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Conserved domains on  [gi|568910358|ref|XP_006496665|]
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dynamin-3 isoform X2 [Mus musculus]

Protein Classification

dynamin( domain architecture ID 12185953)

dynamin is a GTPase that regulates endocytic vesicle formation; similar to human dynamin-1, a microtubule-associated force-producing protein involved in producing microtubule bundles

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 4.84e-161

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


:

Pssm-ID: 197491  Cd Length: 240  Bit Score: 468.97  E-value: 4.84e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358     6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358    86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358   166 RENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGK 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 3.51e-138

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: 411.91  E-value: 3.51e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  295 NFRNKLQGQLLSIEHEVEAFKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVMQELINTVKKCTKRLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 568910358  455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 526-635 2.16e-79

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: 251.47  E-value: 2.16e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 526 VIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQRNVYKD 605
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 568910358 606 YRFLELACDSQEDVDSWKASLLRAGVYPDK 635
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
655-745 2.80e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.09  E-value: 2.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  655 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 568910358  735 LKEALAIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
MISS super family cl25801
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 753-841 9.85e-07

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.


The actual alignment was detected with superfamily member pfam15822:

Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 50.76  E-value: 9.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  753 PAPPPVDDSWlqHSRRSPPPSPTTQ-RRLTISAPLPRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPNSS 825
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205

                          90       100
                  ....*....|....*....|....*
gi 568910358  826 DSFGAP---P------QVPSRPTRA 841
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPSGA 230
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 4.84e-161

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 468.97  E-value: 4.84e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358     6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358    86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358   166 RENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGK 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 29-294 1.31e-147

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: 435.91  E-value: 1.31e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRHE 100
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568910358 258 FFLSHPAYRH-IADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:cd08771  241 FFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 3.51e-138

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: 411.91  E-value: 3.51e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  295 NFRNKLQGQLLSIEHEVEAFKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVMQELINTVKKCTKRLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 568910358  455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 526-635 2.16e-79

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: 251.47  E-value: 2.16e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 526 VIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQRNVYKD 605
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 568910358 606 YRFLELACDSQEDVDSWKASLLRAGVYPDK 635
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 7.48e-70

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 228.27  E-value: 7.48e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358   34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRHEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirDMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 568910358  186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 2.80e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.09  E-value: 2.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  655 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 568910358  735 LKEALAIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 4.65e-29

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 111.17  E-value: 4.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358   654 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 568910358   734 ALKEALAIIGDI 745
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 526-629 6.70e-13

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: 65.65  E-value: 6.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358   526 VIRKGWLTVSNIGiMKGGSKGYWFVLTAESLSWYKDDEEKEK---KYMLPLDNLKVRDVEKGFMSS-KHVFALFNTEQRN 601
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEIKTSDRKT 79

                           90       100
                   ....*....|....*....|....*...
gi 568910358   602 VYkdyrfleLACDSQEDVDSWKASLLRA 629
Cdd:smart00233  80 LL-------LQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 526-629 2.65e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 63.74  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  526 VIRKGWLTVSNIGImKGGSKGYWFVLTAESLSWYKDD---EEKEKKYMLPLDNLKVRDVEKGFMSS-KHVFALFNTEQRN 601
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 568910358  602 VykdyRFLELACDSQEDVDSWKASLLRA 629
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 753-841 9.85e-07

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: 50.76  E-value: 9.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  753 PAPPPVDDSWlqHSRRSPPPSPTTQ-RRLTISAPLPRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPNSS 825
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205

                          90       100
                  ....*....|....*....|....*
gi 568910358  826 DSFGAP---P------QVPSRPTRA 841
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPSGA 230
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 753-834 2.71e-06

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 50.67  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 753 PAPPPVDDSWLQHSRRSPPPSPTTqrrltisaPLPRPTSGRGPAPAIPSPGPHSGAPPV---------PFRPGPLPPFPN 823
Cdd:NF040983  97 PPPPPPPPTPPPPPPPPPPPPPPS--------PPPPPPPSPPPSPPPPTTTPPTRTTPStttptpsmhPIQPTQLPSIPN 168

