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Conserved domains on  [gi|1720430183|ref|XP_030099904|]
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dynamin-2 isoform X15 [Mus musculus]

Protein Classification

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 ...
 57-344 5.80e-146

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


:

Pssm-ID: 460033  Cd Length: 287  Bit Score: 426.93  E-value: 5.80e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  57 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 136
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 137 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 216
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 217 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 296
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1720430183 297 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQR 344
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 362-471 8.30e-71

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


:

Pssm-ID: 269958  Cd Length: 112  Bit Score: 226.05  E-value: 8.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 362 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 441
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1720430183 442 LRQIELACDSQEDVDSWKASFLRAGVYPEK 471
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-87 8.09e-50

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member smart00053:

Pssm-ID: 476819  Cd Length: 240  Bit Score: 174.30  E-value: 8.09e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183    1 MILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRS 80
Cdd:smart00053 154 MIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRS 233


                   ....*..
gi 1720430183   81 QKDIEGK 87
Cdd:smart00053 234 QKDIEGK 240
GED pfam02212
Dynamin GTPase effector domain;
491-581 2.05e-30

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 114.53  E-value: 2.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 491 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 570
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1720430183 571 LKEALNIIGDI 581
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 579-710 1.56e-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: 55.33  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  579 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 658
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720430183  659 SVfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTiiRPAEPSL 710
Cdd:PHA03247  2806 DP-----PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSL 2850
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 57-344 5.80e-146

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


Pssm-ID: 460033  Cd Length: 287  Bit Score: 426.93  E-value: 5.80e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  57 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 136
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 137 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 216
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 217 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 296
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1720430183 297 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQR 344
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 362-471 8.30e-71

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


Pssm-ID: 269958  Cd Length: 112  Bit Score: 226.05  E-value: 8.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 362 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 441
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1720430183 442 LRQIELACDSQEDVDSWKASFLRAGVYPEK 471
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 1-136 4.43e-61

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: 206.33  E-value: 4.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183   1 MILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVV 77
Cdd:cd08771   139 MVKSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVV 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  78 NRSQKDIEGKKDIRAALAAERKFFLSHPAYRH-MADRMGTPHLQKTLNQQLTNHIRESLP 136
Cdd:cd08771   219 NRSQKDIDSGKSIEEALEAEEEFFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 1-87 8.09e-50

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: 174.30  E-value: 8.09e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183    1 MILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRS 80
Cdd:smart00053 154 MIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRS 233


                   ....*..
gi 1720430183   81 QKDIEGK 87
Cdd:smart00053 234 QKDIEGK 240
GED pfam02212
Dynamin GTPase effector domain;
491-581 2.05e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 114.53  E-value: 2.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 491 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 570
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1720430183 571 LKEALNIIGDI 581
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
490-581 1.43e-25

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 100.77  E-value: 1.43e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  490 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 569
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1720430183  570 ALKEALNIIGDI 581
Cdd:smart00302  81 LLKKARQIIAAV 92
Dynamin_N pfam00350
Dynamin family;
1-49 1.46e-13

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 69.18  E-value: 1.46e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720430183   1 MILQFIsRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKL 49
Cdd:pfam00350 121 LTKEYI-KPADIILAVTPANVDLSTSEALFLAREVDPNGKRTIGVLTKA 168
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 362-465 1.16e-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: 1.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  362 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 437
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1720430183  438 VYKDLRQIELACDSQEDVDSWKASFLRA 465
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 362-465 1.74e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 362 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 437
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1720430183 438 VykdlRQIELACDSQEDVDSWKASFLRA 465
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 579-710 1.56e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  579 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 658
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720430183  659 SVfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTiiRPAEPSL 710
Cdd:PHA03247  2806 DP-----PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSL 2850
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 582-675 3.35e-06

