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Conserved domains on  [gi|56549121|ref|NP_001005360|]
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dynamin-2 isoform 1 [Homo sapiens]

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 2.29e-161

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: 469.74  E-value: 2.29e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121      6 MEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEHAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121     86 CKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFIS 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    166 RESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGK 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 4.14e-145

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: 430.02  E-value: 4.14e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   215 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   295 ALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   375 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 56549121   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 9.70e-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: 9.70e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 520 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 599
Cdd:cd01256   3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                        90       100       110
                ....*....|....*....|....*....|
gi 56549121 600 LRQIELACDSQEDVDSWKASFLRAGVYPEK 629
Cdd:cd01256  83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
649-739 1.46e-30

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.30  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   649 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHA 728
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 56549121   729 LKEALNIIGDI 739
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 737-868 7.06e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 7.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   737 GDISTSTVSTPVPPPVDDTwlqSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQ 816
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAG---PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   817 SVFAN---------------------SDLFPAPPQIPSRPVRIPPGIPPGVP-----SRRP--------PAAPSRPTIIR 862
Cdd:PHA03247 2806 DPPAAvlapaaalppaaspagplpppTSAQPTAPPPPPGPPPPSLPLGGSVApggdvRRRPpsrspaakPAAPARPPVRR 2885


                  ....*.
gi 56549121   863 PAEPSL 868
Cdd:PHA03247 2886 LARPAV 2891
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 2.29e-161

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: 469.74  E-value: 2.29e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121      6 MEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEHAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121     86 CKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFIS 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    166 RESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGK 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 1.62e-146

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: 433.21  E-value: 1.62e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFS--------KTEHAEFLHCKSKKFTDFDEVRQE 100
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMD 180
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERK 257
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 56549121 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 4.14e-145

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: 430.02  E-value: 4.14e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   215 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   295 ALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   375 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 56549121   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 9.70e-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: 9.70e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 520 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 599
Cdd:cd01256   3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                        90       100       110
                ....*....|....*....|....*....|
gi 56549121 600 LRQIELACDSQEDVDSWKASFLRAGVYPEK 629
Cdd:cd01256  83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 3.49e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 220.95  E-value: 3.49e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEHAEFLHC----KSKKFTDFDEVRQEIEAETDRVT 109
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGASEGAVKVeykdGEKKFEDFSELREEIEKETEKIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   110 GTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqikDMILQFIsRESSLILAVTPANMDLANSDALKL 189
Cdd:pfam00350  81 GTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSEALFL 150

                         170
                  ....*....|....*...
gi 56549121   190 AKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
649-739 1.46e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.30  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   649 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHA 728
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 56549121   729 LKEALNIIGDI 739
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
648-739 8.94e-26

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 101.93  E-value: 8.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    648 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYH 727
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 56549121    728 ALKEALNIIGDI 739
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 520-623 1.52e-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: 1.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    520 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 595
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 56549121    596 VYKDLRQIELACDSQEDVDSWKASFLRA 623
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 520-623 1.94e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   520 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 595
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 56549121   596 VykdlRQIELACDSQEDVDSWKASFLRA 623
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 737-868 7.06e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 7.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   737 GDISTSTVSTPVPPPVDDTwlqSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQ 816
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAG---PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   817 SVFAN---------------------SDLFPAPPQIPSRPVRIPPGIPPGVP-----SRRP--------PAAPSRPTIIR 862
Cdd:PHA03247 2806 DPPAAvlapaaalppaaspagplpppTSAQPTAPPPPPGPPPPSLPLGGSVApggdvRRRPpsrspaakPAAPARPPVRR 2885


                  ....*.
gi 56549121   863 PAEPSL 868
Cdd:PHA03247 2886 LARPAV 2891
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 750-867 7.31e-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: 39.33  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   750 PPVDDTWLQSASSHSPT-PQRRPVSSI-HPPGRPPAVRGPTPGPPlipvpvgaAASFSAPpiPSRPgpqsvfanSDLFPA 827
Cdd:pfam16058   1 PSSSITEPPRDPSGSYGePPRAPSSSYtEPQRDPSSSITEPPADP--------SSSYTEP--PRDP--------SGSYTE 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 56549121   828 PPQIPSrpvrippgippgVPSRRPPAAPSRPTIIRPAEPS 867
Cdd:pfam16058  63 PQRDPS------------SSSTEPQRDPSSSITEPPRDPS 90
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 760-856 3.68e-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: 39.42  E-value: 3.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 760 ASSHSPTPQRRPvssihppgrppavrGPTPGPPliPVPV-------GAAASFSAPPIPSRPGPQSVFANSDLFPA-PPQI 831
Cdd:cd21576 109 ASSGSSDPARGS--------------SPTLGSE--PAPAsgedavsGPESSFGAPAIPSAPAAPGAPAVSGEVPGgAPGA 172