                         90
                 ....*....|.
gi 568910358 824 SSDSFGAPPQV 834
Cdd:NF040983 169 ATPTSGSATNV 179
PHA03247 PHA03247
large tegument protein UL36; Provisional
 754-869 5.86e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 5.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  754 APPPVDDSWLQHSRRSP-PPSPTTQRRLTISAPLPRPTSGRGP--------APAIPSPGPHSGAPPVPFRPGPLP----- 819
Cdd:PHA03247 2559 APPAAPDRSVPPPRPAPrPSEPAVTSRARRPDAPPQSARPRAPvddrgdprGPAPPSPLPPDTHAPDPPPPSPSPaanep 2638

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568910358  820 --------PFPNSSDSFGAPPQV-PSRPTRAPPSVPSRRPPPSPTRPTIIRPLESSLLD 869
Cdd:PHA03247 2639 dphppptvPPPERPRDDPAPGRVsRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTS 2697
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 762-838 1.38e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 45.38  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 762 WL-QHSRRSPPPS------PTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSFGA---- 830
Cdd:NF041121  10 WLaAQMGRAAAPPspegpaPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPgaal 89


                 ....*...
gi 568910358 831 PPQVPSRP 838
Cdd:NF041121  90 PVRVPAPP 97
HpaP TIGR02557
type III secretion protein HpaP; This family of genes is always found in type III secretion ...
 771-831 2.32e-03

type III secretion protein HpaP; This family of genes is always found in type III secretion operons, althought its function in the processes of secretion and virulence is unclear. Hpa stands for Hrp-associated gene, where Hrp stands for hypersensitivity response and virulence.


Pssm-ID: 274200  Cd Length: 201  Bit Score: 40.26  E-value: 2.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568910358  771 PPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPvpfRPGPLPPFPnsSDSFGAP 831
Cdd:TIGR02557  14 DPARPARRRTPLAQLRRRDALAYAPPPRPEPPPPCDEDRP---EPRADTRAS--DPPPEAP 69
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 751-839 3.77e-03

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 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 KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 39.64  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 751 STPAPPPVDDSWLQHSRRSPP--------PSPTTQRRLTISAPLPrptsgrgPAPAIPSPGPHSGAPPVPFRPGPLP--- 819
Cdd:cd21577   36 SSSSSSSSSSSSSPSSRASPPspysksspPSPPQQRPLSPPLSLP-------PPVAPPPLSPGSVPGGLPVISPVMVqpv 108

                         90       100
                 ....*....|....*....|
gi 568910358 820 PFPNSSdSFGAPPQVPSRPT 839
Cdd:cd21577  109 PVLYPP-HLHQPIMVSSSPP 127
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 4.84e-161

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 468.97  E-value: 4.84e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358     6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358    86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358   166 RENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGK 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 29-294 1.31e-147

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: 435.91  E-value: 1.31e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRHE 100
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 568910358 258 FFLSHPAYRH-IADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:cd08771  241 FFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 3.51e-138

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: 411.91  E-value: 3.51e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  295 NFRNKLQGQLLSIEHEVEAFKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVMQELINTVKKCTKRLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 568910358  455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 526-635 2.16e-79

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: 251.47  E-value: 2.16e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 526 VIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQRNVYKD 605
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 568910358 606 YRFLELACDSQEDVDSWKASLLRAGVYPDK 635
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 7.48e-70

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 228.27  E-value: 7.48e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358   34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRHEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirDMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 568910358  186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 2.80e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.09  E-value: 2.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  655 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 568910358  735 LKEALAIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 4.65e-29

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 111.17  E-value: 4.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358   654 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 568910358   734 ALKEALAIIGDI 745
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 526-629 6.70e-13

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: 65.65  E-value: 6.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358   526 VIRKGWLTVSNIGiMKGGSKGYWFVLTAESLSWYKDDEEKEK---KYMLPLDNLKVRDVEKGFMSS-KHVFALFNTEQRN 601
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEIKTSDRKT 79