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


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 45.87  E-value: 3.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 582 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 659
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 1720430183 660 VFANNDP---FSAPPQIPS 675
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 604-711 1.91e-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: 39.67  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 604 GHSPTPQRRPVSSVHPPGRPPAVRGP--TPGPPLIPMPVGATSSFSAPPI--------PSRPGPQSVFANNDPFSAP-PQ 672
Cdd:cd21975    20 GVRPDPEGAGLAAGLDVRATREVAKGpgPPGPAWKPDGADSPGLVTAAPHllaanvlaPLRGPSVEGSSLESGDADMgSD 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720430183 673 IPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLL 711
Cdd:cd21975   100 SDVAPASGAAASTSPESSSDAASSPSPLSLLHPGEAGLE 138
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 57-344 5.80e-146

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


Pssm-ID: 460033  Cd Length: 287  Bit Score: 426.93  E-value: 5.80e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  57 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 136
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 137 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 216
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 217 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 296
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1720430183 297 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQR 344
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 362-471 8.30e-71

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


Pssm-ID: 269958  Cd Length: 112  Bit Score: 226.05  E-value: 8.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 362 VIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKD 441
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1720430183 442 LRQIELACDSQEDVDSWKASFLRAGVYPEK 471
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 1-136 4.43e-61

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: 206.33  E-value: 4.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183   1 MILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVV 77
Cdd:cd08771   139 MVKSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVV 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  78 NRSQKDIEGKKDIRAALAAERKFFLSHPAYRH-MADRMGTPHLQKTLNQQLTNHIRESLP 136
Cdd:cd08771   219 NRSQKDIDSGKSIEEALEAEEEFFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 1-87 8.09e-50

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: 174.30  E-value: 8.09e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183    1 MILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRS 80
Cdd:smart00053 154 MIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRS 233


                   ....*..
gi 1720430183   81 QKDIEGK 87
Cdd:smart00053 234 QKDIEGK 240
GED pfam02212
Dynamin GTPase effector domain;
491-581 2.05e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 114.53  E-value: 2.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 491 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 570
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1720430183 571 LKEALNIIGDI 581
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
490-581 1.43e-25

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 100.77  E-value: 1.43e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  490 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 569
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1720430183  570 ALKEALNIIGDI 581
Cdd:smart00302  81 LLKKARQIIAAV 92
Dynamin_N pfam00350
Dynamin family;
1-49 1.46e-13

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 69.18  E-value: 1.46e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720430183   1 MILQFIsRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKL 49
Cdd:pfam00350 121 LTKEYI-KPADIILAVTPANVDLSTSEALFLAREVDPNGKRTIGVLTKA 168
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 362-465 1.16e-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: 1.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  362 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 437
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1720430183  438 VYKDLRQIELACDSQEDVDSWKASFLRA 465
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 362-465 1.74e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 55.65  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 362 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 437
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1720430183 438 VykdlRQIELACDSQEDVDSWKASFLRA 465
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 364-458 1.55e-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: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 364 RRGWLTINNISLMKGGsKEYWFVLTAESLSWYKDEEEKEKKY--MLPLDN-LKIRDVEKGfmSNKHVFAIFNTEQRNVYk 440
Cdd:cd00821     1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                          90
                  ....*....|....*...
gi 1720430183 441 dlrqieLACDSQEDVDSW 458
Cdd:cd00821    77 ------LQADSEEERQEW 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 579-710 1.56e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  579 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 658
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720430183  659 SVfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTiiRPAEPSL 710
Cdd:PHA03247  2806 DP-----PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP--GPPPPSL 2850
PHA03247 PHA03247
large tegument protein UL36; Provisional
 582-709 2.24e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  582 STSTVSTPVPPPvddtwlqntsghsPTPQRRP---VSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRP--- 655
Cdd:PHA03247  2694 SLTSLADPPPPP-------------PTPEPAPhalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARParp 2760

