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Conserved domains on  [gi|568958779|ref|XP_006510039|]
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dynamin-2 isoform X5 [Mus musculus]

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 7.92e-163

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: 473.98  E-value: 7.92e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779     6 MEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779    86 CKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFIS 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779   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 ...
 215-498 1.84e-143

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: 425.78  E-value: 1.84e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  215 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  295 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  375 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELISTVRQCTSKLSSYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568958779  455 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFAN 498
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLN 283
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 524-635 1.20e-71

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: 231.06  E-value: 1.20e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 524 NQVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVY 603
Cdd:cd01256    1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568958779 604 KDLRQIELACDSQEDVDSWKASFLRAGVYPEK 635
Cdd:cd01256   81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
655-745 1.30e-30

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.69  E-value: 1.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  655 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 568958779  735 LKEALNIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 743-874 1.06e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  743 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 822
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568958779  823 SVfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTiiRPAEPSL 874
Cdd:PHA03247 2806 DP-----PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSL 2850
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 7.92e-163

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: 473.98  E-value: 7.92e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779     6 MEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779    86 CKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFIS 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779   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 2.40e-148

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


Pssm-ID: 206738  Cd Length: 278  Bit Score: 438.22  E-value: 2.40e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFS--------KTEYAEFLHCKSKKFTDFDEVRQE 100
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMD 180
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERK 257
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568958779 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 ...
 215-498 1.84e-143

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: 425.78  E-value: 1.84e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  215 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  295 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  375 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELISTVRQCTSKLSSYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568958779  455 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFAN 498
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLN 283
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 524-635 1.20e-71

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: 231.06  E-value: 1.20e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 524 NQVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVY 603
Cdd:cd01256    1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568958779 604 KDLRQIELACDSQEDVDSWKASFLRAGVYPEK 635
Cdd:cd01256   81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 1.06e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 222.49  E-value: 1.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779   34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLI--------FSKTEYAEFLhcksKKFTDFDEVRQEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGespgasegAVKVEYKDGE----KKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  106 DRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqikDMILQFIsRESSLILAVTPANMDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 568958779  186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 1.30e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.69  E-value: 1.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  655 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 568958779  735 LKEALNIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 6.93e-26

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 101.93  E-value: 6.93e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779   654 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 568958779   734 ALKEALNIIGDI 745
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 526-629 1.53e-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: 1.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779   526 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 601
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 568958779   602 VYKDLRQIELACDSQEDVDSWKASFLRA 629
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 526-629 1.99e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  526 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 601
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 568958779  602 VykdlRQIELACDSQEDVDSWKASFLRA 629
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 743-874 1.06e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  743 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 822
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568958779  823 SVfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTiiRPAEPSL 874
Cdd:PHA03247 2806 DP-----PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSL 2850
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 746-839 2.77e-06

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


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 46.26  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  746 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 823
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 568958779  824 VFANNDP---FSAPPQIPS 839
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 768-875 1.10e-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: 40.83  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 768 GHSPTPQRRPVSSVHPPGRPPAVRGP--TPGPPLIPMPVGATSSFSAPPI--------PSRPGPQSVFANNDPFSAP-PQ 836
Cdd:cd21975   20 GVRPDPEGAGLAAGLDVRATREVAKGpgPPGPAWKPDGADSPGLVTAAPHllaanvlaPLRGPSVEGSSLESGDADMgSD 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568958779 837 IPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLL 875
Cdd:cd21975  100 SDVAPASGAAASTSPESSSDAASSPSPLSLLHPGEAGLE 138
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 7.92e-163

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: 473.98  E-value: 7.92e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779     6 MEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779    86 CKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFIS 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779   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 2.40e-148

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


Pssm-ID: 206738  Cd Length: 278  Bit Score: 438.22  E-value: 2.40e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFS--------KTEYAEFLHCKSKKFTDFDEVRQE 100
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMD 180
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERK 257
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568958779 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 ...
 215-498 1.84e-143

