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Conserved domains on  [gi|564362559|ref|XP_006242672|]
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dynamin-2 isoform X3 [Rattus norvegicus]

Protein Classification

dynamin( domain architecture ID 11249456)

dynamin such as human dynamin-1, which is involved in clathrin-mediated endocytosis and other vesicular trafficking processes; contains an N-terminal GTPase domain that binds and hydrolyzes GTP, a middle domain involved in self-assembly and oligomerization, and a pleckstrin homology (PH) domain responsible for interactions with the GTPase effector domain (GED)

CATH:  1.20.120.1240|2.30.29.30|3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  15040446
SCOP:  4004047|4002395|4004048

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 1.66e-162

Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.


:

Pssm-ID: 197491  Cd Length: 240  Bit Score: 472.83  E-value: 1.66e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559     6 MEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559    86 CKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFIS 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559   166 RESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGR 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 7.20e-144

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: 426.55  E-value: 7.20e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  215 DARDVLENKLLPLRRGYIGVVNRSQKDIEGRKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  295 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  375 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 564362559  455 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 520-629 9.11e-70

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: 9.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 520 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 599
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 564362559 600 LRQIELACDSQEDVDSWKASFLRAGVYPEK 629
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
649-739 1.70e-30

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.30  E-value: 1.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  649 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 728
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 564362559  729 LKEALNIIGDI 739
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 737-867 9.37e-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: 53.02  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  737 GDISTSTVSTPVPPPVDDTwlqNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 816
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAG---PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564362559  817 NVFANNDPFSAPPQIPSRPARIPPGIPPGvprrAPAAPSRPTiiRPAEPSL 867
Cdd:PHA03247 2806 DPPAAVLAPAAALPPAASPAGPLPPPTSA----QPTAPPPPP--GPPPPSL 2850
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 1.66e-162

Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.


Pssm-ID: 197491  Cd Length: 240  Bit Score: 472.83  E-value: 1.66e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559     6 MEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559    86 CKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFIS 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559   166 RESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGR 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 29-294 7.15e-148

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206738  Cd Length: 278  Bit Score: 436.68  E-value: 7.15e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFS--------KTEYAEFLHCKSKKFTDFDEVRQE 100
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMD 180
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIEGRKDIRAALAAERK 257
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564362559 258 FFLSHPAYRH-MADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:cd08771  241 FFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 7.20e-144

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: 426.55  E-value: 7.20e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  215 DARDVLENKLLPLRRGYIGVVNRSQKDIEGRKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  295 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  375 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 564362559  455 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 520-629 9.11e-70

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: 9.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 520 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 599
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 564362559 600 LRQIELACDSQEDVDSWKASFLRAGVYPEK 629
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 1.33e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 222.11  E-value: 1.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559   34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLI--------FSKTEYAEFLhcksKKFTDFDEVRQEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGespgasegAVKVEYKDGE----KKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  106 DRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqikDMILQFIsRESSLILAVTPANMDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 564362559  186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
649-739 1.70e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.30  E-value: 1.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  649 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 728
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 564362559  729 LKEALNIIGDI 739
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
648-739 8.59e-26

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 101.93  E-value: 8.59e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559   648 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 727
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 564362559   728 ALKEALNIIGDI 739
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 520-623 1.50e-10

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: 1.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559   520 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 595
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 564362559   596 VYKDLRQIELACDSQEDVDSWKASFLRA 623
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 520-623 1.90e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  520 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 595
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 564362559  596 VykdlRQIELACDSQEDVDSWKASFLRA 623
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 737-867 9.37e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  737 GDISTSTVSTPVPPPVDDTwlqNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 816
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAG---PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564362559  817 NVFANNDPFSAPPQIPSRPARIPPGIPPGvprrAPAAPSRPTiiRPAEPSL 867
Cdd:PHA03247 2806 DPPAAVLAPAAALPPAASPAGPLPPPTSA----QPTAPPPPP--GPPPPSL 2850
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 740-833 3.58e-06

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: 46.26  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  740 STSTVSTPVPPPVDDTWLQ-NTSSHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQN 817
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 564362559  818 VFANNDP---FSAPPQIPS 833
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 1.66e-162

Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.


