NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|255683297|ref|NP_766348|]
View 

engulfment and cell motility protein 3 [Mus musculus]

Protein Classification

ELMO_ARM and ELMO_CED12 domain-containing protein( domain architecture ID 10570672)

protein containing domains ELMO_ARM, ELMO_CED12, and PH-like

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ELMO_ARM pfam11841
ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ...
 115-268 5.64e-73

ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ELMO (Elongation and Cell motility) proteins and corresponds to the armadillo repeats domain (ARR). It may play an important role in defining the functions of the ELMO family members and may be functionally linked to the ELMO domain in these proteins, being involved in protein-protein interactions.


:

Pssm-ID: 463369  Cd Length: 154  Bit Score: 233.24  E-value: 5.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  115 TFAQEVISRDGLQKLSTIIENGDDLGEMLALGLRAFLELMEHGVVSWETLSISFVRKVISYVNMNLMDASVQPLALRLLE 194
Cdd:pfam11841   1 TFALEFISRNGLKLLISMVEGGTESGEILAYALTAFVELMDHGIVSWDTLSPSFIKKIASYVNKSAQDASILQRSLAILE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683297  195 SVTLSSPALGQLVKSEVPLDRLLVHLQVMNHQLQTKAMALLTALLQGASPTERKEMLDHLWKKNLRQFIYKNII 268
Cdd:pfam11841  81 SIVLNSSALYQLVEQEVTLESLITHLQSSNQEIQTNAIALINALFLKADDSKRKEIADTLSSKQLRNVILKNII 154
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 534-663 1.55e-58

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 cd13359:

Pssm-ID: 473070 [Multi-domain]  Cd Length: 126  Bit Score: 193.68  E-value: 1.55e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297 534 LIRQQRLLRLCEGMLFRKISSRRRQDKLWFCCLSPNHKVLQYGDVEEGAKPPTLESLPEQLPVADIRALLMGKDCPHVRE 613
Cdd:cd13359    2 LIKQQRLNFLVEGTLFPKYNARGRKDKFWYCRLSPNHKVLHYGDCEESAQPAPLEELPEKLPVADIKALVTGKDCPHMKE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 255683297 614 KGSgkqNKDLYELAFSISYDhgeEEAYLNFIAPSKRDFYLWTDGLSALLG 663
Cdd:cd13359   82 LKK---NKSVASLAFSILYD---SDESLDFVAPNETVFDIWTDGLNALLG 125
ELMO_CED12 pfam04727
ELMO/CED-12 family; This family represents a conserved domain which is found in a number of ...
 292-468 1.06e-52

ELMO/CED-12 family; This family represents a conserved domain which is found in a number of eukaryotic proteins including CED-12, ELMO I and ELMO II. ELMO1 is a component of signalling pathways that regulate phagocytosis and cell migration and is the mammalian orthologue of the C. elegans gene, ced-12. CED-12 is required for the engulfment of dying cells and cell migration. In mammalian cells, ELMO1 interacts with Dock180 as part of the CrkII/Dock180/Rac pathway responsible for phagocytosis and cell migration. ELMO1 is ubiquitously expressed, although its expression is highest in the spleen, an organ rich in immune cells. ELMO1 has a PH domain and a polyproline sequence motif at its C terminus which are not present in this alignment.


:

Pssm-ID: 461411  Cd Length: 161  Bit Score: 179.34  E-value: 1.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  292 LLEPRMRTPLDPYSQEQRDQLQALRQAAFEPEGESlgtglsadrrrSLCVREFRKLGFSNSNPAQDLErvPPGLLALDNM 371
Cdd:pfam04727   2 LLRKRRKTPFDSENPEHERLLKELWKALFPDEPLE-----------SRISEKWKRLGFQGEDPATDFR--GMGLLGLENL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  372 LYFSRHAPSAYSRFVLENSSREDkhECPFARSSIQLTALLCELLRVGEPCSETAQdfSPMFFSQDHSFHELFCVAIQLLN 451
Cdd:pfam04727  69 LYFARNHPDSFQKILLEQSHRPQ--RYPFAVASINLTSLLYELLKIGKLDPEENK--SYLFFPLLLAFEELYCAAFQLFD 144

                         170
                  ....*....|....*..
gi 255683297  452 KTWKEMRATQEDFDKVM 468
Cdd:pfam04727 145 RTWKEMGATIMDFNKVL 161
 
Name Accession Description Interval E-value
ELMO_ARM pfam11841
ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ...
 115-268 5.64e-73

ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ELMO (Elongation and Cell motility) proteins and corresponds to the armadillo repeats domain (ARR). It may play an important role in defining the functions of the ELMO family members and may be functionally linked to the ELMO domain in these proteins, being involved in protein-protein interactions.


