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Conserved domains on  [gi|1387275293|ref|XP_024849880|]
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dynamin-2 isoform X14 [Bos taurus]

Protein Classification

DLP_1 and Dynamin_M domain-containing protein( domain architecture ID 10171892)

protein containing domains DLP_1, Dynamin_M, PH_dynamin, and GED

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 173-456 4.52e-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: 428.86  E-value: 4.52e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 173 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRTALAAERKFFLSHPAYRHIADRMGTPHLQKTLNQQLTNHIRESLP 252
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 253 ALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 332
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 333 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQIVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 412
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1387275293 413 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFAN 456
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLN 283
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 36-252 3.42e-113

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: 346.15  E-value: 3.42e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  36 AEYAEFLHCKSRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQPQDIEYQIK 115
Cdd:cd08771    58 EEWGEFLHLKSKEFTDFEELREEIEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIR 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 116 DMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGV 192
Cdd:cd08771   138 SMVKSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGV 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387275293 193 VNRSQKDIEGKKDIRTALAAERKFFLSHPAYRH-IADRMGTPHLQKTLNQQLTNHIRESLP 252
Cdd:cd08771   218 VNRSQKDIDSGKSIEEALEAEEEFFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 488-597 6.24e-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: 6.24e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 488 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 567
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1387275293 568 LRQIELACDSQEDVDSWKASFLRAGVYPEK 597
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
617-707 7.25e-31

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 116.07  E-value: 7.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 617 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHA 696
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1387275293 697 LKEALNIIGDI 707
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 707-834 6.31e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 6.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  707 ISTSTVSTPVPP-PVDDTWIQNTSSHSPTPQRRPVSSVHPPGRP-PAVRGPTPGPPLIPVPVG------------PASFS 772
Cdd:PHA03247  2791 LSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAqPTAPPPPPGPPPPSLPLGgsvapggdvrrrPPSRS 2870

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387275293  773 APPIPSRPG-------PHPGVFANNDPFSAPPQIPSRParippgippgvpsrRPPAAPSRPTIIRPAEP 834
Cdd:PHA03247  2871 PAAKPAAPArppvrrlARPAVSRSTESFALPPDQPERP--------------PQPQAPPPPQPQPQPPP 2925
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 173-456 4.52e-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: 428.86  E-value: 4.52e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 173 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRTALAAERKFFLSHPAYRHIADRMGTPHLQKTLNQQLTNHIRESLP 252
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 253 ALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 332
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 333 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQIVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 412
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1387275293 413 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFAN 456
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLN 283
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 36-252 3.42e-113

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: 346.15  E-value: 3.42e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  36 AEYAEFLHCKSRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQPQDIEYQIK 115
Cdd:cd08771    58 EEWGEFLHLKSKEFTDFEELREEIEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIR 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 116 DMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGV 192
Cdd:cd08771   138 SMVKSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGV 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387275293 193 VNRSQKDIEGKKDIRTALAAERKFFLSHPAYRH-IADRMGTPHLQKTLNQQLTNHIRESLP 252
Cdd:cd08771   218 VNRSQKDIDSGKSIEEALEAEEEFFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 33-203 2.67e-108

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: 331.84  E-value: 2.67e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293   33 TSWAEYAEFLHCKSRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQPQDIEY 112
Cdd:smart00053  70 KSKTEYAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEY 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  113 QIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGV 192
Cdd:smart00053 150 QIKKMIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGV 229

                          170
                   ....*....|.
gi 1387275293  193 VNRSQKDIEGK 203
Cdd:smart00053 230 VNRSQKDIEGK 240
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 488-597 6.24e-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: 6.24e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 488 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 567
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1387275293 568 LRQIELACDSQEDVDSWKASFLRAGVYPEK 597
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
36-165 1.68e-42

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 152.39  E-value: 1.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  36 AEYAEFLhcksRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQpqdieyqik 115
Cdd:pfam00350  53 VEYKDGE----KKFEDFSELREEIEKETEKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ--------- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1387275293 116 DMILQFIsRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKL 165
Cdd:pfam00350 120 ELTKEYI-KPADIILAVTPANVDLSTSEALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
617-707 7.25e-31

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 116.07  E-value: 7.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 617 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHA 696
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1387275293 697 LKEALNIIGDI 707
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
616-707 5.83e-26

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 102.31  E-value: 5.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  616 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYH 695
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1387275293  696 ALKEALNIIGDI 707
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 488-591 1.42e-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: 1.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  488 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 563
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1387275293  564 VYKDLRQIELACDSQEDVDSWKASFLRA 591
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 488-591 2.10e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 488 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 563
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1387275293 564 VykdlRQIELACDSQEDVDSWKASFLRA 591
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 707-834 6.31e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 6.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  707 ISTSTVSTPVPP-PVDDTWIQNTSSHSPTPQRRPVSSVHPPGRP-PAVRGPTPGPPLIPVPVG------------PASFS 772
Cdd:PHA03247  2791 LSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAqPTAPPPPPGPPPPSLPLGgsvapggdvrrrPPSRS 2870