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: 425.78  E-value: 1.84e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  215 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  295 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  375 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELISTVRQCTSKLSSYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568958779  455 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFAN 498
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLN 283
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 524-635 1.20e-71

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: 231.06  E-value: 1.20e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 524 NQVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVY 603
Cdd:cd01256    1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568958779 604 KDLRQIELACDSQEDVDSWKASFLRAGVYPEK 635
Cdd:cd01256   81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 1.06e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 222.49  E-value: 1.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779   34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLI--------FSKTEYAEFLhcksKKFTDFDEVRQEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGespgasegAVKVEYKDGE----KKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  106 DRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqikDMILQFIsRESSLILAVTPANMDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 568958779  186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 1.30e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.69  E-value: 1.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  655 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 568958779  735 LKEALNIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 6.93e-26

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 101.93  E-value: 6.93e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779   654 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 568958779   734 ALKEALNIIGDI 745
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 526-629 1.53e-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: 1.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779   526 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 601
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 568958779   602 VYKDLRQIELACDSQEDVDSWKASFLRA 629
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 526-629 1.99e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  526 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 601
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 568958779  602 VykdlRQIELACDSQEDVDSWKASFLRA 629
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 743-874 1.06e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  743 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 822
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568958779  823 SVfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTiiRPAEPSL 874
Cdd:PHA03247 2806 DP-----PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSL 2850
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 528-622 2.03e-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: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 528 RRGWLTINNISLMKGGsKEYWFVLTAESLSWYKDEEEKEKKY--MLPLDN-LKIRDVEKGfmSNKHVFAIFNTEQRNVYk 604
Cdd:cd00821    1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                         90
                 ....*....|....*...
gi 568958779 605 dlrqieLACDSQEDVDSW 622
Cdd:cd00821   77 ------LQADSEEERQEW 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 746-873 1.32e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  746 STSTVSTPVPPPvddtwlqntsghsPTPQRRP---VSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRP--- 819
Cdd:PHA03247 2694 SLTSLADPPPPP-------------PTPEPAPhalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARParp 2760

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568958779  820 ----GPQSVFANNDPFSAPPQIPSRPArippgippgvpsrRAPAAPSRPTIIRPAEPS 873
Cdd:PHA03247 2761 pttaGPPAPAPPAAPAAGPPRRLTRPA-------------VASLSESRESLPSPWDPA 2805
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 746-839 2.77e-06

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


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 46.26  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  746 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 823
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 568958779  824 VFANNDP---FSAPPQIPS 839
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 746-873 6.56e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  746 STSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPM--PVGATSSFSAPPIPSRPGPqs 823
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAapARPPVRRLARPAVSRSTES-- 2897

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568958779  824 vFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 873
Cdd:PHA03247 2898 -FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT 2946
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 751-872 9.27e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 49.33  E-value: 9.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 751 STPVPPPvddtwlQNTSGHSPTPQRRPVSSVHPPgrPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDP 830
Cdd:PRK14951 379 KTPARPE------AAAPAAAPVAQAAAAPAPAAA--PAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPA 450

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568958779 831 FSAPPQIPSRPARIPPGIPPGVPSRR-APAAPSRPTIIRPAEP 872
Cdd:PRK14951 451 PPAQAAPETVAIPVRVAPEPAVASAApAPAAAPAAARLTPTEE 493
PHA03247 PHA03247
large tegument protein UL36; Provisional
 772-872 1.23e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  772 TPQRRPvssvHPPGRPPAV-------RGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPfsAPPQIPSRPAri 844
Cdd:PHA03247 2678 SPPQRP----RRRAARPTVgsltslaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP--APPAVPAGPA-- 2749

                          90       100
                  ....*....|....*....|....*...
gi 568958779  845 PPGIPPGVPSRRAPAAPSRPTiiRPAEP 872
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPA--PPAAP 2775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-873 2.81e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  748 STVSTPVPPPVddtwlqnTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFA- 826
Cdd:PHA03247 2873 AKPAAPARPPV-------RRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAp 2945