Pssm-ID: 197491  Cd Length: 240  Bit Score: 472.83  E-value: 1.66e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559     6 MEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559    86 CKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFIS 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559   166 RESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGR 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 29-294 7.15e-148

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206738  Cd Length: 278  Bit Score: 436.68  E-value: 7.15e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFS--------KTEYAEFLHCKSKKFTDFDEVRQE 100
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMD 180
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIEGRKDIRAALAAERK 257
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564362559 258 FFLSHPAYRH-MADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:cd08771  241 FFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 7.20e-144

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: 426.55  E-value: 7.20e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  215 DARDVLENKLLPLRRGYIGVVNRSQKDIEGRKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  295 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  375 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 564362559  455 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 520-629 9.11e-70

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: 9.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 520 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 599
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 564362559 600 LRQIELACDSQEDVDSWKASFLRAGVYPEK 629
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 1.33e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 222.11  E-value: 1.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559   34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLI--------FSKTEYAEFLhcksKKFTDFDEVRQEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGespgasegAVKVEYKDGE----KKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  106 DRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqikDMILQFIsRESSLILAVTPANMDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 564362559  186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
649-739 1.70e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.30  E-value: 1.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  649 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 728
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 564362559  729 LKEALNIIGDI 739
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
648-739 8.59e-26

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 101.93  E-value: 8.59e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559   648 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 727
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 564362559   728 ALKEALNIIGDI 739
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 520-623 1.50e-10

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: 1.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559   520 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 595
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 564362559   596 VYKDLRQIELACDSQEDVDSWKASFLRA 623
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 520-623 1.90e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  520 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 595
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 564362559  596 VykdlRQIELACDSQEDVDSWKASFLRA 623
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 522-616 2.01e-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: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 522 RRGWLTINNISLMKGGsKEYWFVLTAESLSWYKDEEEKEKKY--MLPLDN-LKIRDVEKGfmSNKHVFAIFNTEQRNVYk 598
Cdd:cd00821    1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                         90
                 ....*....|....*...
gi 564362559 599 dlrqieLACDSQEDVDSW 616
Cdd:cd00821   77 ------LQADSEEERQEW 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 737-867 9.37e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  737 GDISTSTVSTPVPPPVDDTwlqNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 816
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAG---PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564362559  817 NVFANNDPFSAPPQIPSRPARIPPGIPPGvprrAPAAPSRPTiiRPAEPSL 867
Cdd:PHA03247 2806 DPPAAVLAPAAALPPAASPAGPLPPPTSA----QPTAPPPPP--GPPPPSL 2850
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 740-833 3.58e-06

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: 46.26  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  740 STSTVSTPVPPPVDDTWLQ-NTSSHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQN 817
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 564362559  818 VFANNDP---FSAPPQIPS 833
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 740-866 3.68e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  740 STSTVSTPVPPPvddtwlqntsshsPTPQRRP---VSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRP--- 813
Cdd:PHA03247 2694 SLTSLADPPPPP-------------PTPEPAPhalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARParp 2760

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564362559  814 ----GPQNVFANNDPFSAPPQIPSRPArippgippgvprRAPAAPSRPTIIRPAEPS 866
Cdd:PHA03247 2761 pttaGPPAPAPPAAPAAGPPRRLTRPA------------VASLSESRESLPSPWDPA 2805
PHA03247 PHA03247
large tegument protein UL36; Provisional
 760-867 9.02e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 9.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  760 TSSHSPT--PQRR----PVSSV------HPPGRPPAVRGP--TPGPPLIPMPVGATSSFSAPPI-PSRPGPQN--VFANN 822
Cdd:PHA03247 2674 AQASSPPqrPRRRaarpTVGSLtsladpPPPPPTPEPAPHalVSATPLPPGPAAARQASPALPAaPAPPAVPAgpATPGG 2753

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 564362559  823 DPFSAPPQIPSRPARIPPGippgvprRAPAAPSRPTIIRPAEPSL 867
Cdd:PHA03247 2754 PARPARPPTTAGPPAPAPP-------AAPAAGPPRRLTRPAVASL 2791
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-865 2.16e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  747 PVPPPVDDtwlqntsSHSPTPQR-RPVSSVHPPGRPPAVRGPT--PGPPLIPMPVGATSSFSAPPIPSR----------- 812
Cdd:PHA03247 2645 TVPPPERP-------RDDPAPGRvSRPRRARRLGRAAQASSPPqrPRRRAARPTVGSLTSLADPPPPPPtpepaphalvs 2717