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387275293  773 APPIPSRPG-------PHPGVFANNDPFSAPPQIPSRParippgippgvpsrRPPAAPSRPTIIRPAEP 834
Cdd:PHA03247  2871 PAAKPAAPArppvrrlARPAVSRSTESFALPPDQPERP--------------PQPQAPPPPQPQPQPPP 2925
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 715-831 3.77e-05

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: 47.45  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 715 PVPPPVDDTWIQNT---------SSHSP---TPQRRPVSSVHP-PGRPPAVRGPTP--------GPPLIPVPVGPASF-- 771
Cdd:pfam03154 221 TQSTAAPHTLIQQTptlhpqrlpSPHPPlqpMTQPPPPSQVSPqPLPQPSLHGQMPpmphslqtGPSHMQHPVPPQPFpl 300

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387275293 772 -------SAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIPPGippgvpsrrPPAAPSRPTIIRP 831
Cdd:pfam03154 301 tpqssqsQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPL---------PPAPLSMPHIKPP 358
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
 708-801 2.02e-03

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 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 KLF4, which is related to the N-terminal domains of KLF1 and KLF2.


Pssm-ID: 409228 [Multi-domain]  Cd Length: 335  Bit Score: 41.22  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 708 STSTVSTPVpppvdDTWIQNTSSHSpTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPAS--FSAPPIPSRPGPHPG 785
Cdd:cd21582   215 STCTISRPM-----DGHLGGNSQHG-FSQRAPLPSRTTPSGGPGGGNSSTAESLMSRDHHPSSqvLSHPPLPLPQGYHPS 288

                          90
                  ....*....|....*.
gi 1387275293 786 vfANNDPFSAPPQIPS 801
Cdd:cd21582   289 --PGYPPFPPPPSQPQ 302
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 173-456 4.52e-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: 428.86  E-value: 4.52e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 173 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRTALAAERKFFLSHPAYRHIADRMGTPHLQKTLNQQLTNHIRESLP 252
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 253 ALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 332
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 333 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQIVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 412
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1387275293 413 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFAN 456
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLN 283
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 36-252 3.42e-113

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: 346.15  E-value: 3.42e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  36 AEYAEFLHCKSRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQPQDIEYQIK 115
Cdd:cd08771    58 EEWGEFLHLKSKEFTDFEELREEIEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIR 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 116 DMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGV 192
Cdd:cd08771   138 SMVKSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGV 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387275293 193 VNRSQKDIEGKKDIRTALAAERKFFLSHPAYRH-IADRMGTPHLQKTLNQQLTNHIRESLP 252
Cdd:cd08771   218 VNRSQKDIDSGKSIEEALEAEEEFFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 33-203 2.67e-108

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: 331.84  E-value: 2.67e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293   33 TSWAEYAEFLHCKSRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQPQDIEY 112
Cdd:smart00053  70 KSKTEYAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEY 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  113 QIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGV 192
Cdd:smart00053 150 QIKKMIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGV 229

                          170
                   ....*....|.
gi 1387275293  193 VNRSQKDIEGK 203
Cdd:smart00053 230 VNRSQKDIEGK 240
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 488-597 6.24e-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: 6.24e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 488 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 567
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1387275293 568 LRQIELACDSQEDVDSWKASFLRAGVYPEK 597
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
36-165 1.68e-42

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 152.39  E-value: 1.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  36 AEYAEFLhcksRKFTDFEEVRQEIEAETDRVTGTNKGISPVPINLRIYSPHVLNLTLIDLPGITKVPVGDQpqdieyqik 115
Cdd:pfam00350  53 VEYKDGE----KKFEDFSELREEIEKETEKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ--------- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1387275293 116 DMILQFIsRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKL 165
Cdd:pfam00350 120 ELTKEYI-KPADIILAVTPANVDLSTSEALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
617-707 7.25e-31

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 116.07  E-value: 7.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 617 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHA 696
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1387275293 697 LKEALNIIGDI 707
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
616-707 5.83e-26

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 102.31  E-value: 5.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  616 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYH 695
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1387275293  696 ALKEALNIIGDI 707
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 488-591 1.42e-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: 1.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  488 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 563
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1387275293  564 VYKDLRQIELACDSQEDVDSWKASFLRA 591
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 488-591 2.10e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 488 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 563
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1387275293 564 VykdlRQIELACDSQEDVDSWKASFLRA 591
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 490-584 1.90e-07

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 49.46  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 490 RRGWLTINNISLMKGGsKEYWFVLTAESLSWYKDEEEKEKKY--MLPLDN-LKIRDVEKGfmSNKHVFAIFNTEQRNVYk 566
Cdd:cd00821     1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                          90
                  ....*....|....*...
gi 1387275293 567 dlrqieLACDSQEDVDSW 584
Cdd:cd00821    77 ------LQADSEEERQEW 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 707-834 6.31e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 6.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  707 ISTSTVSTPVPP-PVDDTWIQNTSSHSPTPQRRPVSSVHPPGRP-PAVRGPTPGPPLIPVPVG------------PASFS 772
Cdd:PHA03247  2791 LSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAqPTAPPPPPGPPPPSLPLGgsvapggdvrrrPPSRS 2870