                        90       100
                ....*....|....*....|....*
gi 56549121 832 PSRPvrippgiPPGVPSRRPPAAPS 856
Cdd:cd21576 173 GPAP-------AAGPAPRRRPVTPA 190
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 747-835 8.02e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 38.23  E-value: 8.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    747 PVPPPVDDTWLQSASSHSPTPQRRPVssihppgRPPAVRGPTPGPPLIPVPVGAAasfsAPPIPSRPGPQSVFAnsdLFP 826
Cdd:smart00818  75 PVPGQHSMTPTQHHQPNLPQPAQQPF-------QPQPLQPPQPQQPMQPQPPVHP----IPPLPPQPPLPPMFP---MQP 140


                   ....*....
gi 56549121    827 APPQIPSRP 835
Cdd:smart00818 141 LPPLLPDLP 149
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 2.29e-161

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: 469.74  E-value: 2.29e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121      6 MEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEHAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121     86 CKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFIS 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    166 RESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGK 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 1.62e-146

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: 433.21  E-value: 1.62e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFS--------KTEHAEFLHCKSKKFTDFDEVRQE 100
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMD 180
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERK 257
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 56549121 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 4.14e-145

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: 430.02  E-value: 4.14e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   215 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   295 ALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   375 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 56549121   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 9.70e-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: 9.70e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 520 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 599
Cdd:cd01256   3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                        90       100       110
                ....*....|....*....|....*....|
gi 56549121 600 LRQIELACDSQEDVDSWKASFLRAGVYPEK 629
Cdd:cd01256  83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 3.49e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 220.95  E-value: 3.49e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEHAEFLHC----KSKKFTDFDEVRQEIEAETDRVT 109
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGASEGAVKVeykdGEKKFEDFSELREEIEKETEKIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   110 GTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqikDMILQFIsRESSLILAVTPANMDLANSDALKL 189
Cdd:pfam00350  81 GTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSEALFL 150

                         170
                  ....*....|....*...
gi 56549121   190 AKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
649-739 1.46e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.30  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   649 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHA 728
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 56549121   729 LKEALNIIGDI 739
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
648-739 8.94e-26

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 101.93  E-value: 8.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    648 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYH 727
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 56549121    728 ALKEALNIIGDI 739
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 520-623 1.52e-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: 1.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    520 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 595
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 56549121    596 VYKDLRQIELACDSQEDVDSWKASFLRA 623
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 520-623 1.94e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   520 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 595
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 56549121   596 VykdlRQIELACDSQEDVDSWKASFLRA 623
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 737-868 7.06e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 7.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   737 GDISTSTVSTPVPPPVDDTwlqSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQ 816
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAG---PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   817 SVFAN---------------------SDLFPAPPQIPSRPVRIPPGIPPGVP-----SRRP--------PAAPSRPTIIR 862
Cdd:PHA03247 2806 DPPAAvlapaaalppaaspagplpppTSAQPTAPPPPPGPPPPSLPLGGSVApggdvRRRPpsrspaakPAAPARPPVRR 2885


                  ....*.
gi 56549121   863 PAEPSL 868
Cdd:PHA03247 2886 LARPAV 2891
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 522-616 2.08e-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: 2.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 522 RRGWLTINNISLMKGGsKEYWFVLTAESLSWYKDEEEKEKKY--MLPLDN-LKIRDVEKGfmSNKHVFAIFNTEQRNVYk 598
Cdd:cd00821   1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                        90
                ....*....|....*...
gi 56549121 599 dlrqieLACDSQEDVDSW 616
Cdd:cd00821  77 ------LQADSEEERQEW 88
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 745-866 1.73e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 51.64  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  745 STPVPPPvddtwlQSASSHSPTPQRRPVSSIHPPgrPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDL 824
Cdd:PRK14951 379 KTPARPE------AAAPAAAPVAQAAAAPAPAAA--PAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPA 450