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430183  656 ----GPQSVFANNDPFSAPPQIPSRPArippgippgvpsrRAPAAPSRPTIIRPAEPS 709
Cdd:PHA03247  2761 pttaGPPAPAPPAAPAAGPPRRLTRPA-------------VASLSESRESLPSPWDPA 2805
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 582-675 3.35e-06

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


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 45.87  E-value: 3.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 582 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 659
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 1720430183 660 VFANNDP---FSAPPQIPS 675
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 582-709 8.40e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 8.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  582 STSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPM--PVGATSSFSAPPIPSRPGPqs 659
Cdd:PHA03247  2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAapARPPVRRLARPAVSRSTES-- 2897

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720430183  660 vFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 709
Cdd:PHA03247  2898 -FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT 2946
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 587-708 1.08e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 48.56  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 587 STPVPPPvddtwlQNTSGHSPTPQRRPVSSVHPPgrPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDP 666
Cdd:PRK14951  379 KTPARPE------AAAPAAAPVAQAAAAPAPAAA--PAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPA 450

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720430183 667 FSAPPQIPSRPARIPPGIPPGVPSRR-APAAPSRPTIIRPAEP 708
Cdd:PRK14951  451 PPAQAAPETVAIPVRVAPEPAVASAApAPAAAPAAARLTPTEE 493
PHA03247 PHA03247
large tegument protein UL36; Provisional
 608-708 1.88e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  608 TPQRRPvssvHPPGRPPAV-------RGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPfsAPPQIPSRPAri 680
Cdd:PHA03247  2678 SPPQRP----RRRAARPTVgsltslaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP--APPAVPAGPA-- 2749

                           90       100
                   ....*....|....*....|....*...
gi 1720430183  681 PPGIPPGVPSRRAPAAPSRPTiiRPAEP 708
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPA--PPAAP 2775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 584-709 4.21e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  584 STVSTPVPPPVddtwlqnTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFA- 662
Cdd:PHA03247  2873 AKPAAPARPPV-------RRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAp 2945

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720430183  663 NNDPFSAPPQIPSRPARIPPG----IPPGVPSRRAPAAPSRPTiirPAEPS 709
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGAlvpgRVAVPRFRVPQPAPSREA---PASST 2993
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 580-709 5.10e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 5.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  580 DISTSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLipmpvGATSSFSAPPIPSRPGPQS 659
Cdd:PHA03307   177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDA-----GASSSDSSSSESSGCGWGP 251

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720430183  660 VFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 709
Cdd:PHA03307   252 ENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPS 301
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 587-709 5.60e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 5.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  587 STPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPM--------------PVGATSSFSAPPIP 652
Cdd:PHA03307    86 STPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlrpvgspgpppaasPPAAGASPAAVASD 165

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430183  653 SRPGPQ-SVFANNDPFSAPPqiPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 709
Cdd:PHA03307   166 AASSRQaALPLSSPEETARA--PSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPA 221
PHA03247 PHA03247
large tegument protein UL36; Provisional
 589-709 8.15e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 8.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  589 PVPPPVDDTwlqntsgHSPTPQR-RPVSSVHPPGRPPAVRGPT--PGPPLIPMPVGATSSFSAPPIPSR----------- 654
Cdd:PHA03247  2645 TVPPPERPR-------DDPAPGRvSRPRRARRLGRAAQASSPPqrPRRRAARPTVGSLTSLADPPPPPPtpepaphalvs 2717

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430183  655 --PGPQSVFANNDPFSAPPQIPSRPArippgippGVPSRRAPAAPSRPTiiRPAEPS 709
Cdd:PHA03247  2718 atPLPPGPAAARQASPALPAAPAPPA--------VPAGPATPGGPARPA--RPPTTA 2764
PHA03247 PHA03247
large tegument protein UL36; Provisional
 607-708 8.29e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 8.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  607 PTPQRR-------PVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSfsAPPIPSRPGPQSVFANND-PFSAPPQIPSRPA 678
Cdd:PHA03247   381 PTRKRRsarhaatPFARGPGGDDQTRPAAPVPASVPTPAPTPVPAS--APPPPATPLPSAEPGSDDgPAPPPERQPPAPA 458