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387275293  773 APPIPSRPG-------PHPGVFANNDPFSAPPQIPSRParippgippgvpsrRPPAAPSRPTIIRPAEP 834
Cdd:PHA03247  2871 PAAKPAAPArppvrrlARPAVSRSTESFALPPDQPERP--------------PQPQAPPPPQPQPQPPP 2925
PHA03247 PHA03247
large tegument protein UL36; Provisional
 705-836 8.13e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 8.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  705 GDISTSTVSTPVPPPVDDTWIqnTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAP--PIPSRPGP 782
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAGPA--TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESREslPSPWDPAD 2806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  783 HPGVF---ANNDPFSAPPQIPSRPARIPPGIPPGVPS--------------------RRP--------PAAPSRPTIIRP 831
Cdd:PHA03247  2807 PPAAVlapAAALPPAASPAGPLPPPTSAQPTAPPPPPgppppslplggsvapggdvrRRPpsrspaakPAAPARPPVRRL 2886


                   ....*
gi 1387275293  832 AEPSL 836
Cdd:PHA03247  2887 ARPAV 2891
PHA03247 PHA03247
large tegument protein UL36; Provisional
 715-835 1.16e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  715 PVPPPVDDtwiqntsSHSPTPQR-RPVSSVHPPGRPPAVRGPT--PGPPLIPVPVGP-ASFSAPPIPSR---PGPHPGVF 787
Cdd:PHA03247  2645 TVPPPERP-------RDDPAPGRvSRPRRARRLGRAAQASSPPqrPRRRAARPTVGSlTSLADPPPPPPtpePAPHALVS 2717

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387275293  788 ANNDP---------FSAPPQIPSRPARIPPGIPPGVPSRRP-PAAPSRPTiiRPAEPS 835
Cdd:PHA03247  2718 ATPLPpgpaaarqaSPALPAAPAPPAVPAGPATPGGPARPArPPTTAGPP--APAPPA 2773
PHA03247 PHA03247
large tegument protein UL36; Provisional
 710-835 1.25e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  710 STVSTPVPPPVddtwiqnTSSHSPTPQRRPVSSVHPPGRPPAVRGP-TPGPPLIPVPVGPASFSAPPIPSRPGPHPGVFA 788
Cdd:PHA03247  2873 AKPAAPARPPV-------RRLARPAVSRSTESFALPPDQPERPPQPqAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP 2945

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1387275293  789 NNDPFSAPPQIPSRPARIPPG----IPPGVPSRRPPAAPSRPTiirPAEPS 835
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGAlvpgRVAVPRFRVPQPAPSREA---PASST 2993
PHA03247 PHA03247
large tegument protein UL36; Provisional
 708-835 1.93e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  708 STSTVSTPVPPPvddtwiqntsshsPTPQRRP---VSSVHPPGRPPAVRGPTPGPPLIPVP-------VGPASFSAPPIP 777
Cdd:PHA03247  2694 SLTSLADPPPPP-------------PTPEPAPhalVSATPLPPGPAAARQASPALPAAPAPpavpagpATPGGPARPARP 2760

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387275293  778 SRPGPHPGVFANNDPFSAPPQ----------IPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEPS 835
Cdd:PHA03247  2761 PTTAGPPAPAPPAAPAAGPPRrltrpavaslSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828
PHA03247 PHA03247
large tegument protein UL36; Provisional
 728-836 2.77e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  728 TSSHSPT--PQRR----PVSSV------HPPGRPPAVRgPTPGPPLIPVPVGPASF--SAPPIPSRPGPHPGVFANNDPF 793
Cdd:PHA03247  2674 AQASSPPqrPRRRaarpTVGSLtsladpPPPPPTPEPA-PHALVSATPLPPGPAAArqASPALPAAPAPPAVPAGPATPG 2752

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1387275293  794 S----APPQIPSRPARIPPGippgvpsrRPPAAPSRPTIIRPAEPSL 836
Cdd:PHA03247  2753 GparpARPPTTAGPPAPAPP--------AAPAAGPPRRLTRPAVASL 2791
PHA03247 PHA03247
large tegument protein UL36; Provisional
 733-838 3.40e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 3.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  733 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAPPIPSRPGPHPGVFA---NNDPFSAPPQIpsRPARIPPG 809
Cdd:PHA03247  2592 PPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPppeRPRDDPAPGRV--SRPRRARR 2669

                           90       100
                   ....*....|....*....|....*....
gi 1387275293  810 IPPGVPSRRPPAAPSRPTiIRPAEPSLLD 838
Cdd:PHA03247  2670 LGRAAQASSPPQRPRRRA-ARPTVGSLTS 2697
PHA03379 PHA03379
EBNA-3A; Provisional
 708-834 7.23e-06

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 49.67  E-value: 7.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 708 STSTVSTPVPPPVDDTW---IQNTSSHSPTP----QRRPVSSVHPPGRPPAV-RGPTPGPPLIPVPVGP----------- 768
Cdd:PHA03379  436 SHGSAQVPEPPPVHDLEpgpLHDQHSMAPCPvaqlPPGPLQDLEPGDQLPGVvQDGRPACAPVPAPAGPivrpweaslsq 515