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 56549121  825 FPAPPQIPSRPVRIPPGIPPGVPSRRP-PAAPSRPTIIRPAEP 866
Cdd:PRK14951 451 PPAQAAPETVAIPVRVAPEPAVASAAPaPAAAPAAARLTPTEE 493
PHA03247 PHA03247
large tegument protein UL36; Provisional
 740-868 5.13e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   740 STSTVSTPVPPPVDDTWLQSASSHSPTPQRRPvssihPPGRPPAVrgpTPGPPLIPVPvgAAASFSAPPIPSRPGPQSVf 819
Cdd:PHA03247 2676 ASSPPQRPRRRAARPTVGSLTSLADPPPPPPT-----PEPAPHAL---VSATPLPPGP--AAARQASPALPAAPAPPAV- 2744

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 56549121   820 ANSDLFPAPPQIPSRPvrIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSL 868
Cdd:PHA03247 2745 PAGPATPGGPARPARP--PTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791
PHA03247 PHA03247
large tegument protein UL36; Provisional
 746-855 5.17e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   746 TPvPPPVDDtwLQSASSHS-----PTPQRR-------PVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAAsfSAPPIPSRP 813
Cdd:PHA03247  360 TP-PSSLED--LSAGRHHPkraslPTRKRRsarhaatPFARGPGGDDQTRPAAPVPASVPTPAPTPVPA--SAPPPPATP 434

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 56549121   814 gPQSVFANSDLFPAPPQIPSRPVRIPPGIPPGVP-----------SRRPPAAP 855
Cdd:PHA03247  435 -LPSAEPGSDDGPAPPPERQPPAPATEPAPDDPDdatrkaldalrERRPPEPP 486
PHA03247 PHA03247
large tegument protein UL36; Provisional
 742-867 7.25e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 7.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   742 STVSTPVPPPVddtwlqsASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFA- 820
Cdd:PHA03247 2873 AKPAAPARPPV-------RRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAp 2945

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 56549121   821 NSDLFPAPPQIPSRPVRIPPG----IPPGVPSRRPPAAPSRPTiirPAEPS 867
Cdd:PHA03247 2946 TTDPAGAGEPSGAVPQPWLGAlvpgRVAVPRFRVPQPAPSREA---PASST 2993
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 738-867 7.88e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.78  E-value: 7.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   738 DISTSTVSTPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGpplipVPVGAAASFSAPPIPSRPGPQS 817
Cdd:PHA03307  177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA-----DDAGASSSDSSSSESSGCGWGP 251

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 56549121   818 VFANSDLFPAPPQIPSRPVRipPGIPPGVPSRRPPAAPSRPTIIRPAEPS 867
Cdd:PHA03307  252 ENECPLPRPAPITLPTRIWE--ASGWNGPSSRPGPASSSSSPRERSPSPS 299
PHA03247 PHA03247
large tegument protein UL36; Provisional
 739-868 8.52e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 8.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   739 ISTSTVSTPVPP-PVDDTWLQSASSHSPTPQRRPVSSIHPPGRP-PAVRGPTPGPPLIPVPVGAAAsfsAP--PIPSRPG 814
Cdd:PHA03247 2791 LSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAqPTAPPPPPGPPPPSLPLGGSV---APggDVRRRPP 2867

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 56549121   815 PQSVFANSdlfPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSL 868
Cdd:PHA03247 2868 SRSPAAKP---AAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-867 1.16e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   747 PVPPPVDDTWLQSASSHSPtpQRRPVSSIHPPGRPPAVRGPTpgPPLIPVPVGAAASFSAPPIPSR-------------P 813
Cdd:PHA03247 2645 TVPPPERPRDDPAPGRVSR--PRRARRLGRAAQASSPPQRPR--RRAARPTVGSLTSLADPPPPPPtpepaphalvsatP 2720

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 56549121   814 GPQSVFANSDLFPAPPQIPSRPVRIPPGIPPGVPSRRP-PAAPSRPTiiRPAEPS 867
Cdd:PHA03247 2721 LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPArPPTTAGPP--APAPPA 2773
PHA03247 PHA03247
large tegument protein UL36; Provisional
 759-870 1.38e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   759 SASSHSPTPQ--RRPVSSI------HPPGRPPAVRGP--TPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDLFPAP 828
Cdd:PHA03247 2677 SSPPQRPRRRaaRPTVGSLtsladpPPPPPTPEPAPHalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPAR 2756

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 56549121   829 PQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTII-----RPAEPSLLD 870
Cdd:PHA03247 2757 PARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAslsesRESLPSPWD 2803
PHA03247 PHA03247
large tegument protein UL36; Provisional
 743-868 1.39e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   743 TVSTPVPP-PVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASfSAPPIPSRPGPQSVFAN 821
Cdd:PHA03247 2716 VSATPLPPgPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA-GPPRRLTRPAVASLSES 2794