                           90       100
                   ....*....|....*....|....*...
gi 568910358   602 VYkdyrfleLACDSQEDVDSWKASLLRA 629
Cdd:smart00233  80 LL-------LQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 526-629 2.65e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 63.74  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  526 VIRKGWLTVSNIGImKGGSKGYWFVLTAESLSWYKDD---EEKEKKYMLPLDNLKVRDVEKGFMSS-KHVFALFNTEQRN 601
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 568910358  602 VykdyRFLELACDSQEDVDSWKASLLRA 629
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 528-626 2.84e-11

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: 60.63  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 528 RKGWLTVSNIGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKY--MLPLDN-LKVRDVEKGfmSSKHVFALFNTEQRNVYk 604
Cdd:cd00821    1 KEGYLLKRGGGGLKSWKK-RWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                         90       100
                 ....*....|....*....|..
gi 568910358 605 dyrfleLACDSQEDVDSWKASL 626
Cdd:cd00821   77 ------LQADSEEERQEWLKAL 92
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 526-629 3.39e-09

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: 55.40  E-value: 3.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 526 VIRKGWLTvsnigiMKGGS----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKgfMSSKHVFALFNTEQRN 601
Cdd:cd01252    3 PDREGWLL------KLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568910358 602 VYKD----------------YRfleLACDSQEDVDSWKASLLRA 629
Cdd:cd01252   75 VIKAcktdsdgkvvegnhtvYR---ISAASEEERDEWIKSIKAS 115
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 753-841 9.85e-07

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: 50.76  E-value: 9.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  753 PAPPPVDDSWlqHSRRSPPPSPTTQ-RRLTISAPLPRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPNSS 825
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205

                          90       100
                  ....*....|....*....|....*
gi 568910358  826 DSFGAP---P------QVPSRPTRA 841
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPSGA 230
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
 548-629 1.07e-06

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. 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: 270110  Cd Length: 106  Bit Score: 48.01  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 548 WFVLTAESLSWYKDDEEKEKKYMLPLDNL----KVRDVEKgfmssKHVFALFNTEqrnvyKDYRFlelACDSQEDVDSWk 623
Cdd:cd13298   26 WVVLRPCQLSYYKDEKEYKLRRVINLSELlavaPLKDKKR-----KNVFGIYTPS-----KNLHF---RATSEKDANEW- 91


                 ....*.
gi 568910358 624 ASLLRA 629
Cdd:cd13298   92 VEALRE 97
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 526-629 1.40e-06

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: 47.65  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 526 VIRKGWLTvsnigimKGGSKGY------WFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGF-MSSKHVFALFNTE 598
Cdd:cd13248    7 VVMSGWLH-------KQGGSGLknwrkrWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHAN 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568910358 599 QRNVYkdyrfleLACDSQEDVDSWKASLLRA 629
Cdd:cd13248   80 MRTYY-------FAADTAEEMEQWMNAMSLA 103
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 753-834 2.71e-06

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 50.67  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 753 PAPPPVDDSWLQHSRRSPPPSPTTqrrltisaPLPRPTSGRGPAPAIPSPGPHSGAPPV---------PFRPGPLPPFPN 823
Cdd:NF040983  97 PPPPPPPPTPPPPPPPPPPPPPPS--------PPPPPPPSPPPSPPPPTTTPPTRTTPStttptpsmhPIQPTQLPSIPN 168

                         90
                 ....*....|.
gi 568910358 824 SSDSFGAPPQV 834
Cdd:NF040983 169 ATPTSGSATNV 179
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 715-838 4.74e-06

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 49.54  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  715 MEESAEQAQRRDemlRMYQALkeALAIIGDINTATVSTPA-----PPPVddswlqhsrrSPPPSPTTqrrltiSAPLPRP 789
Cdd:pfam07174   1 MDQVDPNSTRRK---GLWATL--AIAAVAGASAVAVALPAvahadPEPA----------PPPPSTAT------APPAPPP 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568910358  790 TSgrgPAPAIPSPGPHSGAPPVPfRPGPLPPFPNSSDSFGAPPQVPSRP 838
Cdd:pfam07174  60 PP---PAPAAPAPPPPPAAPNAP-NAPPPPADPNAPPPPPADPNAPPPP 104
PHA03247 PHA03247
large tegument protein UL36; Provisional
 754-869 5.86e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 5.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  754 APPPVDDSWLQHSRRSP-PPSPTTQRRLTISAPLPRPTSGRGP--------APAIPSPGPHSGAPPVPFRPGPLP----- 819
Cdd:PHA03247 2559 APPAAPDRSVPPPRPAPrPSEPAVTSRARRPDAPPQSARPRAPvddrgdprGPAPPSPLPPDTHAPDPPPPSPSPaanep 2638