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  813 --PGPQNVFANNDPFSAPPQIPSRPARIPPGIPPGVPRR-----APAAPSRPTiiRPAEP 865
Cdd:PHA03247 2718 atPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARparppTTAGPPAPA--PPAAP 2775
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 735-865 2.70e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 735 IIGDISTSTVSTPVPPPVDDTWL-QNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPG--PPLIPMPVGATSSFSAPPIPS 811
Cdd:PRK07764 662 ASDGGDGWPAKAGGAAPAAPPPApAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAaqPPQAAQGASAPSPAADDPVPL 741

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564362559 812 RPGPQNVFANNDPFSAPPQIPSRPARIPPGIPPGVPRRAPAAPSRPTIIRPAEP 865
Cdd:PRK07764 742 PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDD 795
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 764-865 2.97e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.79  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 764 SPTPQRRPVSSVHPPGRPPAVRGPTPGPPlipmpvGATSSFSAPPIPSRPGPQNVFANNDPFSAPPQIPSR--------- 834
Cdd:PRK14951 380 TPARPEAAAPAAAPVAQAAAAPAPAAAPA------AAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAvalapappa 453

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564362559 835 ---------PARIPPGIPPGVPRRAPAAPSRPTIIRPAEP 865
Cdd:PRK14951 454 qaapetvaiPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
PHA03247 PHA03247
large tegument protein UL36; Provisional
 742-866 4.89e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  742 STVSTPVPPPVddtwlqnTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQNVFA- 820
Cdd:PHA03247 2873 AKPAAPARPPV-------RRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAp 2945

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564362559  821 NNDPFSAPPQIPSRP-----ARIPPGIPPGVPRRAPAAPSRPTiirPAEPS 866
Cdd:PHA03247 2946 TTDPAGAGEPSGAVPqpwlgALVPGRVAVPRFRVPQPAPSREA---PASST 2993
PHA03247 PHA03247
large tegument protein UL36; Provisional
 765-865 7.59e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 7.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  765 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLI-----PMPVGATSSFSAPPIPSRPGPQNVFANNDP--------------- 824
Cdd:PHA03247 2592 PPQSARPRAPVDDRGDPRGPAPPSPLPPDThapdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvsrprrarrlg 2671

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 564362559  825 ----FSAPPQIPSRPARIPPGIPPGVPRRAPAAP----SRPTIIRPAEP 865
Cdd:PHA03247 2672 raaqASSPPQRPRRRAARPTVGSLTSLADPPPPPptpePAPHALVSATP 2720
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 520-616 1.17e-04

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: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 520 VIRRGWLtinnisLMKGGS----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKgfMSNKHVFAIFNTEQRN 595
Cdd:cd01252    3 PDREGWL------LKLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564362559 596 VYK------DLRQIE-------LACDSQEDVDSW 616
Cdd:cd01252   75 VIKacktdsDGKVVEgnhtvyrISAASEEERDEW 108
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 738-866 1.42e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.93  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  738 DISTSTVSTPVPPPVDDTWLQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLipmPVGATSSFSAPPIPSRPGPQN 817
Cdd:PHA03307  177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDA---GASSSDSSSSESSGCGWGPEN 253

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 564362559  818 vfANNDPFSAPPQIPSRPARiPPGIPPGVPRRAPAAPSRPTIIRPAEPS 866
Cdd:PHA03307  254 --ECPLPRPAPITLPTRIWE-ASGWNGPSSRPGPASSSSSPRERSPSPS 299
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 745-866 1.80e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  745 STPVPPPVDDTWLQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPM--------------PVGATSSFSAPPIP 810
Cdd:PHA03307   86 STPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlrpvgspgpppaasPPAAGASPAAVASD 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564362559  811 SRPGPQNVFANNDPFSAPPQIPSRPARIPPGIPPGVPRRAPAAPSRPTIIRPAEPS 866
Cdd:PHA03307  166 AASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPA 221
PHA03247 PHA03247
large tegument protein UL36; Provisional
 740-866 1.96e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  740 STSTVSTPVPPPVDDTWLQNTSSHSP-------TPQRRPVSSVHPPGRPPAVRGPTPGPPlipmpvGATSSFSAPPIPSR 812
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVS------RSTESFALPPDQPE 2906