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 56549121   822 SDLFPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSL 868
Cdd:PHA03247 2795 RESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPP 2841
PHA03247 PHA03247
large tegument protein UL36; Provisional
 740-866 1.66e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   740 STSTVSTPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAvRGPTPGPPlIPVPvgaaASFSAPPIPSRPGPQsVF 819
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVR-RRPPSRSP-AAKP----AAPARPPVRRLARPA-VS 2892

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 56549121   820 ANSDLFPAPPQIPSRPvrippgippgvpsrRPPAAPSRPTIIRPAEP 866
Cdd:PHA03247 2893 RSTESFALPPDQPERP--------------PQPQAPPPPQPQPQPPP 2925
PHA03247 PHA03247
large tegument protein UL36; Provisional
 743-870 2.09e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   743 TVSTPVPPPVDDTWLQSASSHSPT--PQR-RPVSSIHPPGRPPAVRGPTPGPPLI-----PVPVGAAASFSAPPIPSRPG 814
Cdd:PHA03247 2567 SVPPPRPAPRPSEPAVTSRARRPDapPQSaRPRAPVDDRGDPRGPAPPSPLPPDThapdpPPPSPSPAANEPDPHPPPTV 2646

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 56549121   815 PQSVFANSDlfPAPPQIpSRPVRIPPGIPPGVPSrRPPAAPSRPTiIRPAEPSLLD 870
Cdd:PHA03247 2647 PPPERPRDD--PAPGRV-SRPRRARRLGRAAQAS-SPPQRPRRRA-ARPTVGSLTS 2697
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
747-868 2.37e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.95  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  747 PVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVP---------VGAAASFSAPPIPSRPGPQS 817
Cdd:PRK12323 410 PAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAaarpaaagpRPVAAAAAAAPARAAPAAAP 489

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56549121  818 VFANSDLFP---APPQIPSRPV-------RIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSL 868
Cdd:PRK12323 490 APADDDPPPweeLPPEFASPAPaqpdaapAGWVAESIPDPATADPDDAFETLAPAPAAAPA 550
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 745-867 7.02e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 7.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   745 STPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPV--------------PVGAAASFSAPPIP 810
Cdd:PHA03307   86 STPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlrpvgspgpppaasPPAAGASPAAVASD 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 56549121   811 SRPGPQSVFAnSDLFPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEPS 867
Cdd:PHA03307  166 AASSRQAALP-LSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPA 221
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 701-859 7.97e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 7.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   701 SSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPvddtwlqsASSHSPTPQRRPVSSIHPPGR 780
Cdd:PHA03307  234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGP--------ASSSSSPRERSPSPSPSSPGS 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   781 PPAVRGPTPGPPLIPVP-VGAAASFSAPPIP----SRPGPQSVFANSDLFPAPPQIPSRPVRIPPGIPPGVPSRRPPAAP 855
Cdd:PHA03307  306 GPAPSSPRASSSSSSSReSSSSSTSSSSESSrgaaVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP 385


                  ....
gi 56549121   856 SRPT 859
Cdd:PHA03307  386 TRRR 389
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 735-866 8.33e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.52  E-value: 8.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  735 IIGDISTSTVSTPVPPPVDDTWL-QSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAA--SFSAPPIPS 811
Cdd:PRK07764 662 ASDGGDGWPAKAGGAAPAAPPPApAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASApsPAADDPVPL 741

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 56549121  812 RPGPqsvfansDLFPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEP 866
Cdd:PRK07764 742 PPEP-------DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDD 789
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 747-866 9.22e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 9.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  747 PVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRG---PTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSD 823
Cdd:PRK07764 658 AVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAApaqPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADD 737

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 56549121  824 LFPAP--PQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEP 866
Cdd:PRK07764 738 PVPLPpePDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
PHA03247 PHA03247
large tegument protein UL36; Provisional
 758-866 1.07e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   758 QSASSHSPTPQRRPvssiHPPGRPPAV-------RGPTPGPPLIPVPvgaAASFSAPPIPsrPGPQSVFANSDLFPAPPQ 830
Cdd:PHA03247 2670 LGRAAQASSPPQRP----RRRAARPTVgsltslaDPPPPPPTPEPAP---HALVSATPLP--PGPAAARQASPALPAAPA 2740