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568910358  820 --------PFPNSSDSFGAPPQV-PSRPTRAPPSVPSRRPPPSPTRPTIIRPLESSLLD 869
Cdd:PHA03247 2639 dphppptvPPPERPRDDPAPGRVsRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTS 2697
PHA03247 PHA03247
large tegument protein UL36; Provisional
 754-841 9.74e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 9.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  754 APPPVDDswLQHSRRSPPPSPTtqrrltiSAPLPRPTSGRGPAPAIPSPGPHSgAPPVPFRPGPlPPFPNSSDSFGAPPQ 833
Cdd:PHA03247 2688 ARPTVGS--LTSLADPPPPPPT-------PEPAPHALVSATPLPPGPAAARQA-SPALPAAPAP-PAVPAGPATPGGPAR 2756


                  ....*...
gi 568910358  834 VPSRPTRA 841
Cdd:PHA03247 2757 PARPPTTA 2764
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-841 1.33e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  751 STPAPPPVDDSWLQHSRR-SPPPSPTTQRrltisAPLPRPTSGRGPAPaiPSPGPHSGAPPVPFRPGPLP---------- 819
Cdd:PHA03247 2571 PRPAPRPSEPAVTSRARRpDAPPQSARPR-----APVDDRGDPRGPAP--PSPLPPDTHAPDPPPPSPSPaanepdphpp 2643

                          90       100
                  ....*....|....*....|....*
gi 568910358  820 ---PFPNSSDSFGAPPQVpSRPTRA 841
Cdd:PHA03247 2644 ptvPPPERPRDDPAPGRV-SRPRRA 2667
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
 526-628 1.48e-05

Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 or ArhGap22) are involved in cell polarity, cell morphology and cytoskeletal organization. They activate a GTPase belonging to the RAS superfamily of small GTP-binding proteins. The encoded protein is insulin-responsive, is dependent on the kinase Akt, and requires the Akt-dependent 14-3-3 binding protein which binds sequentially to two serine residues resulting in regulation of cell motility. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 241529  Cd Length: 116  Bit Score: 44.94  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 526 VIRKGWLTVSNiGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMS-SKHVFALF---NTEQRN 601
Cdd:cd13378    3 VLKAGWLKKQR-SIMKNWQQ-RWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNELPPNPEEpGKHLFEILpggAGDREK 80

                         90       100
                 ....*....|....*....|....*..
gi 568910358 602 VYKDYRFLELACDSQEDVDSWKASLLR 628
Cdd:cd13378   81 VPMNHEAFLLMANSQSDMEDWVKAIRR 107
DUF4813 pfam16072
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ...
 745-837 1.91e-05

Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.


Pssm-ID: 435117 [Multi-domain]  Cd Length: 288  Bit Score: 47.44  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  745 INT--ATVSTPAPP--PVDDSWLQHSRRSPPPSP------TTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPvpfr 814
Cdd:pfam16072 161 INAggQQPAAPAAPayPVAPAAYPAQAPAAAPAPapgapqTPLAPLNPVAAAPAAAAGAAAAPVVAAAAPAAAAPP---- 236

                          90       100
                  ....*....|....*....|....*....
gi 568910358  815 pgplPPFPNSSDSFGAPPQ------VPSR 837
Cdd:pfam16072 237 ----PPAPAAPPADAAPPApggiicVPVR 261
PHA03247 PHA03247
large tegument protein UL36; Provisional
 752-841 2.35e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  752 TPaPPPVDD--SWLQHSRRSPPPSPTTQRRLTISAPLPRPTSG------RGPAPA-IPSPGPHSGAPPVPFRP-GPLP-P 820
Cdd:PHA03247  360 TP-PSSLEDlsAGRHHPKRASLPTRKRRSARHAATPFARGPGGddqtrpAAPVPAsVPTPAPTPVPASAPPPPaTPLPsA 438