Pssm-ID: 463369  Cd Length: 154  Bit Score: 233.24  E-value: 5.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  115 TFAQEVISRDGLQKLSTIIENGDDLGEMLALGLRAFLELMEHGVVSWETLSISFVRKVISYVNMNLMDASVQPLALRLLE 194
Cdd:pfam11841   1 TFALEFISRNGLKLLISMVEGGTESGEILAYALTAFVELMDHGIVSWDTLSPSFIKKIASYVNKSAQDASILQRSLAILE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683297  195 SVTLSSPALGQLVKSEVPLDRLLVHLQVMNHQLQTKAMALLTALLQGASPTERKEMLDHLWKKNLRQFIYKNII 268
Cdd:pfam11841  81 SIVLNSSALYQLVEQEVTLESLITHLQSSNQEIQTNAIALINALFLKADDSKRKEIADTLSSKQLRNVILKNII 154
PH_ELMO1_CED-12 cd13359
Engulfment and cell motility protein 1 pleckstrin homology (PH) domain; DOCK2 (Dedicator of ...
 534-663 1.55e-58

Engulfment and cell motility protein 1 pleckstrin homology (PH) domain; DOCK2 (Dedicator of cytokinesis 2), a hematopoietic cell-specific, atypical GEF, controls lymphocyte migration through Rac activation. A DOCK2-ELMO1 complex s necessary for DOCK2-mediated Rac signaling. DOCK2 contains a SH3 domain at its N-terminus, followed by a lipid binding DHR1 domain, and a Rac-binding DHR2 domain at its C-terminus. ELMO1, a mammalian homolog of C. elegans CED-12, contains the N-terminal RhoG-binding region, the ELMO domain, the PH domain, and the C-terminal sequence with three PxxP motifs. The C-terminal region of ELMO1, including the Pro-rich sequence, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle along with the PH domain of ELMO1. Autoinhibition of ELMO1 and DOCK2 is accomplished by the interactions of the EID and EAD domains and SH3 and DHR2 domains, respectively. The interaction of DOCK2 and ELMO1 mutually relieve their autoinhibition and results in the activation of Rac1. The PH domain of ELMO1 does not bind phosphoinositides due to the absence of key binding residues. It more closely resembles the FERM domain rather than other PH domains. 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: 270166 [Multi-domain]  Cd Length: 126  Bit Score: 193.68  E-value: 1.55e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297 534 LIRQQRLLRLCEGMLFRKISSRRRQDKLWFCCLSPNHKVLQYGDVEEGAKPPTLESLPEQLPVADIRALLMGKDCPHVRE 613
Cdd:cd13359    2 LIKQQRLNFLVEGTLFPKYNARGRKDKFWYCRLSPNHKVLHYGDCEESAQPAPLEELPEKLPVADIKALVTGKDCPHMKE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 255683297 614 KGSgkqNKDLYELAFSISYDhgeEEAYLNFIAPSKRDFYLWTDGLSALLG 663
Cdd:cd13359   82 LKK---NKSVASLAFSILYD---SDESLDFVAPNETVFDIWTDGLNALLG 125
ELMO_CED12 pfam04727
ELMO/CED-12 family; This family represents a conserved domain which is found in a number of ...
 292-468 1.06e-52

ELMO/CED-12 family; This family represents a conserved domain which is found in a number of eukaryotic proteins including CED-12, ELMO I and ELMO II. ELMO1 is a component of signalling pathways that regulate phagocytosis and cell migration and is the mammalian orthologue of the C. elegans gene, ced-12. CED-12 is required for the engulfment of dying cells and cell migration. In mammalian cells, ELMO1 interacts with Dock180 as part of the CrkII/Dock180/Rac pathway responsible for phagocytosis and cell migration. ELMO1 is ubiquitously expressed, although its expression is highest in the spleen, an organ rich in immune cells. ELMO1 has a PH domain and a polyproline sequence motif at its C terminus which are not present in this alignment.


Pssm-ID: 461411  Cd Length: 161  Bit Score: 179.34  E-value: 1.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  292 LLEPRMRTPLDPYSQEQRDQLQALRQAAFEPEGESlgtglsadrrrSLCVREFRKLGFSNSNPAQDLErvPPGLLALDNM 371
Cdd:pfam04727   2 LLRKRRKTPFDSENPEHERLLKELWKALFPDEPLE-----------SRISEKWKRLGFQGEDPATDFR--GMGLLGLENL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  372 LYFSRHAPSAYSRFVLENSSREDkhECPFARSSIQLTALLCELLRVGEPCSETAQdfSPMFFSQDHSFHELFCVAIQLLN 451
Cdd:pfam04727  69 LYFARNHPDSFQKILLEQSHRPQ--RYPFAVASINLTSLLYELLKIGKLDPEENK--SYLFFPLLLAFEELYCAAFQLFD 144