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387275293 769 ------ASFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSR-PARIPPGIPPGVPSRRPPAAPSRPtiiRPAEP 834
Cdd:PHA03379  516 vpgvafAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQgPGETSGIVRVRERWRPAPWTPNPP---RSPSQ 585
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 732-838 7.25e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 49.71  E-value: 7.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 732 SPTPQRRPVSSVHPPGRPPAVRGPTPGPPL-IPVPVGPASFSAPPIPSRPGP-HPGVFANNDPFSAPPQI--PSRPARIP 807
Cdd:PRK14951  380 TPARPEAAAPAAAPVAQAAAAPAPAAAPAAaASAPAAPPAAAPPAPVAAPAAaAPAAAPAAAPAAVALAPapPAQAAPET 459

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1387275293 808 PGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD 838
Cdd:PRK14951  460 VAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 669-830 1.67e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  669 SSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVddtwiqntSSHSPTPQRRPVSSVHPPGR 748
Cdd:PHA03307   234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA--------SSSSSPRERSPSPSPSSPGS 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  749 PPAVRGPTPGPPLIPVP--VGPASFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPSRP 826
Cdd:PHA03307   306 GPAPSSPRASSSSSSSResSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP 385


                   ....
gi 1387275293  827 TIIR 830
Cdd:PHA03307   386 TRRR 389
PHA03247 PHA03247
large tegument protein UL36; Provisional
 733-823 1.99e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  733 PTPQRR-------PVSSVHPPGRPPAVRGPTPGPPLIPVPVgPASFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPAR 805
Cdd:PHA03247   381 PTRKRRsarhaatPFARGPGGDDQTRPAAPVPASVPTPAPT-PVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPAT 459

                           90       100
                   ....*....|....*....|....*..
gi 1387275293  806 IPPGIPPGVPS---------RRPPAAP 823
Cdd:PHA03247   460 EPAPDDPDDATrkaldalreRRPPEPP 486
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 713-834 2.47e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.79  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 713 STPVPPPvddtwiQNTSSHSPTPQRRPVSSVHPPgrPPAVRGPTPGPP--LIPVPVGPASFSAPPIPSRPGPHPGVFANN 790
Cdd:PRK14951  379 KTPARPE------AAAPAAAPVAQAAAAPAPAAA--PAAAASAPAAPPaaAPPAPVAAPAAAAPAAAPAAAPAAVALAPA 450

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1387275293 791 DPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPSrPTIIRPAEP 834
Cdd:PRK14951  451 PPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPA-AARLTPTEE 493
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 715-831 3.77e-05

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: 47.45  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 715 PVPPPVDDTWIQNT---------SSHSP---TPQRRPVSSVHP-PGRPPAVRGPTP--------GPPLIPVPVGPASF-- 771
Cdd:pfam03154 221 TQSTAAPHTLIQQTptlhpqrlpSPHPPlqpMTQPPPPSQVSPqPLPQPSLHGQMPpmphslqtGPSHMQHPVPPQPFpl 300

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387275293 772 -------SAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIPPGippgvpsrrPPAAPSRPTIIRP 831
Cdd:pfam03154 301 tpqssqsQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPL---------PPAPLSMPHIKPP 358
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 716-831 6.49e-05

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 45.96  E-value: 6.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 716 VPPPVDDTWIQNTSSHSPTPQRRPVSSVHPPGrPPAVRGPTP----GPPLIPVPVGPASFSAPPIPSRPGPHPGVFAnnd 791
Cdd:pfam15279 195 MPPPFLRPPPSIPQPNSPLSNPMLPGIGPPPK-PPRNLGPPSnpmhRPPFSPHHPPPPPTPPGPPPGLPPPPPRGFT--- 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1387275293 792 PFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPsrPTIIRP 831
Cdd:pfam15279 271 PPFGPPFPPVNMMPNPPEMNFGLPSLAPLVPP--VTVLVP 308
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 728-835 1.09e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 728 TSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAPPIPSRPGPHPGVFANND--PFSAPPQIPSRPAR 805
Cdd:PRK07764  604 ASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDgwPAKAGGAAPAAPPP 683

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1387275293 806 IPPGIPPGVPSRRPPAAP-SRPTIIRPAEPS 835
Cdd:PRK07764  684 APAPAAPAAPAGAAPAQPaPAPAATPPAGQA 714
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 715-831 1.12e-04

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: 45.91  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 715 PVPPPVDDTWIQNTSSHSPTPQRRPvSSVHPPGRPPAVRGPTPGPPLIPVPvgpasfsAPPIPSRPGP----HPGVFANN 790
Cdd:pfam03154 310 PPGPSPAAPGQSQQRIHTPPSQSQL-QSQQPPREQPLPPAPLSMPHIKPPP-------TTPIPQLPNPqshkHPPHLSGP 381

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1387275293 791 DPFSAPPQIPSRPAripPGIPPGVPSRRPPAAPSRPTIIRP 831
Cdd:pfam03154 382 SPFQMNSNLPPPPA---LKPLSSLSTHHPPSAHPPPLQLMP 419
PHA03247 PHA03247
large tegument protein UL36; Provisional
 710-834 1.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  710 STVSTPVPPPVDdTWIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFS------APPIPSR---P 780
Cdd:PHA03247  2523 EPVGEPVHPRML-TWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSrarrpdAPPQSARpraP 2601

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1387275293  781 GPHPGVFANNDPFSAPPQIPSRParippgippgvpsrRPPAAPSRPTIIRPAEP 834
Cdd:PHA03247  2602 VDDRGDPRGPAPPSPLPPDTHAP--------------DPPPPSPSPAANEPDPH 2641
PHA03247 PHA03247
large tegument protein UL36; Provisional
 713-834 1.17e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  713 STPVPPPVDDTWIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPG--PPLIPVPVGPASFSAPPIPSRP---GPHP-GV 786
Cdd:PHA03247  2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPlpPPTSAQPTAPPPPPGPPPPSLPlggSVAPgGD 2861

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1387275293  787 FANNDPFSAPPQIPSRPARippgippGVPSRRPPAAPSRPTIIRPAEP 834
Cdd:PHA03247  2862 VRRRPPSRSPAAKPAAPAR-------PPVRRLARPAVSRSTESFALPP 2902
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 488-584 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 1387275293 488 VIRRGWLtinnisLMKGGS----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKgfMSNKHVFAIFNTEQRN 563
Cdd:cd01252     3 PDREGWL------LKLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1387275293 564 VYK------DLRQIE-------LACDSQEDVDSW 584
Cdd:cd01252    75 VIKacktdsDGKVVEgnhtvyrISAASEEERDEW 108
PHA03247 PHA03247
large tegument protein UL36; Provisional
 711-836 1.33e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  711 TVSTPVPP-PVDDTWIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPvgPASFSAPPIPSRPGPHPGVFAN 789
Cdd:PHA03247  2716 VSATPLPPgPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAP--PAAPAAGPPRRLTRPAVASLSE 2793

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1387275293  790 NDPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPS-RPTIIRPAEPSL 836
Cdd:PHA03247  2794 SRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLpPPTSAQPTAPPP 2841
PHA03378 PHA03378
EBNA-3B; Provisional
 717-833 1.74e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 717 PPPVDDTWIQNTS-SHSPTPQ----RRPVSSVHPPGRPPAvRGPTPGPPLIPVPVGPASFSAPPIPSRPgPHPGVFANND 791
Cdd:PHA03378  659 ITPYKPTWTQIGHiPYQPSPTgantMLPIQWAPGTMQPPP-RAPTPMRPPAAPPGRAQRPAAATGRARP-PAAAPGRARP 736

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1387275293 792 PFSAPPQIP---SRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAE 833
Cdd:PHA03378  737 PAAAPGRARppaAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQ 781
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
715-796 2.58e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 715 PVPPPVDDTWIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAPPIPSRPGPHPGVFANNDPFS 794
Cdd:PRK12323  410 PAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAP 489


                  ..
gi 1387275293 795 AP 796
Cdd:PRK12323  490 AP 491
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 706-835 2.74e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  706 DISTSTVSTPVPPPVDDTWIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGpplipVPVGPASFSAPPIPSRPGPHPG 785
Cdd:PHA03307   177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA-----DDAGASSSDSSSSESSGCGWGP 251

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1387275293  786 VFANNDPFSAPPQIPSRPARipPGIPPGVPSRRPPAAPSRPTIIRPAEPS 835
Cdd:PHA03307   252 ENECPLPRPAPITLPTRIWE--ASGWNGPSSRPGPASSSSSPRERSPSPS 299
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 715-838 2.76e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 715 PVPPPVDDTWI-----------------QNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVG---PASFSAP 774
Cdd:PRK07764  658 AVPDASDGGDGwpakaggaapaapppapAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGasaPSPAADD 737

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387275293 775 PIPSRPGPHPGVFANNDPFSAPPQIPSRPArippgippgvpsrRPPAAPSRPTIIRPAEPSLLD 838
Cdd:PRK07764  738 PVPLPPEPDDPPDPAGAPAQPPPPPAPAPA-------------AAPAAAPPPSPPSEEEEMAED 788
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 706-834 2.83e-04

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: 44.76  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 706 DISTSTVSTPVPPPVDDTWIQNTSSHSPTPQRRP--VSSVHPPGRPP----------AVRGPTPGPPLIPVPVGPASfSA 773
Cdd:pfam03154 138 DQDNRSTSPSIPSPQDNESDSDSSAQQQILQTQPpvLQAQSGAASPPsppppgttqaATAGPTPSAPSVPPQGSPAT-SQ 216

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387275293 774 PPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEP 834
Cdd:pfam03154 217 PPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPP 277
PHA03247 PHA03247
large tegument protein UL36; Provisional
 690-832 3.08e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  690 MLRMYHALKE-ALNIIGDiSTSTVSTPVPPPVDDTWIQnTSSHSPTPQRRPVSS-VHPPGRPP-AVRGPTPGPPLIPVPV 766
Cdd:PHA03247  2533 MLTWIRGLEElASDDAGD-PPPPLPPAAPPAAPDRSVP-PPRPAPRPSEPAVTSrARRPDAPPqSARPRAPVDDRGDPRG 2610