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564362559  813 PGPQnvfanndpfsapPQIPSRPARIPPGIPPGVPRRAPAAPSRPTiiRPAEPS 866
Cdd:PHA03247 2907 RPPQ------------PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ--PPLAPT 2946
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 739-856 2.48e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 44.95  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 739 ISTSTVSTPVPPPVDDTWLQNTSSH--------------SPTPQRRPVSSVHPPGRPPAVRGPTPGPP-------LIPMP 797
Cdd:PHA03321 404 LATELFRTGVPSEHYEASLRLLSSRqppgapaprrdndpPPPPRARPGSTPACARRARAQRARDAGPEyvdplgaLRRLP 483

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564362559 798 VGAtssfSAPPIPSRPGPQNVFANNDPfSAPPQIPSRPARippgippGVPRRAPAAPSR 856
Cdd:PHA03321 484 AGA----APPPEPAAAPSPATYYTRMG-GGPPRLPPRNRA-------TETLRPDWGPPA 530
PHA01929 PHA01929
putative scaffolding protein
 741-836 3.83e-04

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 43.51  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 741 TSTVSTPVPPPVDDTWLQNTSSHSPTPQRRPVSSVHPPGRPPAVRGP----TPGPPLIPMPVGATSSFSAPPIPSRPgpq 816
Cdd:PHA01929   1 TTQNEQQLPPGLAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAPqqlaIPTQQPQPVPTSAMTPHVVQQAPAQP--- 77

                         90       100
                 ....*....|....*....|
gi 564362559 817 nvfannDPFSAPPQIPSRPA 836
Cdd:PHA01929  78 ------APAAPPAAGAALPE 91
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 763-824 4.20e-04

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 42.80  E-value: 4.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564362559 763 HSPTPQRRPVSSVHPPgrppavrgptPGPPLIPMPVGATSSFSAPPIPSRPG----------PQNVFANNDP 824
Cdd:PHA03418  40 HHPNPQEDPDKNPSPP----------PDPPLTPRPPAQPNGHNKPPVTKQPGgegteedhqaPLAADADDDP 101
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
 709-818 5.83e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 43.29  E-value: 5.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 709 MEESAEQAQRRDDMLRMYHALKEALNIIGDI-STSTVSTPVPPPVDDTWLQNTSSHSPTPQRRPVSSVHPP---GRPPAV 784
Cdd:PRK14963 315 LDEQMERFARRSDALSLELALLHALLALGGApSEGVAAVAPPAPAPADLTQRLNRLEKEVRSLRSAPTAAAtaaGAPLPD 394

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564362559 785 RGPTPGPPliPMPVGATSSFSAPPIPSRPGPQNV 818
Cdd:PRK14963 395 FDPRPRGP--PAPEPARSAEAPPLVAPAAAPAGL 426
PHA03379 PHA03379
EBNA-3A; Provisional
 740-865 9.03e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 43.12  E-value: 9.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 740 STSTVSTPVPPPVDDTW---LQNTSSHSPTP----QRRPVSSVHPPGRPPAV-RGPTPGPPLIPMPVG------------ 799
Cdd:PHA03379 436 SHGSAQVPEPPPVHDLEpgpLHDQHSMAPCPvaqlPPGPLQDLEPGDQLPGVvQDGRPACAPVPAPAGpivrpweaslsq 515

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564362559 800 ----ATSSFSAPPIPSRPGPQNVFANNDPFS-APPQIPSR-PARIPPGIPPGVPRRAPaaPSRPTIIRPAEP 865
Cdd:PHA03379 516 vpgvAFAPVMPQPMPVEPVPVPTVALERPVCpAPPLIAMQgPGETSGIVRVRERWRPA--PWTPNPPRSPSQ 585
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
747-865 9.46e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 9.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 747 PVPPPVDDTWLQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMP---------VGATSSFSAPPIPSRPGPQN 817
Cdd:PRK12323 410 PAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAaarpaaagpRPVAAAAAAAPARAAPAAAP 489