                         170
                  ....*....|....*..
gi 255683297  452 KTWKEMRATQEDFDKVM 468
Cdd:pfam04727 145 RTWKEMGATIMDFNKVL 161
PH_12 pfam16457
Pleckstrin homology domain;
535-663 5.75e-48

Pleckstrin homology domain;


Pssm-ID: 465123 [Multi-domain]  Cd Length: 128  Bit Score: 165.12  E-value: 5.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  535 IRQQRLLRLCEGMLFRKISSRRRQDKLWFCCLSPNHKVLQYGDVEEG-AKPPTLESLPEQLPVADIRALLMGKDCPHVRE 613
Cdd:pfam16457   1 VKEQRLNCLLEGAWFPKVRGRRRKKKYRFCRLSPNRKVLHYGDFEEKpTVDPSLESLPEKIDLSDIKEVVTGKECPHVRE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 255683297  614 KGSgKQNKDLYELAFSISYDHGEEEaYLNFIAPSKRDFYLWTDGLSALLG 663
Cdd:pfam16457  81 SGK-KSKKTSSTLAFSLIYGADEYE-LLDFVAPSESVAAIWLDGLNMLLG 128
 
Name Accession Description Interval E-value
ELMO_ARM pfam11841
ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ...
 115-268 5.64e-73

ELMO, armadillo-like helical domain; This domain is found in eukaryotes and predominantly in ELMO (Elongation and Cell motility) proteins and corresponds to the armadillo repeats domain (ARR). It may play an important role in defining the functions of the ELMO family members and may be functionally linked to the ELMO domain in these proteins, being involved in protein-protein interactions.


Pssm-ID: 463369  Cd Length: 154  Bit Score: 233.24  E-value: 5.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  115 TFAQEVISRDGLQKLSTIIENGDDLGEMLALGLRAFLELMEHGVVSWETLSISFVRKVISYVNMNLMDASVQPLALRLLE 194
Cdd:pfam11841   1 TFALEFISRNGLKLLISMVEGGTESGEILAYALTAFVELMDHGIVSWDTLSPSFIKKIASYVNKSAQDASILQRSLAILE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683297  195 SVTLSSPALGQLVKSEVPLDRLLVHLQVMNHQLQTKAMALLTALLQGASPTERKEMLDHLWKKNLRQFIYKNII 268
Cdd:pfam11841  81 SIVLNSSALYQLVEQEVTLESLITHLQSSNQEIQTNAIALINALFLKADDSKRKEIADTLSSKQLRNVILKNII 154
PH_ELMO1_CED-12 cd13359
Engulfment and cell motility protein 1 pleckstrin homology (PH) domain; DOCK2 (Dedicator of ...
 534-663 1.55e-58

Engulfment and cell motility protein 1 pleckstrin homology (PH) domain; DOCK2 (Dedicator of cytokinesis 2), a hematopoietic cell-specific, atypical GEF, controls lymphocyte migration through Rac activation. A DOCK2-ELMO1 complex s necessary for DOCK2-mediated Rac signaling. DOCK2 contains a SH3 domain at its N-terminus, followed by a lipid binding DHR1 domain, and a Rac-binding DHR2 domain at its C-terminus. ELMO1, a mammalian homolog of C. elegans CED-12, contains the N-terminal RhoG-binding region, the ELMO domain, the PH domain, and the C-terminal sequence with three PxxP motifs. The C-terminal region of ELMO1, including the Pro-rich sequence, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle along with the PH domain of ELMO1. Autoinhibition of ELMO1 and DOCK2 is accomplished by the interactions of the EID and EAD domains and SH3 and DHR2 domains, respectively. The interaction of DOCK2 and ELMO1 mutually relieve their autoinhibition and results in the activation of Rac1. The PH domain of ELMO1 does not bind phosphoinositides due to the absence of key binding residues. It more closely resembles the FERM domain rather than other PH domains. 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: 270166 [Multi-domain]  Cd Length: 126  Bit Score: 193.68  E-value: 1.55e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297 534 LIRQQRLLRLCEGMLFRKISSRRRQDKLWFCCLSPNHKVLQYGDVEEGAKPPTLESLPEQLPVADIRALLMGKDCPHVRE 613
Cdd:cd13359    2 LIKQQRLNFLVEGTLFPKYNARGRKDKFWYCRLSPNHKVLHYGDCEESAQPAPLEELPEKLPVADIKALVTGKDCPHMKE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 255683297 614 KGSgkqNKDLYELAFSISYDhgeEEAYLNFIAPSKRDFYLWTDGLSALLG 663
Cdd:cd13359   82 LKK---NKSVASLAFSILYD---SDESLDFVAPNETVFDIWTDGLNALLG 125
ELMO_CED12 pfam04727
ELMO/CED-12 family; This family represents a conserved domain which is found in a number of ...
 292-468 1.06e-52