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387275293  767 GPASFSAPPIPSRPGPhpgvfanndPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPA 832
Cdd:PHA03247  2611 PAPPSPLPPDTHAPDP---------PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRA 2667
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 717-802 3.16e-04

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: 41.22  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 717 PPPVDDtwiqNTSSHSPTPQrrPVSSVHPPgrPPAVRGPTPGPPLIPVPVGPASFSAPPIPSRPGPHPgvfanndpfSAP 796
Cdd:pfam12526  40 PPPVGD----PRPPVVDTPP--PVSAVWVL--PPPSEPAAPEPDLVPPVTGPAGPPSPLAPPAPAQKP---------PLP 102


                  ....*.
gi 1387275293 797 PQIPSR 802
Cdd:pfam12526 103 PPRPQR 108
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 708-797 3.74e-04

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 43.05  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 708 STSTVSTPVPPPVDDTW----IQNTSSHSPTPQRRPVSSVHPPGRP---PAVRGPTP-GP-------------------- 759
Cdd:pfam15822  52 STAPSTVPFGPAPTGMYpsipLTGPSPGPPAPFPPSGPSCPPPGGPypaPTVPGPGPiGPyptpnmpfpelprpygaptd 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1387275293 760 PLIPVPVGP--------------ASFSAPPIPSR-PGPHPGVFANNDPFSAPP 797
Cdd:pfam15822 132 PAAAAPSGPwgsmssgpwapgmgGQYPAPNMPYPsPGPYPAVPPPQSPGAAPP 184
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 703-834 4.04e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 703 IIGDISTSTVSTPVPPPVDDTWI-QNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVG---PASFSAPPIPS 778
Cdd:PRK07764  662 ASDGGDGWPAKAGGAAPAAPPPApAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGasaPSPAADDPVPL 741

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387275293 779 RPGPHPGVFANnDPFSAPPQIPSRPARIPPGIPPgVPSRRPPAAPSRPTIIRPAEP 834
Cdd:PRK07764  742 PPEPDDPPDPA-GAPAQPPPPPAPAPAAAPAAAP-PPSPPSEEEEMAEDDAPSMDD 795
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 731-805 4.06e-04

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 42.80  E-value: 4.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387275293 731 HSPTPQRRPVSSVHPPGRPPavrgPTPGPPLIpvpvgPASFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPAR 805
Cdd:PHA03418   40 HHPNPQEDPDKNPSPPPDPP----LTPRPPAQ-----PNGHNKPPVTKQPGGEGTEEDHQAPLAADADDDPRPGK 105
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 711-836 6.02e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 6.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  711 TVSTPVPPPVDDTWIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAPPIPS---------RPG 781
Cdd:PHA03307    69 TGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEmlrpvgspgPPP 148

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387275293  782 PHPGVFANNDPfSAPPQIPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSL 836
Cdd:PHA03307   149 AASPPAAGASP-AAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAA 202
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 711-837 6.59e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 42.54  E-value: 6.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 711 TVSTPVPP-----PVDDTWIQNTSSHSPTPQRRPVSSVH-PPGRPPAvrGPTPGPPlIPVPVGPASFSAPPIPSR--PGP 782
Cdd:PHA02682   36 APAAPCPPdadvdPLDKYSVKEAGRYYQSRLKANSACMQrPSGQSPL--APSPACA-APAPACPACAPAAPAPAVtcPAP 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387275293 783 HPGVFANNDPFSAPPQIPSRPARIPPgiPPGVPSRRPPAAPSRPTiIRP---AEPSLL 837
Cdd:PHA02682  113 APACPPATAPTCPPPAVCPAPARPAP--ACPPSTRQCPPAPPLPT-PKPapaAKPIFL 167
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 732-825 8.97e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 43.02  E-value: 8.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 732 SPTPQRRPVSSVHPPGRPPAVRGPTPGPP-------LIPVPVGPASfsaPPIPSRPGPHPGVFANNDpfSAPPQIPSRPA 804
Cdd:PHA03321  443 PPPPRARPGSTPACARRARAQRARDAGPEyvdplgaLRRLPAGAAP---PPEPAAAPSPATYYTRMG--GGPPRLPPRNR 517

                          90       100
                  ....*....|....*....|.
gi 1387275293 805 RippgippgVPSRRPPAAPSR 825
Cdd:PHA03321  518 A--------TETLRPDWGPPA 530
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 697-835 1.06e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  697 LKEALNIIGDISTSTVSTPVPPPVDDtwIQNTSSHSPTPQRRPVSSVHPPGRPPAVR-----GPTPGPPLIP-------- 763
Cdd:PHA03307    10 LIEAAAEGGEFFPRPPATPGDAADDL--LSGSQGQLVSDSAELAAVTVVAGAAACDRfepptGPPPGPGTEApanesrst 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387275293  764 -----VPVGPASFSAPPIPSRPGPHPGvfannDPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEPS 835
Cdd:PHA03307    88 ptwslSTLAPASPAREGSPTPPGPSSP-----DPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASP 159
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
726-826 1.14e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 726 QNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAPPI----PSRPGPHPGVFANNDPFSAP----- 796
Cdd:PRK12323  368 SGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAvaaaPARRSPAPEALAAARQASARgpgga 447