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 818 VFANNDP---FSAPPQIPS-------------------RPARIPPGIPPGVPRRAPAAPSRPTIIRPAEP 865
Cdd:PRK12323 490 APADDDPppwEELPPEFASpapaqpdaapagwvaesipDPATADPDDAFETLAPAPAAAPAPRAAAATEP 559
PHA03247 PHA03247
large tegument protein UL36; Provisional
 722-867 1.02e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  722 MLRMYHALKE-ALNIIGDISTSTVSTPVPPPVDDTwlQNTSSHSPTP--------QRRPvsSVHP-PGRPPAVRGPtPGP 791
Cdd:PHA03247 2533 MLTWIRGLEElASDDAGDPPPPLPPAAPPAAPDRS--VPPPRPAPRPsepavtsrARRP--DAPPqSARPRAPVDD-RGD 2607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  792 PLIPMPVGATSSFSAPPIPSRPGPQ-NVFANNDPFSAPPQIPSRPARIPPGIPPGVPRRA-----PAAPSRPTiIRPAEP 865
Cdd:PHA03247 2608 PRGPAPPSPLPPDTHAPDPPPPSPSpAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRArrlgrAAQASSPP-QRPRRR 2686


                  ..
gi 564362559  866 SL 867
Cdd:PHA03247 2687 AA 2688
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 701-867 1.39e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  701 SSADQSSLMEESAEQA--QRRDDMLRMYHALKEALNIiGDISTSTVSTPVPPPVDDTWLQNTS---SHSPTPQRRPVS-- 773
Cdd:pfam03154 150 SPQDNESDSDSSAQQQilQTQPPVLQAQSGAASPPSP-PPPGTTQAATAGPTPSAPSVPPQGSpatSQPPNQTQSTAAph 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  774 -------SVHPPGRP---PAVRG-PTPGPPLI-------------PMPVGATSSFSAPPIPSRPGPQNVFANNdPFSAPP 829
Cdd:pfam03154 229 tliqqtpTLHPQRLPsphPPLQPmTQPPPPSQvspqplpqpslhgQMPPMPHSLQTGPSHMQHPVPPQPFPLT-PQSSQS 307

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 564362559  830 QIPSRPARIPPGIPPGVPRRAPAAPSRPTIIRPAEPSL 867
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPL 345
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 760-866 1.43e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 760 TSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQNVFANNDPFSAPPQIPSRPARIP 839
Cdd:PRK07764 604 ASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPP 683

                         90       100
                 ....*....|....*....|....*..
gi 564362559 840 PGIPPGVPRRAPAAPSRPTIIRPAEPS 866
Cdd:PRK07764 684 APAPAAPAAPAGAAPAQPAPAPAATPP 710
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
758-866 1.50e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 758 QNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPI---PSRPGPQNVF-------------AN 821
Cdd:PRK12323 368 SGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVaaaPARRSPAPEAlaaarqasargpgGA 447

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564362559 822 NDPFSAPPQIPSRPARIPPGIPPGVPRRAPAAPSRPTIIRPAEPS 866
Cdd:PRK12323 448 PAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPA 492
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-834 1.96e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  747 PVPPPVDDTWLQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFS----AP---PIPSRPGPQNvf 819
Cdd:PHA03247 2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlgalVPgrvAVPRFRVPQP-- 2982

                          90
                  ....*....|....*
gi 564362559  820 ANNDPFSAPPQIPSR 834
Cdd:PHA03247 2983 APSREAPASSTPPLT 2997
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 747-869 2.08e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 747 PVPPPVDDTWLQNTSSHSPTPQRRPVSSVHPPGRPPAVRG---PTPGPPLIPMPVGATSSFSAPPIPSRPGPQNVFANND 823
Cdd:PRK07764 658 AVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAApaqPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADD 737

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564362559 824 PFSAPPQ-----IPSRPARIPPGIPPGVPRRAPAAPSRPTIIRPAEPSLLD 869
Cdd:PRK07764 738 PVPLPPEpddppDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAED 788
PHA03247 PHA03247
large tegument protein UL36; Provisional
 765-865 2.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  765 PTPQRR-------PVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSsfSAPPIPSRPgPQNVFANNDPFSAPPQIPSRPAR 837
Cdd:PHA03247  381 PTRKRRsarhaatPFARGPGGDDQTRPAAPVPASVPTPAPTPVPA--SAPPPPATP-LPSAEPGSDDGPAPPPERQPPAP 457