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 56549121   831 IPSRPVRIPPGIPPGVPSRRP-PAAPSRPTiiRPAEP 866
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPtTAGPPAPA--PPAAP 2775
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 520-616 1.22e-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: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 520 VIRRGWLtinnisLMKGGS----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKgfMSNKHVFAIFNTEQRN 595
Cdd:cd01252   3 PDREGWL------LKLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                        90       100       110
                ....*....|....*....|....*....|....
gi 56549121 596 VYK------DLRQIE-------LACDSQEDVDSW 616
Cdd:cd01252  75 VIKacktdsDGKVVEgnhtvyrISAASEEERDEW 108
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 765-870 1.43e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 44.85  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  765 PTPQRRPVS-SIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDLFPAPPqIPSRPVRIPPGIP 843
Cdd:PHA02682  87 ACAAPAPACpACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPP-LPTPKPAPAAKPI 165

                         90       100       110
                 ....*....|....*....|....*....|
gi 56549121  844 PGVPSRRPPAAP--SRPTI-IRPAEPSLLD 870
Cdd:PHA02682 166 FLHNQLPPPDYPaaSCPTIeTAPAASPVLE 195
PHA03378 PHA03378
EBNA-3B; Provisional
 749-865 1.51e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  749 PPPVDDTWLQSAS-SHSPTPQ----RRPVSSIHPPGRPPAvRGPTPGPPLIPVPVG----AAASFSAPPIPSRPGPQSVF 819
Cdd:PHA03378 659 ITPYKPTWTQIGHiPYQPSPTgantMLPIQWAPGTMQPPP-RAPTPMRPPAAPPGRaqrpAAATGRARPPAAAPGRARPP 737

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 56549121  820 ANSDLFPAPPQipSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAE 865
Cdd:PHA03378 738 AAAPGRARPPA--AAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQ 781
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
765-868 3.34e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  765 PTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSvfansdlfPAPPQIPsrPVRIPPGIPP 844
Cdd:PRK12323 375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRS--------PAPEALA--AARQASARGP 444

                         90       100
                 ....*....|....*....|....*
gi 56549121  845 GVPSRRPPAAPSRPT-IIRPAEPSL 868
Cdd:PRK12323 445 GGAPAPAPAPAAAPAaAARPAAAGP 469
PHA01929 PHA01929
putative scaffolding protein
 741-835 4.86e-04

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 43.12  E-value: 4.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  741 TSTVSTPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGP----TPGPPLIPVPVGAAASFSAPPIPSRPGPQ 816
Cdd:PHA01929   1 TTQNEQQLPPGLAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAPqqlaIPTQQPQPVPTSAMTPHVVQQAPAQPAPA 80

                         90
                 ....*....|....*....
gi 56549121  817 SVFANSDLFPAPPQIPSRP 835
Cdd:PHA01929  81 APPAAGAALPEALEVPPPP 99
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
759-867 5.48e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  759 SASSHSPTPQRRPVSsihPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDLFPAPPQIPSRPVRI 838
Cdd:PRK12323 452 PAPAAAPAAAARPAA---AGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPD 528

                         90       100
                 ....*....|....*....|....*....
gi 56549121  839 PPGIPPGVPSRRPPAAPSRPTIIRPAEPS 867
Cdd:PRK12323 529 PATADPDDAFETLAPAPAAAPAPRAAAAT 557
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
758-867 5.80e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  758 QSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFAN-----SDLFPAPPQIP 832
Cdd:PRK07003 413 KAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSasapaSDAPPDAAFEP 492

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 56549121  833 SRP-VRIPPGIPPGVPSRRPPAAPSRPTII-RPAEPS 867
Cdd:PRK07003 493 APRaAAPSAATPAAVPDARAPAAASREDAPaAAAPPA 529
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 750-867 7.31e-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: 39.33  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   750 PPVDDTWLQSASSHSPT-PQRRPVSSI-HPPGRPPAVRGPTPGPPlipvpvgaAASFSAPpiPSRPgpqsvfanSDLFPA 827
Cdd:pfam16058   1 PSSSITEPPRDPSGSYGePPRAPSSSYtEPQRDPSSSITEPPADP--------SSSYTEP--PRDP--------SGSYTE 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 56549121   828 PPQIPSrpvrippgippgVPSRRPPAAPSRPTIIRPAEPS 867
Cdd:pfam16058  63 PQRDPS------------SSSTEPQRDPSSSITEPPRDPS 90
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 758-867 7.37e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 7.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  758 QSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPP---------LIPVPVGAAASFSAPPIPSRPGPQSVFANSD--LFP 826
Cdd:PRK07764 602 APASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPaeasaapapGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAapAAP 681