                          90       100       110
                  ....*....|....*....|....*....|
gi 1387275293 797 PQIPSRPArippgiPPGVPSRRPPAAPSRP 826
Cdd:PRK12323  448 PAPAPAPA------AAPAAAARPAAAGPRP 471
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 709-835 1.42e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  709 TSTVSTPVPPPVDDTWIQNTSSHSPTPQRRPVSSVHPPGRPPAV-----RGPTPGPPLIPVPV-GPASFSAPPIPSRPGP 782
Cdd:PHA03307    91 SLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLsemlrPVGSPGPPPAASPPaAGASPAAVASDAASSR 170

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1387275293  783 HPGVFANNDPFSAPPqiPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEPS 835
Cdd:PHA03307   171 QAALPLSSPEETARA--PSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPA 221
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 729-833 1.53e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  729 SSHSPTPQRRPVSSVHPPGrPPAVRGPTPGPPLIPVPVGPASFSAPPIPSRPGPHPGVFANndPFSAPPQIPSRPAripp 808
Cdd:PHA03307   829 GSESSGPARPPGAAARPPP-ARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAP--PKAAAAAPPAGAP---- 901

                           90       100
                   ....*....|....*....|....*
gi 1387275293  809 gippgvpSRRPPAAPSRPTIIRPAE 833
Cdd:PHA03307   902 -------APRPRPAPRVKLGPMPPG 919
PHA03378 PHA03378
EBNA-3B; Provisional
 714-824 1.64e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.98  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 714 TPVPPPvddtwiqntsSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASfSAPPIPSRPGPHPGvfanndPF 793
Cdd:PHA03378  702 TPMRPP----------AAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPA-AAPGRARPPAAAPG------RA 764

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1387275293 794 SAPPQIPSRPARIPPGIPPGVPSRRPPAAPS 824
Cdd:PHA03378  765 RPPAAAPGAPTPQPPPQAPPAPQQRPRGAPT 795
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
 708-801 2.02e-03

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 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 KLF4, which is related to the N-terminal domains of KLF1 and KLF2.


Pssm-ID: 409228 [Multi-domain]  Cd Length: 335  Bit Score: 41.22  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 708 STSTVSTPVpppvdDTWIQNTSSHSpTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPAS--FSAPPIPSRPGPHPG 785
Cdd:cd21582   215 STCTISRPM-----DGHLGGNSQHG-FSQRAPLPSRTTPSGGPGGGNSSTAESLMSRDHHPSSqvLSHPPLPLPQGYHPS 288

                          90
                  ....*....|....*.
gi 1387275293 786 vfANNDPFSAPPQIPS 801
Cdd:cd21582   289 --PGYPPFPPPPSQPQ 302
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 737-824 2.16e-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: 40.19  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 737 RRPVSSVHPPGRPPAVRGPTPGPPLIPVPV-GPA-SFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPArippgipPGV 814
Cdd:cd21576   108 RASSGSSDPARGSSPTLGSEPAPASGEDAVsGPEsSFGAPAIPSAPAAPGAPAVSGEVPGGAPGAGPAPA-------AGP 180

                          90
                  ....*....|
gi 1387275293 815 PSRRPPAAPS 824
Cdd:cd21576   181 APRRRPVTPA 190
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 708-801 2.31e-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: 38.17  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 708 STSTVSTPVPPPVDDTWIQ-NTSSHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipvpvgPASFSAPPI-PSRPGPHP 784
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP-------SGSYTEPQRdPSSSSTEP 74

                          90
                  ....*....|....*..
gi 1387275293 785 GVFANNDpFSAPPQIPS 801
Cdd:pfam16058  75 QRDPSSS-ITEPPRDPS 90
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
712-838 2.70e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 712 VSTPVPPPVddtwiQNTSSHSPTPQRRPVSSVHPPGR--PPAVRGPTPG--PPLIPVPVGPASFSapPIPSRPGPHPGVF 787
Cdd:PRK12323  451 APAPAAAPA-----AAARPAAAGPRPVAAAAAAAPARaaPAAAPAPADDdpPPWEELPPEFASPA--PAQPDAAPAGWVA 523

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1387275293 788 AN-NDPFSAPPQIP---SRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD 838
Cdd:PRK12323  524 ESiPDPATADPDDAfetLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFD 578
PHA03247 PHA03247
large tegument protein UL36; Provisional
 709-824 3.20e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  709 TSTVSTPVPPPVDDTWIQNTSS------------HSPTPQR---RPVSSVHPP----GRPPAVRGPTPGPplIPvPVGPA 769
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPlggsvapggdvrRRPPSRSpaaKPAAPARPPvrrlARPAVSRSTESFA--LP-PDQPE 2906

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387275293  770 SFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRPPAAPS 824
Cdd:PHA03247  2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQ 2961
PHA01929 PHA01929
putative scaffolding protein
 709-804 3.23e-03