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1720430183  679 RIPPGIPPGVPSRRA-PAAPSRptiiRPAEP 708
Cdd:PHA03247   459 TEPAPDDPDDATRKAlDALRER----RPPEP 485
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 362-458 8.76e-05

General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 and the related proteins ARNO (ARF nucleotide-binding site opener)/cytohesin-2 and cytohesin-1 are ARF exchange factors that contain a pleckstrin homology (PH) domain thought to target these proteins to cell membranes through binding polyphosphoinositides. The PH domains of all three proteins exhibit relatively high affinity for PtdIns(3,4,5)P3. Within the Grp1 family, diglycine (2G) and triglycine (3G) splice variants, differing only in the number of glycine residues in the PH domain, strongly influence the affinity and specificity for phosphoinositides. The 2G variants selectively bind PtdIns(3,4,5)P3 with high affinity,the 3G variants bind PtdIns(3,4,5)P3 with about 30-fold lower affinity and require the polybasic region for plasma membrane targeting. These ARF-GEFs share a common, tripartite structure consisting of an N-terminal coiled-coil domain, a central domain with homology to the yeast protein Sec7, a PH domain, and a C-terminal polybasic region. The Sec7 domain is autoinhibited by conserved elements proximal to the PH domain. GRP1 binds to the DNA binding domain of certain nuclear receptors (TRalpha, TRbeta, AR, ER, but not RXR), and can repress thyroid hormone receptor (TR)-mediated transactivation by decreasing TR-complex formation on thyroid hormone response elements. ARNO promotes sequential activation of Arf6, Cdc42 and Rac1 and insulin secretion. Cytohesin acts as a PI 3-kinase effector mediating biological responses including cell spreading and adhesion, chemotaxis, protein trafficking, and cytoskeletal rearrangements, only some of which appear to depend on their ability to activate ARFs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269954  Cd Length: 119  Bit Score: 42.69  E-value: 8.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 362 VIRRGWLtinnisLMKGGS----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKgfMSNKHVFAIFNTEQRN 437
Cdd:cd01252     3 PDREGWL------LKLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720430183 438 VYK------DLRQIE-------LACDSQEDVDSW 458
Cdd:cd01252    75 VIKacktdsDGKVVEgnhtvyrISAASEEERDEW 108
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 605-697 1.29e-04

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 43.96  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 605 HSPTPQRRPVSSVHPPgrppavrgptPGPPLIPMPVGATSSFSAPPIPSRPG----------PQSVFANNDPfsappqip 674
Cdd:PHA03418   40 HHPNPQEDPDKNPSPP----------PDPPLTPRPPAQPNGHNKPPVTKQPGgegteedhqaPLAADADDDP-------- 101

                          90       100
                  ....*....|....*....|...
gi 1720430183 675 sRPARIPPGIPPGVPSRRAPAAP 697
Cdd:PHA03418  102 -RPGKRSKADEHGPAPGRAALAP 123
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
589-709 1.68e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 589 PVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMP---------VGATSSFSAPPIPSRPGPQS 659
Cdd:PRK12323  410 PAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAaarpaaagpRPVAAAAAAAPARAAPAAAP 489

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720430183 660 VFANNDP---------FSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 709
Cdd:PRK12323  490 APADDDPppweelppeFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAA 548
PHA03247 PHA03247
large tegument protein UL36; Provisional
 607-708 1.92e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  607 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLI-----PMPVGATSSFSAPPIPSRPGPQSVFANNDP--------------- 666
Cdd:PHA03247  2592 PPQSARPRAPVDDRGDPRGPAPPSPLPPDThapdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvsrprrarrlg 2671