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 56549121  827 APPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEPS 867
Cdd:PRK07764 682 PPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPP 722
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
745-864 8.73e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.91  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  745 STPVPPPVDDTWLQSA-SSHSPTPQRRPVSSIHP-PGRPPAVRGP-TPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFAN 821
Cdd:PRK07003 421 TRAEAPPAAPAPPATAdRGDDAADGDAPVPAKANaRASADSRCDErDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPS 500

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 56549121  822 SDLFPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPA 864
Cdd:PRK07003 501 AATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 746-835 1.24e-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: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   746 TPVPPPVDDTWLQSASSHSPTPQRRPVSS-IHPPGRPPAVRGPTPGPPLIPVPVGAaaSFSAPPIPSrpgPQSVFANSDL 824
Cdd:pfam03154 180 AASPPSPPPPGTTQAATAGPTPSAPSVPPqGSPATSQPPNQTQSTAAPHTLIQQTP--TLHPQRLPS---PHPPLQPMTQ 254

                          90
                  ....*....|.
gi 56549121   825 FPAPPQIPSRP 835
Cdd:pfam03154 255 PPPPSQVSPQP 265
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 740-866 1.33e-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: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   740 STSTVSTPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPgrppavRGPTPGPPLIPVPVGAAASFSAP-PIPS------- 811
Cdd:pfam03154 202 SAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQ------RLPSPHPPLQPMTQPPPPSQVSPqPLPQpslhgqm 275

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 56549121   812 RPGPQSVFANSDLFPAPpqIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEP 866
Cdd:pfam03154 276 PPMPHSLQTGPSHMQHP--VPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTP 328
PHA03247 PHA03247
large tegument protein UL36; Provisional
 749-864 1.46e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   749 PPPVDDTWLQSASSHS-PTPQRRP-------VSSIHPPGRPP-AVRGPTPGPPLIPvPVGAAASFSAPPIPSRPGPQSvf 819
Cdd:PHA03247 2552 PPPLPPAAPPAAPDRSvPPPRPAPrpsepavTSRARRPDAPPqSARPRAPVDDRGD-PRGPAPPSPLPPDTHAPDPPP-- 2628

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 56549121   820 ansdlfPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPA 864
Cdd:PHA03247 2629 ------PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRA 2667
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 740-811 1.61e-03

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: 38.56  E-value: 1.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56549121   740 STSTVSTPVPPPVDDTWLQSASSHSPT-PQRRPVSSIHPPGRPPAVRGPTPGPPlipvPVGaaaSFSAPP-IPS 811
Cdd:pfam16058  24 SSSYTEPQRDPSSSITEPPADPSSSYTePPRDPSGSYTEPQRDPSSSSTEPQRD----PSS---SITEPPrDPS 90
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
 757-829 1.73e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 41.42  E-value: 1.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56549121  757 LQSASSHSPTPQRRPVS----SIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDLFPAPP 829
Cdd:PHA03201   1 MKRARSRSPSPPRRPSPprptPPRSPDASPEETPPSPPGPGAEPPPGRAAGPAAPRRRPRGCPAGVTFSSSAPPRPP 77
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 755-859 1.79e-03

Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 38.91  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   755 TWLQSASSHSPTPqrrPVSSIHPPgrPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDlfPAPPQ---I 831
Cdd:pfam12526  19 TWSTSGFSSCFSP---PESAHPDP--PPPVGDPRPPVVDTPPPVSAVWVLPPPSEPAAPEPDLVPPVTG--PAGPPsplA 91

                          90       100
                  ....*....|....*....|....*...
gi 56549121   832 PSRPVRippgippgvpsrRPPAAPSRPT 859
Cdd:pfam12526  92 PPAPAQ------------KPPLPPPRPQ 107
PHA03378 PHA03378
EBNA-3B; Provisional
 745-856 2.13e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.98  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  745 STPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPP-IPSRPGPQSvfansd 823
Cdd:PHA03378 705 RPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAaAPGAPTPQP------ 778