                          90       100
                  ....*....|....*....|....*...
gi 564362559  838 IPPGIPPGVPRRAPAAPSRPTIIRPAEP 865
Cdd:PHA03247  458 ATEPAPDDPDDATRKALDALRERRPPEP 485
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 701-866 2.85e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  701 SSADQSSLMEESAEQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVddtwlqntSSHSPTPQRRPVSSVHPPGR 780
Cdd:PHA03307  234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA--------SSSSSPRERSPSPSPSSPGS 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  781 PPAVRGPTPGPPLIPMP---VGATSSFSAPP--IPSRPGPQNVFANNDPFSAPPQIPSRPARIPPGIPPGVPRRAPAAPS 855
Cdd:PHA03307  306 GPAPSSPRASSSSSSSRessSSSTSSSSESSrgAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP 385

                         170
                  ....*....|.
gi 564362559  856 RPTIIRPAEPS 866
Cdd:PHA03307  386 TRRRARAAVAG 396
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 747-835 4.13e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 38.87  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  747 PVPPPVDDTWL--QNTSSHSPTPQRRPVSSVHPPgrPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQNVFANNDP 824
Cdd:pfam15240  56 PQPPASDDPPGppPPGGPQQPPPQGGKQKPQGPP--PQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPP 133

                          90
                  ....*....|.
gi 564362559  825 FSAPPQIPSRP 835
Cdd:pfam15240 134 QGGNQQGPPPP 144
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 749-858 4.42e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 40.37  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 749 PPPVddtwlqnTSSHSPTPQRRPVSSVHPPGRPPavrgpTPGPP------LIPMPVGATSSFSAPPIPsRPGPQNVFANN 822
Cdd:PHA03264 266 PPPA-------PSGGSPAPPGDDRPEAKPEPGPV-----EDGAPgretggEGEGPEPAGRDGAAGGEP-KPGPPRPAPDA 332

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 564362559 823 DPFSAPPQIPSRParippgippgVPRRAPAAPSRPT 858
Cdd:PHA03264 333 DRPEGWPSLEAIT----------FPPPTPATPAVPR 358
PHA03378 PHA03378
EBNA-3B; Provisional
 749-864 5.50e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 749 PPPVDDTWLQNTS-SHSPTPQ----RRPVSSVHPPGRPPAvRGPTPGPPLIPMPVGATSSfSAPPIPSRPGPQNVFANND 823
Cdd:PHA03378 659 ITPYKPTWTQIGHiPYQPSPTgantMLPIQWAPGTMQPPP-RAPTPMRPPAAPPGRAQRP-AAATGRARPPAAAPGRARP 736

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564362559 824 PFSAPPQIP---SRPARIPPGIPPGVPRRAP-AAPSRPTIIRPAE 864
Cdd:PHA03378 737 PAAAPGRARppaAAPGRARPPAAAPGRARPPaAAPGAPTPQPPPQ 781
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 520-616 6.67e-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: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559 520 VIRRGWLTinnislMKGGS-----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGF-MSNKHVFAIFNTEQ 593
Cdd:cd13248    7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                         90       100
                 ....*....|....*....|...
gi 564362559 594 RNVYkdlrqieLACDSQEDVDSW 616
Cdd:cd13248   81 RTYY-------FAADTAEEMEQW 96
Gag_spuma pfam03276
Spumavirus gag protein;
721-865 7.97e-03

Spumavirus gag protein;


Pssm-ID: 460872 [Multi-domain]  Cd Length: 614  Bit Score: 39.73  E-value: 7.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564362559  721 DMLRMYHALKEALNIiGDISTSTVSTPVPPPVddtwlqntSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPplIPMPVGA 800
Cdd:pfam03276 159 ELLALREQEAEALRI-GLAEISPGAQGGIPPG--------ASFSGLPSLPAIGGIHLPAIPGIHARAPPGN--IARSLGD 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564362559  801 ----TSSFSAPPIPS---RPGPQNVFANNDPFSA-----PPQIPSRPARIppgippgvprrAPAAPSRPTIIRPAEP 865
Cdd:pfam03276 228 dimpSLGDAGMPQPRfafHPGNPFAEAEGHPFAEaegerPRDIPRAPRID-----------APSAPAIPAIQPIAPP 293
 
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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