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 40.42  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 709 TSTVSTPVPPPVDDTWIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGP----TPGPPLIPVPVGP-ASFSAPPIPSRPgph 783
Cdd:PHA01929    1 TTQNEQQLPPGLAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAPqqlaIPTQQPQPVPTSAmTPHVVQQAPAQP--- 77

                          90       100
                  ....*....|....*....|.
gi 1387275293 784 pgvfannDPFSAPPQIPSRPA 804
Cdd:PHA01929   78 -------APAAPPAAGAALPE 91
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 733-838 3.31e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 733 PTPQRRPVSSVHPPGRPPAVRGPTPGPPlipvpvGPASFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIPPGIPP 812
Cdd:PRK07764  413 AAAAPAAAAAPAPAAAPQPAPAPAPAPA------PPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPA 486

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1387275293 813 GVPSRRPPAAPSRPTI---------IRPAEPSLLD 838
Cdd:PRK07764  487 APAPAAAPAAPAAPAApagaddaatLRERWPEILA 521
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 728-838 4.54e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 728 TSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAPPIPSRPGPHPGVFANNDPFSAPPQIPSRPARIP 807
Cdd:PRK07764  639 ASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPA 718

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1387275293 808 PGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD 838
Cdd:PRK07764  719 AQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 715-825 4.57e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 4.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  715 PVPPPVDDTWIQNTSSHSPTPQRRPvSSVHPPGRPPAVRGPTPGPPLIPVPVGPASFSAPPIPSrPGPHPGVFANNDPFS 794
Cdd:PHA03307   126 PPPSPAPDLSEMLRPVGSPGPPPAA-SPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS-PPAEPPPSTPPAAAS 203

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1387275293  795 APPQIPSRPARippgippgVPSRRPPAAPSR 825
Cdd:PHA03307   204 PRPPRRSSPIS--------ASASSPAPAPGR 226
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-834 4.71e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 4.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293  748 RPPAVRGP-TPGPPLIPVPVGPASFSAPPIPSRPGP------------HPGVF---------ANNDPFSAPPQIP--SRP 803
Cdd:PHA03247  2482 RPAEARFPfAAGAAPDPGGGGPPDPDAPPAPSRLAPailpdepvgepvHPRMLtwirgleelASDDAGDPPPPLPpaAPP 2561

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1387275293  804 ARIPPGIPPGVPSRRP--PAAPSRPTiiRPAEP 834
Cdd:PHA03247  2562 AAPDRSVPPPRPAPRPsePAVTSRAR--RPDAP 2592
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 739-796 4.77e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 39.82  E-value: 4.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387275293 739 PVSSVHPPgrPPAVRGPTPGPPLIPVPVGPASfSAPPIPSRPGPHPGVFANNDPFSAP 796
Cdd:PLN02983  149 PVVMMQPP--PPHAMPPASPPAAQPAPSAPAS-SPPPTPASPPPAKAPKSSHPPLKSP 203
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 731-837 4.82e-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: 38.52  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 731 HSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPVPV----GPASFSAPPI--------PSRPGPHPGVFANNDPFSAPPQ 798
Cdd:cd21975    21 VRPDPEGAGLAAGLDVRATREVA-KGPGPPGPAWKPdgadSPGLVTAAPHllaanvlaPLRGPSVEGSSLESGDADMGSD 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1387275293 799 IPSRPARIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSLL 837
Cdd:cd21975   100 SDVAPASGAAASTSPESSSDAASSPSPLSLLHPGEAGLE 138
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
690-826 5.91e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 690 MLRMYhalkeALNIIGDISTSTVSTPVPPPVDDTWIQNTSSHSPTPqrRPVSSVHPPGRPPAVRGPTPGPPLIPVPVGPA 769
Cdd:PRK12323  357 LLRML-----AFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAP--APAAPPAAPAAAPAAAAAARAVAAAPARRSPA 429

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387275293 770 SFSAPPIPSRPGPHPGvfANNDPFSAPPQIP---SRPA----RIPPGIPPGVPSRRPPAAPSRP 826
Cdd:PRK12323  430 PEALAAARQASARGPG--GAPAPAPAPAAAPaaaARPAaagpRPVAAAAAAAPARAAPAAAPAP 491
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 488-584 6.35e-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: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 488 VIRRGWLTinnislMKGGS-----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGF-MSNKHVFAIFNTEQ 561
Cdd:cd13248     7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                          90       100
                  ....*....|....*....|...
gi 1387275293 562 RNVYkdlrqieLACDSQEDVDSW 584
Cdd:cd13248    81 RTYY-------FAADTAEEMEQW 96
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
 677-800 8.49e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 39.44  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387275293 677 MEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVddtwIQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPT 756
Cdd:PRK14963  315 LDEQMERFARRSDALSLELALLHALLALGGAPSEGVAAVAPPAP----APADLTQRLNRLEKEVRSLRSAPTAAATAAGA 390

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1387275293 757 PGPPLIPVPVGPASfsapPIPSRPGPHPgvfanndPFSAPPQIP 800
Cdd:PRK14963  391 PLPDFDPRPRGPPA----PEPARSAEAP-------PLVAPAAAP 423
 
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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