                         90       100       110
                 ....*....|....*....|....*....|...
gi 56549121  824 lfpaPPQIPSRPvrippgippgvpSRRPPAAPS 856
Cdd:PHA03378 779 ----PPQAPPAP------------QQRPRGAPT 795
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 747-866 2.77e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 39.64  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   747 PVPPPVDDTWL--QSASSHSPTPQRRPVSSIHPPgrPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDL 824
Cdd:pfam15240  56 PQPPASDDPPGppPPGGPQQPPPQGGKQKPQGPP--PQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPP 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 56549121   825 FPAPPQIPSRPvrippgipPGVPSRRPPAAPSRPTiiRPAEP 866
Cdd:pfam15240 134 QGGNQQGPPPP--------PPGNPQGPPQRPPQPG--NPQGP 165
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 760-856 3.68e-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: 39.42  E-value: 3.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 760 ASSHSPTPQRRPvssihppgrppavrGPTPGPPliPVPV-------GAAASFSAPPIPSRPGPQSVFANSDLFPA-PPQI 831
Cdd:cd21576 109 ASSGSSDPARGS--------------SPTLGSE--PAPAsgedavsGPESSFGAPAIPSAPAAPGAPAVSGEVPGgAPGA 172

                        90       100
                ....*....|....*....|....*
gi 56549121 832 PSRPvrippgiPPGVPSRRPPAAPS 856
Cdd:cd21576 173 GPAP-------AAGPAPRRRPVTPA 190
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 747-863 3.73e-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: 40.91  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   747 PVPPPVDDTWLQSASSHSPTPQRRPvSSIHPPGRPPAVRGPTP-----GPPLIPVP-VGAAASFSAPPIPSRPGPQSVFA 820
Cdd:pfam03154 310 PPGPSPAAPGQSQQRIHTPPSQSQL-QSQQPPREQPLPPAPLSmphikPPPTTPIPqLPNPQSHKHPPHLSGPSPFQMNS 388

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 56549121   821 NsdlFPAPPQIpsRPVrippgipPGVPSRRPPAAPSRPTIIRP 863
Cdd:pfam03154 389 N---LPPPPAL--KPL-------SSLSTHHPPSAHPPPLQLMP 419
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 747-857 5.21e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   747 PVPPPVDDTW--LQSASSHSPTPQRRPVSsihPPGRPPAVRGPTPGPPLIPVPVGAAASfSAPPIPSRPGPQSVFANSDL 824
Cdd:PHA03307  126 PPPSPAPDLSemLRPVGSPGPPPAASPPA---AGASPAAVASDAASSRQAALPLSSPEE-TARAPSSPPAEPPPSTPPAA 201

                          90       100       110
                  ....*....|....*....|....*....|...
gi 56549121   825 FPAPPQIPSRPVRippgippgVPSRRPPAAPSR 857
Cdd:PHA03307  202 ASPRPPRRSSPIS--------ASASSPAPAPGR 226
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
742-858 6.29e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  742 STVSTPVPPPVDDTWLQSASSHSPT--PQRRPVSSIHPPGRPPAVRGPTPGPPlIPVPVGAAASFSAPPIPSRPGPQSVF 819
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAapPAAPAAAPAAAAAARAVAAAPARRSP-APEALAAARQASARGPGGAPAPAPAP 454

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 56549121  820 ANSDLFPAPPQIPsrPVRIPPGIPPGVPSRRPPAAPSRP 858
Cdd:PRK12323 455 AAAPAAAARPAAA--GPRPVAAAAAAAPARAAPAAAPAP 491
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 520-616 6.61e-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: 6.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 520 VIRRGWLTinnislMKGGS-----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGF-MSNKHVFAIFNTEQ 593
Cdd:cd13248   7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                        90       100
                ....*....|....*....|...
gi 56549121 594 RNVYkdlrqieLACDSQEDVDSW 616
Cdd:cd13248  81 RTYY-------FAADTAEEMEQW 96
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 740-870 7.92e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 7.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  740 STSTVSTPVPPPvddtwlQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPlipvPVGAAASFSAPPIPSRPGPQSVF 819
Cdd:PRK07764 394 PAAAAPSAAAAA------PAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPA----PPSPAGNAPAGGAPSPPPAAAPS 463

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  820 ANSDlfPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTI---------IRPAEPSLLD 870
Cdd:PRK07764 464 AQPA--PAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAApagaddaatLRERWPEILA 521
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 747-835 8.02e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 38.23  E-value: 8.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121    747 PVPPPVDDTWLQSASSHSPTPQRRPVssihppgRPPAVRGPTPGPPLIPVPVGAAasfsAPPIPSRPGPQSVFAnsdLFP 826
Cdd:smart00818  75 PVPGQHSMTPTQHHQPNLPQPAQQPF-------QPQPLQPPQPQQPMQPQPPVHP----IPPLPPQPPLPPMFP---MQP 140


