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Conserved domains on  [gi|1907194915|ref|XP_036010501|]
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dynamin-2 isoform X22 [Mus musculus]

Protein Classification

Dynamin_M and PH_dynamin domain-containing protein( domain architecture ID 10470541)

protein containing domains Dynamin_M, PH_dynamin, GED, and PHA03247

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 124-233 4.47e-73

Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle formation. It has an N-terminal GTPase domain, followed by a PH domain, a GTPase effector domain and a C-terminal proline arginine rich domain. Dynamin-like proteins, which are found in metazoa, plants and yeast have the same domain architecture as dynamin, but lack the PH 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: 269958  Cd Length: 112  Bit Score: 225.66  E-value: 4.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 124 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 203
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907194915 204 LRQIELACDSQEDVDSWKASFLRAGVYPEK 233
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 2-106 1.13e-42

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


:

Pssm-ID: 460033  Cd Length: 287  Bit Score: 152.29  E-value: 1.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915   2 TRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLREETERIVTTYIREREGRTKDQILL 81
Cdd:pfam01031 183 IRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRERIKEVVEDLLRERLEPTEKMIRS 262

                          90       100
                  ....*....|....*....|....*
gi 1907194915  82 LIDIEQSYINTNHEDFIGFANAQQR 106
Cdd:pfam01031 263 LIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
253-343 5.67e-32

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 117.23  E-value: 5.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 253 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 332
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1907194915 333 LKEALNIIGDI 343
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 341-440 5.79e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 5.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  341 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 420
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100
                   ....*....|....*....|
gi 1907194915  421 SVFANNDPFSAPPQIPSRPA 440
Cdd:PHA03247  2806 DPPAAVLAPAAALPPAASPA 2825
 
Name Accession Description Interval E-value
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 124-233 4.47e-73

Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle formation. It has an N-terminal GTPase domain, followed by a PH domain, a GTPase effector domain and a C-terminal proline arginine rich domain. Dynamin-like proteins, which are found in metazoa, plants and yeast have the same domain architecture as dynamin, but lack the PH 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: 269958  Cd Length: 112  Bit Score: 225.66  E-value: 4.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 124 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 203
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907194915 204 LRQIELACDSQEDVDSWKASFLRAGVYPEK 233
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 2-106 1.13e-42

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


Pssm-ID: 460033  Cd Length: 287  Bit Score: 152.29  E-value: 1.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915   2 TRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLREETERIVTTYIREREGRTKDQILL 81
Cdd:pfam01031 183 IRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRERIKEVVEDLLRERLEPTEKMIRS 262

                          90       100
                  ....*....|....*....|....*
gi 1907194915  82 LIDIEQSYINTNHEDFIGFANAQQR 106
Cdd:pfam01031 263 LIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
253-343 5.67e-32

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 117.23  E-value: 5.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 253 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 332
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1907194915 333 LKEALNIIGDI 343
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
252-343 7.28e-27

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 103.47  E-value: 7.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  252 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 331
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1907194915  332 ALKEALNIIGDI 343
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 124-227 8.13e-11

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: 58.71  E-value: 8.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  124 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 199
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1907194915  200 VYKDLRQIELACDSQEDVDSWKASFLRA 227
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 124-227 1.04e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 124 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 199
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1907194915 200 VykdlRQIELACDSQEDVDSWKASFLRA 227
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 341-440 5.79e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 5.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  341 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 420
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100
                   ....*....|....*....|
gi 1907194915  421 SVFANNDPFSAPPQIPSRPA 440
Cdd:PHA03247  2806 DPPAAVLAPAAALPPAASPA 2825
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 344-437 3.38e-05

Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated lipase, where is O-glycosylated. This region is composed of biased amino acid composition that is likely to be disordered. The region contains many repeats of an approximately 11 residue degenerate repeat.


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 42.41  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 344 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 421
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 1907194915 422 VFANNDP---FSAPPQIPS 437
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
 
Name Accession Description Interval E-value
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 124-233 4.47e-73

Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle formation. It has an N-terminal GTPase domain, followed by a PH domain, a GTPase effector domain and a C-terminal proline arginine rich domain. Dynamin-like proteins, which are found in metazoa, plants and yeast have the same domain architecture as dynamin, but lack the PH 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: 269958  Cd Length: 112  Bit Score: 225.66  E-value: 4.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 124 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 203
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907194915 204 LRQIELACDSQEDVDSWKASFLRAGVYPEK 233
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 2-106 1.13e-42

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


Pssm-ID: 460033  Cd Length: 287  Bit Score: 152.29  E-value: 1.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915   2 TRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLREETERIVTTYIREREGRTKDQILL 81
Cdd:pfam01031 183 IRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRERIKEVVEDLLRERLEPTEKMIRS 262

                          90       100
                  ....*....|....*....|....*
gi 1907194915  82 LIDIEQSYINTNHEDFIGFANAQQR 106
Cdd:pfam01031 263 LIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
253-343 5.67e-32

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 117.23  E-value: 5.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 253 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 332
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1907194915 333 LKEALNIIGDI 343
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
252-343 7.28e-27

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 103.47  E-value: 7.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  252 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 331
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1907194915  332 ALKEALNIIGDI 343
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 124-227 8.13e-11

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: 58.71  E-value: 8.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  124 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 199
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1907194915  200 VYKDLRQIELACDSQEDVDSWKASFLRA 227
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 124-227 1.04e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 124 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 199
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1907194915 200 VykdlRQIELACDSQEDVDSWKASFLRA 227
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 126-220 1.05e-07

Pleckstrin homology (PH) 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: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 49.46  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 126 RRGWLTINNISLMKGGsKEYWFVLTAESLSWYKDEEEKEKKY--MLPLDN-LKIRDVEKGfmSNKHVFAIFNTEQRNVYk 202
Cdd:cd00821     1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                          90
                  ....*....|....*...
gi 1907194915 203 dlrqieLACDSQEDVDSW 220
Cdd:cd00821    77 ------LQADSEEERQEW 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 341-440 5.79e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 5.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  341 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 420
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100
                   ....*....|....*....|
gi 1907194915  421 SVFANNDPFSAPPQIPSRPA 440
Cdd:PHA03247  2806 DPPAAVLAPAAALPPAASPA 2825
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 344-437 3.38e-05

Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated lipase, where is O-glycosylated. This region is composed of biased amino acid composition that is likely to be disordered. The region contains many repeats of an approximately 11 residue degenerate repeat.


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 42.41  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 344 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 421
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 1907194915 422 VFANNDP---FSAPPQIPS 437
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 124-220 5.75e-05

General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 and the related proteins ARNO (ARF nucleotide-binding site opener)/cytohesin-2 and cytohesin-1 are ARF exchange factors that contain a pleckstrin homology (PH) domain thought to target these proteins to cell membranes through binding polyphosphoinositides. The PH domains of all three proteins exhibit relatively high affinity for PtdIns(3,4,5)P3. Within the Grp1 family, diglycine (2G) and triglycine (3G) splice variants, differing only in the number of glycine residues in the PH domain, strongly influence the affinity and specificity for phosphoinositides. The 2G variants selectively bind PtdIns(3,4,5)P3 with high affinity,the 3G variants bind PtdIns(3,4,5)P3 with about 30-fold lower affinity and require the polybasic region for plasma membrane targeting. These ARF-GEFs share a common, tripartite structure consisting of an N-terminal coiled-coil domain, a central domain with homology to the yeast protein Sec7, a PH domain, and a C-terminal polybasic region. The Sec7 domain is autoinhibited by conserved elements proximal to the PH domain. GRP1 binds to the DNA binding domain of certain nuclear receptors (TRalpha, TRbeta, AR, ER, but not RXR), and can repress thyroid hormone receptor (TR)-mediated transactivation by decreasing TR-complex formation on thyroid hormone response elements. ARNO promotes sequential activation of Arf6, Cdc42 and Rac1 and insulin secretion. Cytohesin acts as a PI 3-kinase effector mediating biological responses including cell spreading and adhesion, chemotaxis, protein trafficking, and cytoskeletal rearrangements, only some of which appear to depend on their ability to activate ARFs. 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: 269954  Cd Length: 119  Bit Score: 42.30  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 124 VIRRGWLtinnisLMKGGS----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKgfMSNKHVFAIFNTEQRN 199
Cdd:cd01252     3 PDREGWL------LKLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907194915 200 VYK------DLRQIE-------LACDSQEDVDSW 220
Cdd:cd01252    75 VIKacktdsDGKVVEgnhtvyrISAASEEERDEW 108
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 367-428 2.19e-04

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 42.80  E-value: 2.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907194915 367 HSPTPQRRPVSSVHPPgrppavrgptPGPPLIPMPVGATSSFSAPPIPSRPG----------PQSVFANNDP 428
Cdd:PHA03418   40 HHPNPQEDPDKNPSPP----------PDPPLTPRPPAQPNGHNKPPVTKQPGgegteedhqaPLAADADDDP 101
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 368-441 4.71e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 42.64  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 368 SPTPQRRPVSSVHPPGRPPAVRGPTPGPP-------LIPMPVGAtssfSAPPIPSRPGPQSVFANNDPfSAPPQIPSRPA 440
Cdd:PHA03321  443 PPPPRARPGSTPACARRARAQRARDAGPEyvdplgaLRRLPAGA----APPPEPAAAPSPATYYTRMG-GGPPRLPPRNR 517


                  .
gi 1907194915 441 R 441
Cdd:PHA03321  518 A 518
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
 313-419 4.78e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 42.52  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 313 MEESAEQAQRRDDMLRMYHALKEALNIIGDI-STSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPP---GRPPAV 388
Cdd:PRK14963  315 LDEQMERFARRSDALSLELALLHALLALGGApSEGVAAVAPPAPAPADLTQRLNRLEKEVRSLRSAPTAAAtaaGAPLPD 394

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907194915 389 RGPTPGPPliPMPVGATSSFSAPPIPSRPGP 419
Cdd:PRK14963  395 FDPRPRGP--PAPEPARSAEAPPLVAPAAAP 423
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 342-441 5.73e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 5.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  342 DISTSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLipmpvGATSSFSAPPIPSRPGPQS 421
Cdd:PHA03307   177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDA-----GASSSDSSSSESSGCGWGP 251

                           90       100
                   ....*....|....*....|
gi 1907194915  422 VFANNDPFSAPPQIPSRPAR 441
Cdd:PHA03307   252 ENECPLPRPAPITLPTRIWE 271
PHA03247 PHA03247
large tegument protein UL36; Provisional
 351-421 5.78e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 5.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  351 PVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPP----------------LIPMPVGATSSFSAPPIP 414
Cdd:PHA03247  2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgagepsgavpqpwlgaLVPGRVAVPRFRVPQPAP 2984


                   ....*..
gi 1907194915  415 SRPGPQS 421
Cdd:PHA03247  2985 SREAPAS 2991
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
351-440 9.32e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 9.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 351 PVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPliPMPVGATssfsAPPIPSrPGPQSVFANNDPFS 430
Cdd:PRK12323  410 PAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPA--AAPAAAA----RPAAAG-PRPVAAAAAAAPAR 482

                          90
                  ....*....|
gi 1907194915 431 APPQIPSRPA 440
Cdd:PRK12323  483 AAPAAAPAPA 492
PHA03247 PHA03247
large tegument protein UL36; Provisional
 344-439 9.65e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 9.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  344 STSTVSTPVPPPVDDTWLQNTSGHSP-------TPQRRPVSSVHPPGRPPAVRGPTPGPPL----IPMPVGATSSFSAPP 412
Cdd:PHA03247  2833 SAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRstesFALPPDQPERPPQPQ 2912

                           90       100
                   ....*....|....*....|....*..
gi 1907194915  413 IPSRPGPQSVFANNDPFSAPPQIPSRP 439
Cdd:PHA03247  2913 APPPPQPQPQPPPPPQPQPPPPPPPRP 2939
PHA03247 PHA03247
large tegument protein UL36; Provisional
 369-440 1.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  369 PTPQRR-------PVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSsfSAPPIPSRPGPQSVFANND-PFSAPPQIPSRPA 440
Cdd:PHA03247   381 PTRKRRsarhaatPFARGPGGDDQTRPAAPVPASVPTPAPTPVPA--SAPPPPATPLPSAEPGSDDgPAPPPERQPPAPA 458
PHA03247 PHA03247
large tegument protein UL36; Provisional
 369-440 1.90e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  369 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLI-----PMPVGATSSFSAPPIPSRPGPQSVFANNDP--------------- 428
Cdd:PHA03247  2592 PPQSARPRAPVDDRGDPRGPAPPSPLPPDThapdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvsrprrarrlg 2671

                           90
                   ....*....|....*.
gi 1907194915  429 ----FSAPPQIPSRPA 440
Cdd:PHA03247  2672 raaqASSPPQRPRRRA 2687
PHA03247 PHA03247
large tegument protein UL36; Provisional
 370-440 2.18e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 2.18e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194915  370 TPQRRPvssvHPPGRPPAV-------RGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPfsAPPQIPSRPA 440
Cdd:PHA03247  2678 SPPQRP----RRRAARPTVgsltslaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP--APPAVPAGPA 2749
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 351-439 3.80e-03

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 38.10  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 351 PVPPPVDDtwlqntsGHSPTPQRRPVSSVHPPGR-------PPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVF 423
Cdd:pfam15240  56 PQPPASDD-------PPGPPPPGGPQQPPPQGGKqkpqgppPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQG 128

                          90
                  ....*....|....*.
gi 1907194915 424 ANNDPFSAPPQIPSRP 439
Cdd:pfam15240 129 GGPPPQGGNQQGPPPP 144
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 124-220 3.83e-03

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. 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: 270068  Cd Length: 104  Bit Score: 36.87  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 124 VIRRGWLTinnislMKGGS-----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGF-MSNKHVFAIFNTEQ 197
Cdd:cd13248     7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                          90       100
                  ....*....|....*....|...
gi 1907194915 198 RNVYkdlrqieLACDSQEDVDSW 220
Cdd:cd13248    81 RTYY-------FAADTAEEMEQW 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
 343-439 4.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 4.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  343 ISTSTVSTPVPP-PVDDTWLQNTSGHSPTPQRRPVSSVHPPGRP-PAVRGPTPGPPLIPMPVG--------------ATS 406
Cdd:PHA03247  2791 LSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAqPTAPPPPPGPPPPSLPLGgsvapggdvrrrppSRS 2870

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907194915  407 SFSAPPIPSRPGPQSVFA-----NNDPFSAPPQIPSRP 439
Cdd:PHA03247  2871 PAAKPAAPARPPVRRLARpavsrSTESFALPPDQPERP 2908
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 339-448 4.99e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 339 IIGDISTSTVSTPVPPPVDDTWL-QNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPG--PPLIPMPVGATSSFSAPPIPS 415
Cdd:PRK07764  662 ASDGGDGWPAKAGGAAPAAPPPApAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAaqPPQAAQGASAPSPAADDPVPL 741

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907194915 416 RPGPQSVFANNDPFSAPPQIPSRPARIPPGIPP 448
Cdd:PRK07764  742 PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774
PHA03247 PHA03247
large tegument protein UL36; Provisional
 364-440 6.39e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 6.39e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194915  364 TSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPsrPGPQSVFANNDPFSAPPQIPSRPA 440
Cdd:PHA03247   399 PGGDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPP--PERQPPAPATEPAPDDPDDATRKA 473
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 349-440 6.50e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.00  E-value: 6.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  349 STPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPM--------------PVGATSSFSAPPIP 414
Cdd:PHA03307    86 STPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlrpvgspgpppaasPPAAGASPAAVASD 165

                           90       100
                   ....*....|....*....|....*..
gi 1907194915  415 SRPGPQ-SVFANNDPFSAPPqiPSRPA 440
Cdd:PHA03307   166 AASSRQaALPLSSPEETARA--PSSPP 190
PHA01929 PHA01929
putative scaffolding protein
 345-440 7.14e-03

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 38.50  E-value: 7.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 345 TSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGP----TPGPPLIPMPVGATSSFSAPPIPSRPGPQ 420
Cdd:PHA01929    1 TTQNEQQLPPGLAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAPqqlaIPTQQPQPVPTSAMTPHVVQQAPAQPAPA 80

                          90       100
                  ....*....|....*....|
gi 1907194915 421 SVFANNDPFSAPPQIPSRPA 440
Cdd:PHA01929   81 APPAAGAALPEALEVPPPPA 100
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 361-440 7.52e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 38.30  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 361 LQNTSGHSP------TPQRRPVS-SVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPP 433
Cdd:PHA02682   73 MQRPSGQSPlapspaCAAPAPACpACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPP 152


                  ....*..
gi 1907194915 434 QIPSRPA 440
Cdd:PHA02682  153 LPTPKPA 159
PHA03247 PHA03247
large tegument protein UL36; Provisional
 344-440 8.26e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.77  E-value: 8.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915  344 STSTVSTPVPPPvddtwlqntsghsPTPQRRP---VSSVHPPGRPPAVRGPTPGPPLIPMPV---------GATSSFSAP 411
Cdd:PHA03247  2694 SLTSLADPPPPP-------------PTPEPAPhalVSATPLPPGPAAARQASPALPAAPAPPavpagpatpGGPARPARP 2760

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907194915  412 PI---PSRPGPQSvfannDPFSAPPQIPSRPA 440
Cdd:PHA03247  2761 PTtagPPAPAPPA-----APAAGPPRRLTRPA 2787
PHA03379 PHA03379
EBNA-3A; Provisional
 344-435 9.25e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 38.50  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 344 STSTVSTPVPPPVDDTW---LQNTSGHSPTP----QRRPVSSVHPPGRPPAV-RGPTPGPPLIPMPVG------------ 403
Cdd:PHA03379  436 SHGSAQVPEPPPVHDLEpgpLHDQHSMAPCPvaqlPPGPLQDLEPGDQLPGVvQDGRPACAPVPAPAGpivrpweaslsq 515

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907194915 404 ----ATSSFSAPPIPSRPGPQSVFANNDPFS-APPQI 435
Cdd:PHA03379  516 vpgvAFAPVMPQPMPVEPVPVPTVALERPVCpAPPLI 552
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
 124-157 9.29e-03

Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the third MyoX PH repeat. PLEKHH3/Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) member 3 is also part of this CD and like MyoX contains a FERM domain, a MyTH4 domain, and a single PH domain. Not much is known about the function of PLEKHH3. 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: 270109  Cd Length: 126  Bit Score: 36.26  E-value: 9.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907194915 124 VIRRGWLTINNISLMKGGS---KEYWFVLTAESLSWY 157
Cdd:cd13297    13 VIERGWLYKEGGKGGARGNltkKKRWFVLTGNSLDYY 49
PHA03378 PHA03378
EBNA-3B; Provisional
 350-439 9.52e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 38.51  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194915 350 TPVPPPvddtwlqntsGHSPTPQRRPVSSVH----PPGRPPAVRGPTPGPPLIPMPVGATSSFSAP---PIPSRPgPQSV 422
Cdd:PHA03378  702 TPMRPP----------AAPPGRAQRPAAATGrarpPAAAPGRARPPAAAPGRARPPAAAPGRARPPaaaPGRARP-PAAA 770

                          90
                  ....*....|....*..
gi 1907194915 423 FANNDPfSAPPQIPSRP 439
Cdd:PHA03378  771 PGAPTP-QPPPQAPPAP 786
 
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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