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568958779  827 NNDPFSAPPQIPSRPARIPPGIPPGVPS---RRAPA-APSRPTiirPAEPS 873
Cdd:PHA03247 2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAvprFRVPQpAPSREA---PASST 2993
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 751-873 3.98e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  751 STPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPM--------------PVGATSSFSAPPIP 816
Cdd:PHA03307   86 STPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlrpvgspgpppaasPPAAGASPAAVASD 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568958779  817 SRPGPQ-SVFANNDPFSAPPqiPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 873
Cdd:PHA03307  166 AASSRQaALPLSSPEETARA--PSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPA 221
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 744-873 4.12e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  744 DISTSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLipmpvGATSSFSAPPIPSRPGPQS 823
Cdd:PHA03307  177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDA-----GASSSDSSSSESSGCGWGP 251

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568958779  824 VFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 873
Cdd:PHA03307  252 ENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPS 301
PHA03247 PHA03247
large tegument protein UL36; Provisional
 753-873 4.98e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  753 PVPPPVDDTwlqntsgHSPTPQR-RPVSSVHPPGRPPAVRGPT--PGPPLIPMPVGATSSFSAPPIPSR----------- 818
Cdd:PHA03247 2645 TVPPPERPR-------DDPAPGRvSRPRRARRLGRAAQASSPPqrPRRRAARPTVGSLTSLADPPPPPPtpepaphalvs 2717

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568958779  819 --PGPQSVFANNDPFSAPPQIPSRPArippgippGVPSRRAPAAPSRPTiiRPAEPS 873
Cdd:PHA03247 2718 atPLPPGPAAARQASPALPAAPAPPA--------VPAGPATPGGPARPA--RPPTTA 2764
PHA03247 PHA03247
large tegument protein UL36; Provisional
 771-872 5.52e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  771 PTPQRR-------PVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSfsAPPIPSRPGPQSVFANND-PFSAPPQIPSRPA 842
Cdd:PHA03247  381 PTRKRRsarhaatPFARGPGGDDQTRPAAPVPASVPTPAPTPVPAS--APPPPATPLPSAEPGSDDgPAPPPERQPPAPA 458

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568958779  843 RIPPGIPPGVPSRRA-PAAPSRptiiRPAEP 872
Cdd:PHA03247  459 TEPAPDDPDDATRKAlDALRER----RPPEP 485
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 526-622 1.20e-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: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 526 VIRRGWLtinnisLMKGGS----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKgfMSNKHVFAIFNTEQRN 601
Cdd:cd01252    3 PDREGWL------LKLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568958779 602 VYK------DLRQIE-------LACDSQEDVDSW 622
Cdd:cd01252   75 VIKacktdsDGKVVEgnhtvyrISAASEEERDEW 108
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 769-861 1.26e-04

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 44.34  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 769 HSPTPQRRPVSSVHPPgrppavrgptPGPPLIPMPVGATSSFSAPPIPSRPG----------PQSVFANNDPfsappqip 838
Cdd:PHA03418  40 HHPNPQEDPDKNPSPP----------PDPPLTPRPPAQPNGHNKPPVTKQPGgegteedhqaPLAADADDDP-------- 101

                         90       100
                 ....*....|....*....|...
gi 568958779 839 sRPARIPPGIPPGVPSRRAPAAP 861
Cdd:PHA03418 102 -RPGKRSKADEHGPAPGRAALAP 123
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 770-863 1.30e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 45.72  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 770 SPTPQRRPVSSVHPPGRPPAVRGPTPGPP-------LIPMPVGAtssfSAPPIPSRPGPQSVFANNDPfSAPPQIPSRPA 842
Cdd:PHA03321 443 PPPPRARPGSTPACARRARAQRARDAGPEyvdplgaLRRLPAGA----APPPEPAAAPSPATYYTRMG-GGPPRLPPRNR 517