                   ....*....
gi 56549121    827 APPQIPSRP 835
Cdd:smart00818 141 LPPLLPDLP 149
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 744-867 8.35e-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: 39.75  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   744 VSTPVPppvddtwLQSASSHSPTPQRRPVSSI---HPP-GRPPAVR-----GPTPGPPLIPvPV-------GAAASFSAP 807
Cdd:pfam03154 378 LSGPSP-------FQMNSNLPPPPALKPLSSLsthHPPsAHPPPLQlmpqsQQLPPPPAQP-PVltqsqslPPPAASHPP 449

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56549121   808 PIPSRPGP-QSVFANSDLFPAPPQIPSRPVRIPPGIPPGVPSRRPP-AAPSRPTIIRPAEPS 867
Cdd:pfam03154 450 TSGLHQVPsQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPsSASVSSSGPVPAAVS 511
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 740-837 8.77e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.70  E-value: 8.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  740 STSTVSTPVPPPvddtwlqsASSHSPTPQRRPVSSIHPPGRPPAVRgPTPGPPLIPVPVGAAASFSAPP------IPSRP 813
Cdd:PRK14951 396 QAAAAPAPAAAP--------AAAASAPAAPPAAAPPAPVAAPAAAA-PAAAPAAAPAAVALAPAPPAQAapetvaIPVRV 466

                         90       100
                 ....*....|....*....|....
gi 56549121  814 GPQSVFANSDLFPAPPQIPSRPVR 837
Cdd:PRK14951 467 APEPAVASAAPAPAAAPAAARLTP 490
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 768-869 9.08e-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: 37.75  E-value: 9.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121 768 QRRPVSSIHPPGRPPAVRGPTPGPPLIPV-PVGAAASFSAP-PIPS------RPGPQSVFANSDLFPAPPQIP-SRPVRi 838
Cdd:cd21975  38 ATREVAKGPGPPGPAWKPDGADSPGLVTAaPHLLAANVLAPlRGPSvegsslESGDADMGSDSDVAPASGAAAsTSPES- 116

                        90       100       110
                ....*....|....*....|....*....|.
gi 56549121 839 ppgippgvpSRRPPAAPSRPTIIRPAEPSLL 869
Cdd:cd21975 117 ---------SSDAASSPSPLSLLHPGEAGLE 138
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 745-862 9.47e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.22  E-value: 9.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  745 STPVPPPvddtwlQSASSHSPTPQRRPVSSIHPPGRPPavrgpTPGPP------LIPVPVGAAASFSAPPIPsRPGPQSV 818
Cdd:PHA03264 261 SKGYEPP------PAPSGGSPAPPGDDRPEAKPEPGPV-----EDGAPgretggEGEGPEPAGRDGAAGGEP-KPGPPRP 328

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 56549121  819 FANSDLFPAPPQIPSRPvrippgippgvpsrRPPAAPSRPTIIR 862
Cdd:PHA03264 329 APDADRPEGWPSLEAIT--------------FPPPTPATPAVPR 358
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 746-856 9.73e-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: 39.75  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121   746 TPVPPP--VDDTWLQSASSHSPTP------QRRPVSSIHP------PGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPS 811
Cdd:pfam03154 253 TQPPPPsqVSPQPLPQPSLHGQMPpmphslQTGPSHMQHPvppqpfPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQS 332

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 56549121   812 RPGPQSVFANSDLFPAP---PQIPSRPVRIPPGIPPGVPSRRPP--AAPS 856
Cdd:pfam03154 333 QLQSQQPPREQPLPPAPlsmPHIKPPPTTPIPQLPNPQSHKHPPhlSGPS 382
PHA02030 PHA02030
hypothetical protein
 781-868 9.79e-03

hypothetical protein


Pssm-ID: 222843 [Multi-domain]  Cd Length: 336  Bit Score: 39.19  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549121  781 PPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFAnsdlfPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTI 860
Cdd:PHA02030 256 KPKSKAAGSNLPAVPNVAADAGSAAAPAVPAAAAAVAQAA-----PSVPQVPNVAVLPDVPQVAPVAAPAAPEVPAVPVV 330


                 ....*...
gi 56549121  861 irPAEPSL 868
Cdd:PHA02030 331 --PAAPQV 336
 
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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