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1720430183  667 ----FSAPPQIPSRPARIPPGIPPGVPSRRAPAAP---SRPTIIRPAEP 708
Cdd:PHA03247  2672 raaqASSPPQRPRRRAARPTVGSLTSLADPPPPPPtpePAPHALVSATP 2720
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 606-699 1.94e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 44.95  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 606 SPTPQRRPVSSVHPPGRPPAVRGPTPGPP-------LIPMPVGAtssfSAPPIPSRPGPQSVFANNDPfSAPPQIPSRPA 678
Cdd:PHA03321  443 PPPPRARPGSTPACARRARAQRARDAGPEyvdplgaLRRLPAGA----APPPEPAAAPSPATYYTRMG-GGPPRLPPRNR 517

                          90       100
                  ....*....|....*....|.
gi 1720430183 679 RippgippgVPSRRAPAAPSR 699
Cdd:PHA03321  518 A--------TETLRPDWGPPA 530
PHA03247 PHA03247
large tegument protein UL36; Provisional
 581-700 2.71e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  581 ISTSTVSTPVPPPvddtwlqntsghSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVgatssfSAPPIPSRPGPQSV 660
Cdd:PHA03247  2891 VSRSTESFALPPD------------QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR------PQPPLAPTTDPAGA 2952

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720430183  661 FANNDPFSAP---PQIPSRPARIPPGIPPGVPSRRAPAAPSRP 700
Cdd:PHA03247  2953 GEPSGAVPQPwlgALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
607-710 3.35e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.10  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 607 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSvfanndpfsaPPQIPSRPARIPPGIPP 686
Cdd:PRK12323  375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRS----------PAPEALAAARQASARGP 444

                          90       100
                  ....*....|....*....|....*
gi 1720430183 687 GVPSRRAPAAPSRPT-IIRPAEPSL 710
Cdd:PRK12323  445 GGAPAPAPAPAAAPAaAARPAAAGP 469
PHA03247 PHA03247
large tegument protein UL36; Provisional
 581-708 4.75e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  581 ISTSTVSTPVPP-PVDDTWLQNTSGHSPTPQRRPVSSVHPPGRP-PAVRGPTPGPPLIPMPVGATSsfsAP--PIPSRPG 656
Cdd:PHA03247  2791 LSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAqPTAPPPPPGPPPPSLPLGGSV---APggDVRRRPP 2867

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720430183  657 PQSVFANNdpfSAPPQIP---------SRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEP 708
Cdd:PHA03247  2868 SRSPAAKP---AAPARPPvrrlarpavSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 589-708 5.08e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 589 PVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRG---PTPGPPLIPMPVGATSSFSAPPIPSRPG--PQSVFAN 663
Cdd:PRK07764  658 AVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAApaqPAPAPAATPPAGQADDPAAQPPQAAQGAsaPSPAADD 737

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720430183 664 NDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEP 708
Cdd:PRK07764  738 PVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
PHA01929 PHA01929
putative scaffolding protein
 583-678 5.57e-04

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 42.73  E-value: 5.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 583 TSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGP----TPGPPLIPMPVGATSSFSAPPIPSRPgpq 658
Cdd:PHA01929    1 TTQNEQQLPPGLAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAPqqlaIPTQQPQPVPTSAMTPHVVQQAPAQP--- 77

                          90       100
                  ....*....|....*....|
gi 1720430183 659 svfannDPFSAPPQIPSRPA 678
Cdd:PHA01929   78 ------APAAPPAAGAALPE 91
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 577-708 6.39e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 577 IIGDISTSTVSTPVPPPVDDTWL-QNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPG--PPLIPMPVGATSSFSAPPIPS 653
Cdd:PRK07764  662 ASDGGDGWPAKAGGAAPAAPPPApAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAaqPPQAAQGASAPSPAADDPVPL 741

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720430183 654 RPGPQSVFANNDPFSAPPQIPSRPARIPPGIPPgVPSRRAPAAPSRPTIIRPAEP 708
Cdd:PRK07764  742 PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP-PPSPPSEEEEMAEDDAPSMDD 795
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 543-701 9.34e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 9.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  543 SSADQSSLMEESAEQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVddtwlqntSGHSPTPQRRPVSSVHPPGR 622
Cdd:PHA03307   234 ASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA--------SSSSSPRERSPSPSPSSPGS 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  623 PPAVRGPTPGPPLIPMP---VGATSSFSAPP--IPSRPGPQSVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAP 697
Cdd:PHA03307   306 GPAPSSPRASSSSSSSRessSSSTSSSSESSrgAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP 385


                   ....
gi 1720430183  698 SRPT 701
Cdd:PHA03307   386 TRRR 389
PHA03247 PHA03247
large tegument protein UL36; Provisional
 602-712 1.04e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  602 TSGHSPTPQRRPVSSV------HPPGRPPAVRGP--TPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPPQI 673
Cdd:PHA03247  2680 PQRPRRRAARPTVGSLtsladpPPPPPTPEPAPHalVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720430183  674 PSRPARIPPGIPPGVPSRRAPAAPSRPTII-----RPAEPSLLD 712
Cdd:PHA03247  2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVAslsesRESLPSPWD 2803
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 602-709 1.34e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 602 TSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANND--PFSAPPQIPSRPAR 679
Cdd:PRK07764  604 ASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDgwPAKAGGAAPAAPPP 683

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720430183 680 IPPGIPPGVPSRRAPAAP-SRPTIIRPAEPS 709
Cdd:PRK07764  684 APAPAAPAAPAGAAPAQPaPAPAATPPAGQA 714
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 571-709 1.39e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  571 LKEALNIIGDISTSTVSTPVPPPVDDtwLQNTSGHSPTPQRRPVSSVHPPGRPPAVR-----GPTPGPPLIP-----MPV 640
Cdd:PHA03307    10 LIEAAAEGGEFFPRPPATPGDAADDL--LSGSQGQLVSDSAELAAVTVVAGAAACDRfepptGPPPGPGTEApanesRST 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430183  641 GATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPSR--------PARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPS 709
Cdd:PHA03307    88 PTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPaspppspaPDLSEMLRPVGSPGPPPAASPPAAGASPAAVAS 164
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 591-701 1.45e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 41.53  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 591 PPPVddtwlqnTSGHSPTPQRRPVSSVHPPGRPPavrgpTPGPP------LIPMPVGATSSFSAPPIPsRPGPQSVFANN 664
Cdd:PHA03264  266 PPPA-------PSGGSPAPPGDDRPEAKPEPGPV-----EDGAPgretggEGEGPEPAGRDGAAGGEP-KPGPPRPAPDA 332

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720430183 665 DPFSAPPQIPSRParippgippgvPSRRAPAAPSRPT 701
Cdd:PHA03264  333 DRPEGWPSLEAIT-----------FPPPTPATPAVPR 358
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 589-677 1.53e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.02  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 589 PVPPPVDDtwlqntsGHSPTPQRRPVSSVHPPGR-------PPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVF 661
Cdd:pfam15240  56 PQPPASDD-------PPGPPPPGGPQQPPPQGGKqkpqgppPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQG 128

                          90
                  ....*....|....*.
gi 1720430183 662 ANNDPFSAPPQIPSRP 677
Cdd:pfam15240 129 GGPPPQGGNQQGPPPP 144
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
 551-657 1.62e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 41.75  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 551 MEESAEQAQRRDDMLRMYHALKEALNIIGDI-STSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPP---GRPPAV 626
Cdd:PRK14963  315 LDEQMERFARRSDALSLELALLHALLALGGApSEGVAAVAPPAPAPADLTQRLNRLEKEVRSLRSAPTAAAtaaGAPLPD 394