ELMO/CED-12 family; This family represents a conserved domain which is found in a number of eukaryotic proteins including CED-12, ELMO I and ELMO II. ELMO1 is a component of signalling pathways that regulate phagocytosis and cell migration and is the mammalian orthologue of the C. elegans gene, ced-12. CED-12 is required for the engulfment of dying cells and cell migration. In mammalian cells, ELMO1 interacts with Dock180 as part of the CrkII/Dock180/Rac pathway responsible for phagocytosis and cell migration. ELMO1 is ubiquitously expressed, although its expression is highest in the spleen, an organ rich in immune cells. ELMO1 has a PH domain and a polyproline sequence motif at its C terminus which are not present in this alignment.


Pssm-ID: 461411  Cd Length: 161  Bit Score: 179.34  E-value: 1.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  292 LLEPRMRTPLDPYSQEQRDQLQALRQAAFEPEGESlgtglsadrrrSLCVREFRKLGFSNSNPAQDLErvPPGLLALDNM 371
Cdd:pfam04727   2 LLRKRRKTPFDSENPEHERLLKELWKALFPDEPLE-----------SRISEKWKRLGFQGEDPATDFR--GMGLLGLENL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  372 LYFSRHAPSAYSRFVLENSSREDkhECPFARSSIQLTALLCELLRVGEPCSETAQdfSPMFFSQDHSFHELFCVAIQLLN 451
Cdd:pfam04727  69 LYFARNHPDSFQKILLEQSHRPQ--RYPFAVASINLTSLLYELLKIGKLDPEENK--SYLFFPLLLAFEELYCAAFQLFD 144

                         170
                  ....*....|....*..
gi 255683297  452 KTWKEMRATQEDFDKVM 468
Cdd:pfam04727 145 RTWKEMGATIMDFNKVL 161
PH_12 pfam16457
Pleckstrin homology domain;
535-663 5.75e-48

Pleckstrin homology domain;


Pssm-ID: 465123 [Multi-domain]  Cd Length: 128  Bit Score: 165.12  E-value: 5.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297  535 IRQQRLLRLCEGMLFRKISSRRRQDKLWFCCLSPNHKVLQYGDVEEG-AKPPTLESLPEQLPVADIRALLMGKDCPHVRE 613
Cdd:pfam16457   1 VKEQRLNCLLEGAWFPKVRGRRRKKKYRFCRLSPNRKVLHYGDFEEKpTVDPSLESLPEKIDLSDIKEVVTGKECPHVRE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 255683297  614 KGSgKQNKDLYELAFSISYDHGEEEaYLNFIAPSKRDFYLWTDGLSALLG 663
Cdd:pfam16457  81 SGK-KSKKTSSTLAFSLIYGADEYE-LLDFVAPSESVAAIWLDGLNMLLG 128
PH_PLC_ELMO1 cd01248
Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The ...
 543-662 7.26e-19

Phospholipase C and Engulfment and cell motility protein 1 pleckstrin homology domain; The C-terminal region of ELMO1, the PH domain and Pro-rich sequences, binds the SH3-containing region of DOCK2 forming a intermolecular five-helix bundle allowing for DOCK mediated Rac1 activation. ELMO1, a mammalian homolog of C. elegans CED-12, contains an N-terminal RhoG-binding region, a ELMO domain, a PH domain, and a C-terminal sequence with three PxxP motifs. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). All PLCs, except for PLCzeta, have a PH domain which is for most part N-terminally located, though lipid binding specificity is not conserved between them. In addition PLC gamma contains a split PH domain within its catalytic domain that is separated by 2 SH2 domains and a single SH3 domain. 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: 269952  Cd Length: 108  Bit Score: 82.37  E-value: 7.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683297 543 LCEGMLFRKISSRRRqDKLWFCCLSPNHKVLQYgdveegaKPPTLESLPEQLPVADIRALLMGKDCPHVREKGSGKQNKD 622
Cdd:cd01248    1 LQQGTLLLKYREGSK-PKERTFYLDPDGTRITW-------ESSKKKSEKKSIDISDIKEIRPGKDTDGFKRKKKSNKPKE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 255683297 623 lyELAFSISYdhGEEEAYLNFIAPSKRDFYLWTDGLSALL 662
Cdd:cd01248   73 --ERCFSIIY--GSNNKTLDLVAPSEDEANLWVEGLRALL 108
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH