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Conserved domains on  [gi|1907194905|ref|XP_036010498|]
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dynamin-2 isoform X19 [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 5.67e-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: 5.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 124 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 203
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907194905 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 ...
 1-92 1.95e-37

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: 138.42  E-value: 1.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905   1 MAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYI 80
Cdd:pfam01031 192 KAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYI 271

                          90
                  ....*....|..
gi 1907194905  81 NTNHEDFIGFAN 92
Cdd:pfam01031 272 NTNHPDFIGGLN 283
GED pfam02212
Dynamin GTPase effector domain;
253-343 5.41e-32

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 117.61  E-value: 5.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 253 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 332
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1907194905 333 LKEALNIIGDI 343
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 341-472 1.83e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.17  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  341 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 420
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907194905  421 SVfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTiiRPAEPSL 472
Cdd:PHA03247  2806 DP-----PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSL 2850
 
Name Accession Description Interval E-value
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 124-233 5.67e-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: 5.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 124 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 203
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907194905 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 ...
 1-92 1.95e-37

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: 138.42  E-value: 1.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905   1 MAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYI 80
Cdd:pfam01031 192 KAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYI 271

                          90
                  ....*....|..
gi 1907194905  81 NTNHEDFIGFAN 92
Cdd:pfam01031 272 NTNHPDFIGGLN 283
GED pfam02212
Dynamin GTPase effector domain;
253-343 5.41e-32

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 117.61  E-value: 5.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 253 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 332
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1907194905 333 LKEALNIIGDI 343
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
252-343 8.00e-27

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 103.47  E-value: 8.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  252 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 331
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1907194905  332 ALKEALNIIGDI 343
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 124-227 8.01e-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: 8.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  124 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 199
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1907194905  200 VYKDLRQIELACDSQEDVDSWKASFLRA 227
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 124-227 1.02e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 124 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 199
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1907194905 200 VykdlRQIELACDSQEDVDSWKASFLRA 227
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 341-472 1.83e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.17  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  341 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 420
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907194905  421 SVfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTiiRPAEPSL 472
Cdd:PHA03247  2806 DP-----PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSL 2850
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 344-437 2.06e-04

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: 40.10  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 344 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 421
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 1907194905 422 VFANNDP---FSAPPQIPS 437
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 366-473 7.69e-03

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 37.36  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 366 GHSPTPQRRPVSSVHPPGRPPAVRGP--TPGPPLIPMPVGATSSFSAPPI--------PSRPGPQSVFANNDPFSAP-PQ 434
Cdd:cd21975    20 GVRPDPEGAGLAAGLDVRATREVAKGpgPPGPAWKPDGADSPGLVTAAPHllaanvlaPLRGPSVEGSSLESGDADMgSD 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907194905 435 IPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLL 473
Cdd:cd21975   100 SDVAPASGAAASTSPESSSDAASSPSPLSLLHPGEAGLE 138
 
Name Accession Description Interval E-value
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 124-233 5.67e-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: 5.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 124 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 203
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907194905 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 ...
 1-92 1.95e-37

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: 138.42  E-value: 1.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905   1 MAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYI 80
Cdd:pfam01031 192 KAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYI 271

                          90
                  ....*....|..
gi 1907194905  81 NTNHEDFIGFAN 92
Cdd:pfam01031 272 NTNHPDFIGGLN 283
GED pfam02212
Dynamin GTPase effector domain;
253-343 5.41e-32

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 117.61  E-value: 5.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 253 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 332
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1907194905 333 LKEALNIIGDI 343
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
252-343 8.00e-27

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 103.47  E-value: 8.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  252 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 331
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1907194905  332 ALKEALNIIGDI 343
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 124-227 8.01e-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: 8.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  124 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 199
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1907194905  200 VYKDLRQIELACDSQEDVDSWKASFLRA 227
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 124-227 1.02e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 124 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 199
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1907194905 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 1.08e-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: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 126 RRGWLTINNISLMKGGsKEYWFVLTAESLSWYKDEEEKEKKY--MLPLDN-LKIRDVEKGfmSNKHVFAIFNTEQRNVYk 202
Cdd:cd00821     1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                          90
                  ....*....|....*...
gi 1907194905 203 dlrqieLACDSQEDVDSW 220
Cdd:cd00821    77 ------LQADSEEERQEW 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 341-472 1.83e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.17  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  341 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 420
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907194905  421 SVfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTiiRPAEPSL 472
Cdd:PHA03247  2806 DP-----PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSL 2850
PHA03247 PHA03247
large tegument protein UL36; Provisional
 344-471 3.88e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  344 STSTVSTPVPPPvddtwlqntsghsPTPQRRP---VSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRP--- 417
Cdd:PHA03247  2694 SLTSLADPPPPP-------------PTPEPAPhalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARParp 2760

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194905  418 ----GPQSVFANNDPFSAPPQIPSRPArippgippgvpsrRAPAAPSRPTIIRPAEPS 471
Cdd:PHA03247  2761 pttaGPPAPAPPAAPAAGPPRRLTRPA-------------VASLSESRESLPSPWDPA 2805
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 349-470 6.66e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 48.56  E-value: 6.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 349 STPVPPPvddtwlQNTSGHSPTPQRRPVSSVHPPgrPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDP 428
Cdd:PRK14951  379 KTPARPE------AAAPAAAPVAQAAAAPAPAAA--PAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPA 450

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907194905 429 FSAPPQIPSRPARIPPGIPPGVPSRR-APAAPSRPTIIRPAEP 470
Cdd:PRK14951  451 PPAQAAPETVAIPVRVAPEPAVASAApAPAAAPAAARLTPTEE 493
PHA03247 PHA03247
large tegument protein UL36; Provisional
 344-471 8.84e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 8.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  344 STSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPM--PVGATSSFSAPPIPSRPGPqs 421
Cdd:PHA03247  2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAapARPPVRRLARPAVSRSTES-- 2897

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907194905  422 vFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 471
Cdd:PHA03247  2898 -FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT 2946
PHA03247 PHA03247
large tegument protein UL36; Provisional
 370-470 2.62e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  370 TPQRRPvssvHPPGRPPAV-------RGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPfsAPPQIPSRPAri 442
Cdd:PHA03247  2678 SPPQRP----RRRAARPTVgsltslaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP--APPAVPAGPA-- 2749

                           90       100
                   ....*....|....*....|....*...
gi 1907194905  443 PPGIPPGVPSRRAPAAPSRPTiiRPAEP 470
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPA--PPAAP 2775
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 124-220 5.67e-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: 42.69  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 124 VIRRGWLtinnisLMKGGS----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKgfMSNKHVFAIFNTEQRN 199
Cdd:cd01252     3 PDREGWL------LKLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907194905 200 VYK------DLRQIE-------LACDSQEDVDSW 220
Cdd:cd01252    75 VIKacktdsDGKVVEgnhtvyrISAASEEERDEW 108
PHA03247 PHA03247
large tegument protein UL36; Provisional
 346-471 6.23e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 6.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  346 STVSTPVPPPVddtwlqnTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFA- 424
Cdd:PHA03247  2873 AKPAAPARPPV-------RRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAp 2945

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907194905  425 NNDPFSAPPQIPSRPARIPPG----IPPGVPSRRAPAAPSRPTiirPAEPS 471
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGAlvpgRVAVPRFRVPQPAPSREA---PASST 2993
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 342-471 7.23e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  342 DISTSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLipmpvGATSSFSAPPIPSRPGPQS 421
Cdd:PHA03307   177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDA-----GASSSDSSSSESSGCGWGP 251

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907194905  422 VFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 471
Cdd:PHA03307   252 ENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPS 301
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 349-471 1.06e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  349 STPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPM--------------PVGATSSFSAPPIP 414
Cdd:PHA03307    86 STPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlrpvgspgpppaasPPAAGASPAAVASD 165

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194905  415 SRPGPQ-SVFANNDPFSAPPqiPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 471
Cdd:PHA03307   166 AASSRQaALPLSSPEETARA--PSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPA 221
PHA03247 PHA03247
large tegument protein UL36; Provisional
 369-470 1.20e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  369 PTPQRR-------PVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSfsAPPIPSRPGPQSVFANND-PFSAPPQIPSRPA 440
Cdd:PHA03247   381 PTRKRRsarhaatPFARGPGGDDQTRPAAPVPASVPTPAPTPVPAS--APPPPATPLPSAEPGSDDgPAPPPERQPPAPA 458

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907194905  441 RIPPGIPPGVPSRRA-PAAPSRptiiRPAEP 470
Cdd:PHA03247   459 TEPAPDDPDDATRKAlDALRER----RPPEP 485
PHA03247 PHA03247
large tegument protein UL36; Provisional
 351-471 1.37e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  351 PVPPPVDDTwlqntsgHSPTPQR-RPVSSVHPPGRPPAVRGPT--PGPPLIPMPVGATSSFSAPPIPSR----------- 416
Cdd:PHA03247  2645 TVPPPERPR-------DDPAPGRvSRPRRARRLGRAAQASSPPqrPRRRAARPTVGSLTSLADPPPPPPtpepaphalvs 2717

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194905  417 --PGPQSVFANNDPFSAPPQIPSRPArippgippGVPSRRAPAAPSRPTiiRPAEPS 471
Cdd:PHA03247  2718 atPLPPGPAAARQASPALPAAPAPPA--------VPAGPATPGGPARPA--RPPTTA 2764
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
351-471 1.61e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.10  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 351 PVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMP---------VGATSSFSAPPIPSRPGPQS 421
Cdd:PRK12323  410 PAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAaarpaaagpRPVAAAAAAAPARAAPAAAP 489

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194905 422 VFANNDP---------FSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 471
Cdd:PRK12323  490 APADDDPppweelppeFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAA 548
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 344-437 2.06e-04

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: 40.10  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 344 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 421
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 1907194905 422 VFANNDP---FSAPPQIPS 437
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 369-470 2.47e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  369 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLI-----PMPVGATSSFSAPPIPSRPGPQSVFANNDP--------------- 428
Cdd:PHA03247  2592 PPQSARPRAPVDDRGDPRGPAPPSPLPPDThapdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvsrprrarrlg 2671

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907194905  429 ----FSAPPQIPSRPARIPPGIPPGVPSRRAPAAP---SRPTIIRPAEP 470
Cdd:PHA03247  2672 raaqASSPPQRPRRRAARPTVGSLTSLADPPPPPPtpePAPHALVSATP 2720
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 368-461 2.50e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 43.79  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 368 SPTPQRRPVSSVHPPGRPPAVRGPTPGPP-------LIPMPVGAtssfSAPPIPSRPGPQSVFANNDPfSAPPQIPSRPA 440
Cdd:PHA03321  443 PPPPRARPGSTPACARRARAQRARDAGPEyvdplgaLRRLPAGA----APPPEPAAAPSPATYYTRMG-GGPPRLPPRNR 517

                          90       100
                  ....*....|....*....|.
gi 1907194905 441 RippgippgVPSRRAPAAPSR 461
Cdd:PHA03321  518 A--------TETLRPDWGPPA 530
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
369-472 3.05e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 369 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSvfanndpfsaPPQIPSRPARIPPGIPP 448
Cdd:PRK12323  375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRS----------PAPEALAAARQASARGP 444

                          90       100
                  ....*....|....*....|....*
gi 1907194905 449 GVPSRRAPAAPSRPT-IIRPAEPSL 472
Cdd:PRK12323  445 GGAPAPAPAPAAAPAaAARPAAAGP 469
PHA03247 PHA03247
large tegument protein UL36; Provisional
 343-462 3.51e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  343 ISTSTVSTPVPPPvddtwlqntsghSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVgatssfSAPPIPSRPGPQSV 422
Cdd:PHA03247  2891 VSRSTESFALPPD------------QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR------PQPPLAPTTDPAGA 2952

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907194905  423 FANNDPFSAP---PQIPSRPARIPPGIPPGVPSRRAPAAPSRP 462
Cdd:PHA03247  2953 GEPSGAVPQPwlgALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 367-459 3.96e-04

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 42.03  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 367 HSPTPQRRPVSSVHPPgrppavrgptPGPPLIPMPVGATSSFSAPPIPSRPG----------PQSVFANNDPfsappqip 436
Cdd:PHA03418   40 HHPNPQEDPDKNPSPP----------PDPPLTPRPPAQPNGHNKPPVTKQPGgegteedhqaPLAADADDDP-------- 101

                          90       100
                  ....*....|....*....|...
gi 1907194905 437 sRPARIPPGIPPGVPSRRAPAAP 459
Cdd:PHA03418  102 -RPGKRSKADEHGPAPGRAALAP 123
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 351-470 4.27e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 351 PVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRG---PTPGPPLIPMPVGATSSFSAPPIPSRPG--PQSVFAN 425
Cdd:PRK07764  658 AVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAApaqPAPAPAATPPAGQADDPAAQPPQAAQGAsaPSPAADD 737

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907194905 426 NDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEP 470
Cdd:PRK07764  738 PVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 339-470 4.69e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 339 IIGDISTSTVSTPVPPPVDDTWL-QNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPG--PPLIPMPVGATSSFSAPPIPS 415
Cdd:PRK07764  662 ASDGGDGWPAKAGGAAPAAPPPApAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAaqPPQAAQGASAPSPAADDPVPL 741

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907194905 416 RPGPQSVFANNDPFSAPPQIPSRPARIPPGIPPgVPSRRAPAAPSRPTIIRPAEP 470
Cdd:PRK07764  742 PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP-PPSPPSEEEEMAEDDAPSMDD 795
PHA03247 PHA03247
large tegument protein UL36; Provisional
 343-470 7.02e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 7.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  343 ISTSTVSTPVPP-PVDDTWLQNTSGHSPTPQRRPVSSVHPPGRP-PAVRGPTPGPPLIPMPVGATSsfsAP--PIPSRPG 418
Cdd:PHA03247  2791 LSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAqPTAPPPPPGPPPPSLPLGGSV---APggDVRRRPP 2867

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907194905  419 PQSVFANNdpfSAPPQIP---------SRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEP 470
Cdd:PHA03247  2868 SRSPAAKP---AAPARPPvrrlarpavSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925
PHA01929 PHA01929
putative scaffolding protein
 345-440 7.63e-04

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 41.58  E-value: 7.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 345 TSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGP----TPGPPLIPMPVGATSSFSAPPIPSRPgpq 420
Cdd:PHA01929    1 TTQNEQQLPPGLAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAPqqlaIPTQQPQPVPTSAMTPHVVQQAPAQP--- 77

                          90       100
                  ....*....|....*....|
gi 1907194905 421 svfannDPFSAPPQIPSRPA 440
Cdd:PHA01929   78 ------APAAPPAAGAALPE 91
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
 313-419 8.23e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 41.75  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 313 MEESAEQAQRRDDMLRMYHALKEALNIIGDI-STSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPP---GRPPAV 388
Cdd:PRK14963  315 LDEQMERFARRSDALSLELALLHALLALGGApSEGVAAVAPPAPAPADLTQRLNRLEKEVRSLRSAPTAAAtaaGAPLPD 394

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907194905 389 RGPTPGPPliPMPVGATSSFSAPPIPSRPGP 419
Cdd:PRK14963  395 FDPRPRGP--PAPEPARSAEAPPLVAPAAAP 423
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 364-471 9.03e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 364 TSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANND--PFSAPPQIPSRPAR 441
Cdd:PRK07764  604 ASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDgwPAKAGGAAPAAPPP 683

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907194905 442 IPPGIPPGVPSRRAPAAP-SRPTIIRPAEPS 471
Cdd:PRK07764  684 APAPAAPAAPAGAAPAQPaPAPAATPPAGQA 714
PHA03247 PHA03247
large tegument protein UL36; Provisional
 364-474 1.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  364 TSGHSPTPQRRPVSSV------HPPGRPPAVRGP--TPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPPQI 435
Cdd:PHA03247  2680 PQRPRRRAARPTVGSLtsladpPPPPPTPEPAPHalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907194905  436 PSRPARIPPGIPPGVPSRRAPAAPSRPTII-----RPAEPSLLD 474
Cdd:PHA03247  2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVAslsesRESLPSPWD 2803
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 305-463 1.37e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  305 SSADQSSLMEESAEQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVddtwlqntSGHSPTPQRRPVSSVHPPGR 384
Cdd:PHA03307   234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA--------SSSSSPRERSPSPSPSSPGS 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  385 PPAVRGPTPGPPLIPMP---VGATSSFSAPP--IPSRPGPQSVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAP 459
Cdd:PHA03307   306 GPAPSSPRASSSSSSSRessSSSTSSSSESSrgAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP 385


                   ....
gi 1907194905  460 SRPT 463
Cdd:PHA03307   386 TRRR 389
PHA03247 PHA03247
large tegument protein UL36; Provisional
 349-472 2.42e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  349 STPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDP 428
Cdd:PHA03247  2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD 2861

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907194905  429 FSAPPqiPSRPARIPpgippgvpsrraPAAPSRPTIIRPAEPSL 472
Cdd:PHA03247  2862 VRRRP--PSRSPAAK------------PAAPARPPVRRLARPAV 2891
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 333-471 2.68e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  333 LKEALNIIGDISTSTVSTPVPPPVDDtwLQNTSGHSPTPQRRPVSSVHPPGRPPAVR-----GPTPGPPLIP-----MPV 402
Cdd:PHA03307    10 LIEAAAEGGEFFPRPPATPGDAADDL--LSGSQGQLVSDSAELAAVTVVAGAAACDRfepptGPPPGPGTEApanesRST 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194905  403 GATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPSR--------PARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 471
Cdd:PHA03307    88 PTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPaspppspaPDLSEMLRPVGSPGPPPAASPPAAGASPAAVAS 164
PHA03379 PHA03379
EBNA-3A; Provisional
 344-471 3.37e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 40.04  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 344 STSTVSTPVPPPVDDTW---LQNTSGHSPTP----QRRPVSSVHPPGRPPAV-RGPTPGPPLIPMPVGatsSFSAP--PI 413
Cdd:PHA03379  436 SHGSAQVPEPPPVHDLEpgpLHDQHSMAPCPvaqlPPGPLQDLEPGDQLPGVvQDGRPACAPVPAPAG---PIVRPweAS 512

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194905 414 PSRpGPQSVFANNDPFSAPPQIPSRPArippgippGVPSRRAPAAPSRPTIIRPAEPS 471
Cdd:PHA03379  513 LSQ-VPGVAFAPVMPQPMPVEPVPVPT--------VALERPVCPAPPLIAMQGPGETS 561
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 124-220 3.74e-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: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 124 VIRRGWLTinnislMKGGS-----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGF-MSNKHVFAIFNTEQ 197
Cdd:cd13248     7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                          90       100
                  ....*....|....*....|...
gi 1907194905 198 RNVYkdlrqieLACDSQEDVDSW 220
Cdd:cd13248    81 RTYY-------FAADTAEEMEQW 96
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 353-463 5.15e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.22  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 353 PPPVddtwlqnTSGHSPTPQRRPVSSVHPPGRPPavrgpTPGPP------LIPMPVGATSSFSAPPIPsRPGPQSVFANN 426
Cdd:PHA03264  266 PPPA-------PSGGSPAPPGDDRPEAKPEPGPV-----EDGAPgretggEGEGPEPAGRDGAAGGEP-KPGPPRPAPDA 332