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720430183 627 RGPTPGPPliPMPVGATSSFSAPPIPSRPGP 657
Cdd:PRK14963  395 FDPRPRGP--PAPEPARSAEAPPLVAPAAAP 423
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 604-711 1.91e-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: 39.67  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 604 GHSPTPQRRPVSSVHPPGRPPAVRGP--TPGPPLIPMPVGATSSFSAPPI--------PSRPGPQSVFANNDPFSAP-PQ 672
Cdd:cd21975    20 GVRPDPEGAGLAAGLDVRATREVAKGpgPPGPAWKPDGADSPGLVTAAPHllaanvlaPLRGPSVEGSSLESGDADMgSD 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720430183 673 IPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLL 711
Cdd:cd21975   100 SDVAPASGAAASTSPESSSDAASSPSPLSLLHPGEAGLE 138
PHA03247 PHA03247
large tegument protein UL36; Provisional
 587-710 2.02e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  587 STPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDP 666
Cdd:PHA03247  2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD 2861

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720430183  667 FSAPPqiPSRPARIPpgippgvpsrraPAAPSRPTIIRPAEPSL 710
Cdd:PHA03247  2862 VRRRP--PSRSPAAK------------PAAPARPPVRRLARPAV 2891
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 603-698 2.22e-03

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


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 39.80  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 603 SGHSPtpqRRPVSSVHPPGRPPAVRGPTPGPPLIPMPV-GATSSFSAPPIPSRPG-PQSVFANNDPFSAPPQIPSRPAri 680
Cdd:cd21576   103 SGEAP---RASSGSSDPARGSSPTLGSEPAPASGEDAVsGPESSFGAPAIPSAPAaPGAPAVSGEVPGGAPGAGPAPA-- 177

                          90
                  ....*....|....*...
gi 1720430183 681 ppgipPGVPSRRAPAAPS 698
Cdd:cd21576   178 -----AGPAPRRRPVTPA 190
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 362-458 5.04e-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: 37.25  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 362 VIRRGWLTinnislMKGGS-----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGF-MSNKHVFAIFNTEQ 435
Cdd:cd13248     7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                          90       100
                  ....*....|....*....|...
gi 1720430183 436 RNVYkdlrqieLACDSQEDVDSW 458
Cdd:cd13248    81 RTYY-------FAADTAEEMEQW 96
PHA03378 PHA03378
EBNA-3B; Provisional
 591-707 6.75e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.05  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 591 PPPVDDTWLQ--------NTSGHSPT--PQRRPvSSVHPPGRPPAVRGPTPGPPlIPMPVGATSSFSAPPIPSRPGPQSV 660
Cdd:PHA03378  659 ITPYKPTWTQighipyqpSPTGANTMlpIQWAP-GTMQPPPRAPTPMRPPAAPP-GRAQRPAAATGRARPPAAAPGRARP 736

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720430183 661 FANNDPFSAPPQipSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAE 707
Cdd:PHA03378  737 PAAAPGRARPPA--AAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQ 781
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
602-708 7.11e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183 602 TSGHSPTPQRRPVSSVHPPG---RPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPS--- 675
Cdd:PRK12323  447 APAPAPAPAAAPAAAARPAAagpRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAesi 526

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720430183 676 -RPArIPPGIPPGVPSRRAPAAPSRPTIIRPAEP 708
Cdd:PRK12323  527 pDPA-TADPDDAFETLAPAPAAAPAPRAAAATEP 559
PHA03247 PHA03247
large tegument protein UL36; Provisional
 564-706 7.14e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430183  564 MLRMYHALKE-ALNIIGDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSS-VHPPGRPP-AVRGPTPGPPLIPMPV 640
Cdd:PHA03247  2533 MLTWIRGLEElASDDAGDPPPPLPPAAPPAAPDRS--VPPPRPAPRPSEPAVTSrARRPDAPPqSARPRAPVDDRGDPRG 2610

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720430183  641 GATSSfSAPPIPSRPGPqsvfanndPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPA 706
Cdd:PHA03247  2611 PAPPS-PLPPDTHAPDP--------PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRA 2667
 
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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