKNSLNT 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 25151215 327 ISLGYDTSSRTGASRFEVWDDAKTDAYVIETIDQTARTKWIQRLGKSETAQ 377
Cdd:cd01227  76 TAVGLTENVKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 276-370 3.93e-03

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 36.76  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215    276 RKKKAKLSRAQKRFIFFFDGAVMFCKKRVSNPGTTlnsepeyfeHKFCIPI----ISLGYDTSSRTGASRFEVW-DDAKT 350
Cdd:smart00233   9 KKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYK---------PKGSIDLsgctVREAPDPDSSKKPHCFEIKtSDRKT 79

                           90       100
                   ....*....|....*....|
gi 25151215    351 daYVIETIDQTARTKWIQRL 370
Cdd:smart00233  80 --LLLQAESEEEREKWVEAL 97
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 276-370 8.99e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 36.00  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151215   276 RKKKAKLSRAQKRFIFFFDGAVMFCKKRvsnpgttlnSEPEYFEHKFCIPIISLGY----DTSSRTGASRFEVW--DDAK 349
Cdd:pfam00169   9 KKGGGKKKSWKKRYFVLFDGSLLYYKDD---------KSGKSKEPKGSISLSGCEVvevvASDSPKRKFCFELRtgERTG 79

                          90       100
                  ....*....|....*....|.
gi 25151215   350 TDAYVIETIDQTARTKWIQRL 370
Cdd:pfam00169  80 KRTYLLQAESEEERKDWIKAI 100
 
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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