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907194905 427 DPFSAPPQIPSRPARIppgippgvpsrRAPAAPSRPT 463
Cdd:PHA03264  333 DRPEGWPSLEAITFPP-----------PTPATPAVPR 358
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
364-470 6.41e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.09  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 364 TSGHSPTPQRRPVSSVHPPG---RPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPS--- 437
Cdd:PRK12323  447 APAPAPAPAAAPAAAARPAAagpRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAesi 526

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907194905 438 -RPArIPPGIPPGVPSRRAPAAPSRPTIIRPAEP 470
Cdd:PRK12323  527 pDPA-TADPDDAFETLAPAPAAAPAPRAAAATEP 559
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 366-473 7.69e-03

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 37.36  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 366 GHSPTPQRRPVSSVHPPGRPPAVRGP--TPGPPLIPMPVGATSSFSAPPI--------PSRPGPQSVFANNDPFSAP-PQ 434
Cdd:cd21975    20 GVRPDPEGAGLAAGLDVRATREVAKGpgPPGPAWKPDGADSPGLVTAAPHllaanvlaPLRGPSVEGSSLESGDADMgSD 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907194905 435 IPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLL 473
Cdd:cd21975   100 SDVAPASGAAASTSPESSSDAASSPSPLSLLHPGEAGLE 138
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 365-460 7.94e-03

N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 37.49  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 365 SGHSPtpqRRPVSSVHPPGRPPAVRGPTPGPPLIPMPV-GATSSFSAPPIPSRPG-PQSVFANNDPFSAPPQIPSRPAri 442
Cdd:cd21576   103 SGEAP---RASSGSSDPARGSSPTLGSEPAPASGEDAVsGPESSFGAPAIPSAPAaPGAPAVSGEVPGGAPGAGPAPA-- 177

                          90
                  ....*....|....*...
gi 1907194905 443 ppgipPGVPSRRAPAAPS 460
Cdd:cd21576   178 -----AGPAPRRRPVTPA 190
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 369-471 9.31e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.43  E-value: 9.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 369 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVfANNDPFSAPPQIPSRPARIPPGIPP 448
Cdd:PRK07764  399 PSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGG-APSPPPAAAPSAQPAPAPAAAPEPT 477

                          90       100
                  ....*....|....*....|...
gi 1907194905 449 GVPSRRAPAAPSRPTiiRPAEPS 471
Cdd:PRK07764  478 AAPAPAPPAAPAPAA--APAAPA 498
PHA03247 PHA03247
large tegument protein UL36; Provisional
 326-468 9.43e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.77  E-value: 9.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905  326 MLRMYHALKE-ALNIIGDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSS-VHPPGRPP-AVRGPTPGPPLIPMPV 402
Cdd:PHA03247  2533 MLTWIRGLEElASDDAGDPPPPLPPAAPPAAPDRS--VPPPRPAPRPSEPAVTSrARRPDAPPqSARPRAPVDDRGDPRG 2610

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194905  403 GATSSfSAPPIPSRPGPqsvfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPA 468
Cdd:PHA03247  2611 PAPPS-PLPPDTHAPDP--------PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRA 2667
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 344-441 9.55e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.54  E-value: 9.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194905 344 STSTVSTPVPPPvddtwlqntSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPP------IPSRP 417
Cdd:PRK14951  396 QAAAAPAPAAAP---------AAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAapetvaIPVRV 466

                          90       100
                  ....*....|....*....|....
gi 1907194905 418 GPQSVFANNDPFSAPPQIPSRPAR 441
Cdd:PRK14951  467 APEPAVASAAPAPAAAPAAARLTP 490
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
 124-157 9.70e-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: 9.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907194905 124 VIRRGWLTINNISLMKGGS---KEYWFVLTAESLSWY 157
Cdd:cd13297    13 VIERGWLYKEGGKGGARGNltkKKRWFVLTGNSLDYY 49
 
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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