                          90       100
                  ....*....|....*....|.
gi 568910358  821 FPNSSDSfGAPPQVPSRPTRA 841
Cdd:PHA03247  439 EPGSDDG-PAPPPERQPPAPA 458
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 707-841 2.41e-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: 48.22  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  707 SSEDQNTLMEESAEQAQRRDEMLRMyQALKEAL--AIIGDINTATVSTPAPPPVDDSwlQHSRRSPPPSPTTQRRLTISA 784
Cdd:pfam03154 150 SPQDNESDSDSSAQQQILQTQPPVL-QAQSGAAspPSPPPPGTTQAATAGPTPSAPS--VPPQGSPATSQPPNQTQSTAA 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  785 P--------------LPRPTSGRGPAP-----------AIPSPGPHSGAPPVPFR--------PGPLPPFPNSSDSFGAP 831
Cdd:pfam03154 227 PhtliqqtptlhpqrLPSPHPPLQPMTqppppsqvspqPLPQPSLHGQMPPMPHSlqtgpshmQHPVPPQPFPLTPQSSQ 306

                         170
                  ....*....|
gi 568910358  832 PQVPSRPTRA 841
Cdd:pfam03154 307 SQVPPGPSPA 316
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 745-840 2.81e-05

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 48.03  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 745 INTATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAI-------PSPGPHSGAP-------P 810
Cdd:PHA03321 404 LATELFRTGVPSEHYEASLRLLSSRQPPGAPAPRRDNDPPPPPRARPGSTPACARraraqraRDAGPEYVDPlgalrrlP 483

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568910358 811 VPFRPGPLPPFPNSSDSF-----GAPPQVPSRPTR 840
Cdd:PHA03321 484 AGAAPPPEPAAAPSPATYytrmgGGPPRLPPRNRA 518
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-839 2.82e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  747 TATVSTPAPPPVDDSWLQHS--------------RRSPPPSPTTQ---------RRL--------TISAPLPRPTSGRGP 795
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSlplggsvapggdvrRRPPSRSPAAKpaaparppvRRLarpavsrsTESFALPPDQPERPP 2909

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568910358  796 APAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSFGAP---PQVPSRPT 839
Cdd:PHA03247 2910 QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPttdPAGAGEPS 2956
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-838 3.37e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  748 ATVSTPAPPPVDDswlqHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSP---------------------GPHS 806
Cdd:PHA03247 2794 SRESLPSPWDPAD----PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGppppslplggsvapggdvrrrPPSR 2869

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568910358  807 GAPPVPFRPG-------PLPPFPNSSDSFGAPPQVPSRP 838
Cdd:PHA03247 2870 SPAAKPAAPArppvrrlARPAVSRSTESFALPPDQPERP 2908
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 748-851 6.55e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  748 ATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRP------TSGRGPAPAIPSPGPHSGAPPvpfrpGPLPPF 821
Cdd:PHA03307  119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAavasdaASSRQAALPLSSPEETARAPS-----SPPAEP 193

                          90       100       110
                  ....*....|....*....|....*....|
gi 568910358  822 PNSSDSFGAPPqvPSRPTRAPPSVPSRRPP 851
Cdd:PHA03307  194 PPSTPPAAASP--RPPRRSSPISASASSPA 221
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-841 8.12e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 8.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  748 ATVSTPAPPPVDDSWLQHSRRSPPPSPTTqrrlTISAPLPRPTSGR--GPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSS 825
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPT----TAGPPAPAPPAAPaaGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809