                         90       100
                 ....*....|....*....|.
gi 568958779 843 RippgippgVPSRRAPAAPSR 863
Cdd:PHA03321 518 A--------TETLRPDWGPPA 530
PHA03247 PHA03247
large tegument protein UL36; Provisional
 771-872 1.39e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  771 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLI-----PMPVGATSSFSAPPIPSRPGPQSVFANNDP--------------- 830
Cdd:PHA03247 2592 PPQSARPRAPVDDRGDPRGPAPPSPLPPDThapdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvsrprrarrlg 2671

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568958779  831 ----FSAPPQIPSRPARIPPGIPPGVPSRRAPAAP---SRPTIIRPAEP 872
Cdd:PHA03247 2672 raaqASSPPQRPRRRAARPTVGSLTSLADPPPPPPtpePAPHALVSATP 2720
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
753-873 1.39e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.64  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 753 PVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMP---------VGATSSFSAPPIPSRPGPQS 823
Cdd:PRK12323 410 PAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAaarpaaagpRPVAAAAAAAPARAAPAAAP 489

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568958779 824 VFANNDP---------FSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 873
Cdd:PRK12323 490 APADDDPppweelppeFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAA 548
PHA03247 PHA03247
large tegument protein UL36; Provisional
 745-864 2.10e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  745 ISTSTVSTPVPPPvddtwlqntsghSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVgatssfSAPPIPSRPGPQSV 824
Cdd:PHA03247 2891 VSRSTESFALPPD------------QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR------PQPPLAPTTDPAGA 2952

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568958779  825 FANNDPFSAP---PQIPSRPARIPPGIPPGVPSRRAPAAPSRP 864
Cdd:PHA03247 2953 GEPSGAVPQPwlgALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
771-874 2.87e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 771 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSvfanndpfsaPPQIPSRPARIPPGIPP 850
Cdd:PRK12323 375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRS----------PAPEALAAARQASARGP 444

                         90       100
                 ....*....|....*....|....*
gi 568958779 851 GVPSRRAPAAPSRPT-IIRPAEPSL 874
Cdd:PRK12323 445 GGAPAPAPAPAAAPAaAARPAAAGP 469
PHA03247 PHA03247
large tegument protein UL36; Provisional
 745-872 3.17e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  745 ISTSTVSTPVPP-PVDDTWLQNTSGHSPTPQRRPVSSVHPPGRP-PAVRGPTPGPPLIPMPVGATSsfsAP--PIPSRPG 820
Cdd:PHA03247 2791 LSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAqPTAPPPPPGPPPPSLPLGGSV---APggDVRRRPP 2867

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568958779  821 PQSVFANNdpfSAPPQIP---------SRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEP 872
Cdd:PHA03247 2868 SRSPAAKP---AAPARPPvrrlarpavSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925
PHA01929 PHA01929
putative scaffolding protein
 747-842 3.93e-04

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 43.51  E-value: 3.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 747 TSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGP----TPGPPLIPMPVGATSSFSAPPIPSRPgpq 822
Cdd:PHA01929   1 TTQNEQQLPPGLAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAPqqlaIPTQQPQPVPTSAMTPHVVQQAPAQP--- 77

                         90       100
                 ....*....|....*....|
gi 568958779 823 svfannDPFSAPPQIPSRPA 842
Cdd:PHA01929  78 ------APAAPPAAGAALPE 91
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 753-872 5.02e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 753 PVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRG---PTPGPPLIPMPVGATSSFSAPPIPSRPG--PQSVFAN 827
Cdd:PRK07764 658 AVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAApaqPAPAPAATPPAGQADDPAAQPPQAAQGAsaPSPAADD 737

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568958779 828 NDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEP 872
Cdd:PRK07764 738 PVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 741-872 6.32e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 741 IIGDISTSTVSTPVPPPVDDTWL-QNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPG--PPLIPMPVGATSSFSAPPIPS 817
Cdd:PRK07764 662 ASDGGDGWPAKAGGAAPAAPPPApAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAaqPPQAAQGASAPSPAADDPVPL 741

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568958779 818 RPGPQSVFANNDPFSAPPQIPSRPARIPPGIPPgVPSRRAPAAPSRPTIIRPAEP 872
Cdd:PRK07764 742 PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP-PPSPPSEEEEMAEDDAPSMDD 795
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 707-865 7.73e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  707 SSADQSSLMEESAEQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVddtwlqntSGHSPTPQRRPVSSVHPPGR 786
Cdd:PHA03307  234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA--------SSSSSPRERSPSPSPSSPGS 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  787 PPAVRGPTPGPPLIPMP---VGATSSFSAPP--IPSRPGPQSVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAP 861
Cdd:PHA03307  306 GPAPSSPRASSSSSSSRessSSSTSSSSESSrgAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP 385


                  ....
gi 568958779  862 SRPT 865
Cdd:PHA03307  386 TRRR 389
PHA03247 PHA03247
large tegument protein UL36; Provisional
 766-876 8.81e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  766 TSGHSPTPQRRPVSSV------HPPGRPPAVRGP--TPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPPQI 837
Cdd:PHA03247 2680 PQRPRRRAARPTVGSLtsladpPPPPPTPEPAPHalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568958779  838 PSRPARIPPGIPPGVPSRRAPAAPSRPTII-----RPAEPSLLD 876
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVAslsesRESLPSPWD 2803
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 735-873 9.89e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 9.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  735 LKEALNIIGDISTSTVSTPVPPPVDDtwLQNTSGHSPTPQRRPVSSVHPPGRPPAVR-----GPTPGPPLIP-----MPV 804
Cdd:PHA03307   10 LIEAAAEGGEFFPRPPATPGDAADDL--LSGSQGQLVSDSAELAAVTVVAGAAACDRfepptGPPPGPGTEApanesRST 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568958779  805 GATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPSR--------PARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 873
Cdd:PHA03307   88 PTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPaspppspaPDLSEMLRPVGSPGPPPAASPPAAGASPAAVAS 164
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 768-875 1.10e-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: 40.83  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 768 GHSPTPQRRPVSSVHPPGRPPAVRGP--TPGPPLIPMPVGATSSFSAPPI--------PSRPGPQSVFANNDPFSAP-PQ 836
Cdd:cd21975   20 GVRPDPEGAGLAAGLDVRATREVAKGpgPPGPAWKPDGADSPGLVTAAPHllaanvlaPLRGPSVEGSSLESGDADMgSD 99

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568958779 837 IPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLL 875
Cdd:cd21975  100 SDVAPASGAAASTSPESSSDAASSPSPLSLLHPGEAGLE 138
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 766-873 1.24e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 766 TSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANND--PFSAPPQIPSRPAR 843
Cdd:PRK07764 604 ASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDgwPAKAGGAAPAAPPP 683

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568958779 844 IPPGIPPGVPSRRAPAAP-SRPTIIRPAEPS 873
Cdd:PRK07764 684 APAPAAPAAPAGAAPAQPaPAPAATPPAGQA 714
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
 715-821 1.34e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 42.13  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 715 MEESAEQAQRRDDMLRMYHALKEALNIIGDI-STSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPP---GRPPAV 790
Cdd:PRK14963 315 LDEQMERFARRSDALSLELALLHALLALGGApSEGVAAVAPPAPAPADLTQRLNRLEKEVRSLRSAPTAAAtaaGAPLPD 394

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568958779 791 RGPTPGPPliPMPVGATSSFSAPPIPSRPGP 821
Cdd:PRK14963 395 FDPRPRGP--PAPEPARSAEAPPLVAPAAAP 423
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 755-865 1.36e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 41.91  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 755 PPPVddtwlqnTSGHSPTPQRRPVSSVHPPGRPPavrgpTPGPP------LIPMPVGATSSFSAPPIPsRPGPQSVFANN 828
Cdd:PHA03264 266 PPPA-------PSGGSPAPPGDDRPEAKPEPGPV-----EDGAPgretggEGEGPEPAGRDGAAGGEP-KPGPPRPAPDA 332

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568958779 829 DPFSAPPQIPSRParippgippgvPSRRAPAAPSRPT 865
Cdd:PHA03264 333 DRPEGWPSLEAIT-----------FPPPTPATPAVPR 358
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-874 1.56e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  751 STPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDP 830
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD 2861

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568958779  831 FSAPPqiPSRPARIPpgippgvpsrraPAAPSRPTIIRPAEPSL 874
Cdd:PHA03247 2862 VRRRP--PSRSPAAK------------PAAPARPPVRRLARPAV 2891
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 753-841 1.90e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.02  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  753 PVPPPVDDtwlqntsGHSPTPQRRPVSSVHPPGR-------PPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVF 825
Cdd:pfam15240  56 PQPPASDD-------PPGPPPPGGPQQPPPQGGKqkpqgppPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQG 128

                          90
                  ....*....|....*.
gi 568958779  826 ANNDPFSAPPQIPSRP 841
Cdd:pfam15240 129 GGPPPQGGNQQGPPPP 144
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 767-862 2.94e-03

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


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 39.80  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 767 SGHSPtpqRRPVSSVHPPGRPPAVRGPTPGPPLIPMPV-GATSSFSAPPIPSRPG-PQSVFANNDPFSAPPQIPSRPAri 844
Cdd:cd21576  103 SGEAP---RASSGSSDPARGSSPTLGSEPAPASGEDAVsGPESSFGAPAIPSAPAaPGAPAVSGEVPGGAPGAGPAPA-- 177

                         90
                 ....*....|....*...
gi 568958779 845 ppgipPGVPSRRAPAAPS 862
Cdd:cd21576  178 -----AGPAPRRRPVTPA 190
PHA03247 PHA03247
large tegument protein UL36; Provisional
 728-870 4.73e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779  728 MLRMYHALKE-ALNIIGDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSS-VHPPGRPP-AVRGPTPGPPLIPMPV 804
Cdd:PHA03247 2533 MLTWIRGLEElASDDAGDPPPPLPPAAPPAAPDRS--VPPPRPAPRPSEPAVTSrARRPDAPPqSARPRAPVDDRGDPRG 2610

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568958779  805 GATSSfSAPPIPSRPGPqsvfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPA 870
Cdd:PHA03247 2611 PAPPS-PLPPDTHAPDP--------PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRA 2667
PHA03378 PHA03378
EBNA-3B; Provisional
 755-871 6.25e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 755 PPPVDDTWLQ--------NTSGHSPT--PQRRPvSSVHPPGRPPAVRGPTPGPPlIPMPVGATSSFSAPPIPSRPGPQSV 824
Cdd:PHA03378 659 ITPYKPTWTQighipyqpSPTGANTMlpIQWAP-GTMQPPPRAPTPMRPPAAPP-GRAQRPAAATGRARPPAAAPGRARP 736

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568958779 825 FANNDPFSAPPQipSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAE 871
Cdd:PHA03378 737 PAAAPGRARPPA--AAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQ 781
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
766-872 6.46e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 766 TSGHSPTPQRRPVSSVHPPG---RPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPS--- 839
Cdd:PRK12323 447 APAPAPAPAAAPAAAARPAAagpRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAesi 526

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568958779 840 -RPArIPPGIPPGVPSRRAPAAPSRPTIIRPAEP 872
Cdd:PRK12323 527 pDPA-TADPDDAFETLAPAPAAAPAPRAAAATEP 559
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 526-622 6.72e-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: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958779 526 VIRRGWLTinnislMKGGS-----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGF-MSNKHVFAIFNTEQ 599
Cdd:cd13248    7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                         90       100
                 ....*....|....*....|...
gi 568958779 600 RNVYkdlrqieLACDSQEDVDSW 622
Cdd:cd13248   81 RTYY-------FAADTAEEMEQW 96
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
 523-559 7.50e-03

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but 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: 275402  Cd Length: 116  Bit Score: 37.22  E-value: 7.50e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568958779 523 PNQVIRRGWLTInnISLMKGGSKEYWFVLTAESLSWY 559
Cdd:cd13215   18 SGAVIKSGYLSK--RSKRTLRYTRYWFVLKGDTLSWY 52
 
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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