                          90
                  ....*....|....*.
gi 568910358  826 DSFGAPPQVPSRPTRA 841
Cdd:PHA03247 2810 AVLAPAAALPPAASPA 2825
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-840 1.06e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  747 TATVSTPAPPPVDDSWLQhsRRSPPPSPTTQRRLTISAPLPR-----PTSGRGPAPAIP-SPGPHSGAPP----VPFRPG 816
Cdd:PHA03247 2763 TAGPPAPAPPAAPAAGPP--RRLTRPAVASLSESRESLPSPWdpadpPAAVLAPAAALPpAASPAGPLPPptsaQPTAPP 2840

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568910358  817 PLPPFPNSSDSFG----------------APPQVPSRPTR 840
Cdd:PHA03247 2841 PPPGPPPPSLPLGgsvapggdvrrrppsrSPAAKPAAPAR 2880
PH2_PH_fungal cd13299
Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal ...
 526-626 1.24e-04

Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the second PH repeat. 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: 270111  Cd Length: 102  Bit Score: 41.84  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 526 VIRKGWLTVsnigiMKGGS----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNL-KVRDVEKGFMSSKHVFALFNTEQR 600
Cdd:cd13299    6 VIEQGYLQV-----LKKKGvnqwKKYWLVLRNRSLSFYKDQSEYSPVKIIPIDDIiDVVELDPLSKSKKWCLQIITPEKR 80

                         90       100
                 ....*....|....*....|....*.
gi 568910358 601 nvykdYRFlelACDSQEDVDSWKASL 626
Cdd:cd13299   81 -----IRF---CADDEESLIKWLGAL 98
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 762-838 1.38e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 45.38  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 762 WL-QHSRRSPPPS------PTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSFGA---- 830
Cdd:NF041121  10 WLaAQMGRAAAPPspegpaPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPgaal 89


                 ....*...
gi 568910358 831 PPQVPSRP 838
Cdd:NF041121  90 PVRVPAPP 97
PRK04654 PRK04654
sec-independent translocase; Provisional
 703-841 1.46e-04

sec-independent translocase; Provisional


Pssm-ID: 135173 [Multi-domain]  Cd Length: 214  Bit Score: 44.03  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 703 AQLYSSEDQNTLMEESAEQAQR--RDEMLRmyqalkealaiigDINTATVSTPAPPPVDdswLQHSRRSPPPSPTTQRRL 780
Cdd:PRK04654  68 ASLREAEDQLRNTQQQVEQGARalHDDVSR-------------DIDIRTSATPVATPLE---LAHADLSASAQVDAAAGA 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568910358 781 TISAPlPRPTSGRGPAPAIP-----SPGPHSGAPPVPFrpGPLPPFPNSSDSFGAP-PQVPSRPTRA 841
Cdd:PRK04654 132 EPGAG-QAHTPVPAPAPVIAqaqpiAPAPHQTLVPAPH--DTIVPAPHAAHLPSAPaTPVSVAPVDA 195
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 726-839 2.16e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 44.80  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 726 DEMLRM--YQALKEALAII-GDINTATVSTPAPPpvddswlqhsrRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSP 802
Cdd:PRK14950 338 DFQLRTtsYGQLPLELAVIeALLVPVPAPQPAKP-----------TAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRET 406

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568910358 803 GPHSGAPPVPFRPGPLPPFPNSSDSFGAPPQVPSRPT 839
Cdd:PRK14950 407 ATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEKPK 443
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
 526-626 2.20e-04

Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the third MyoX PH repeat. PLEKHH3/Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) member 3 is also part of this CD and like MyoX contains a FERM domain, a MyTH4 domain, and a single PH domain. Not much is known about the function of PLEKHH3. 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: 270109  Cd Length: 126  Bit Score: 42.04  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 526 VIRKGWLT--VSNIGIMKGGS-KGYWFVLTAESLSWYKD-DEEKEKKYMLPLDNL--KVRDVEKgfMSSKHVFALFnteq 599
Cdd:cd13297   13 VIERGWLYkeGGKGGARGNLTkKKRWFVLTGNSLDYYKSsEKNSLKLGTLVLNSLcsVVPPDEK--MAKETGYWTF---- 86

                         90       100
                 ....*....|....*....|....*..
gi 568910358 600 rNVYKDYRFLELACDSQEDVDSWKASL 626
Cdd:cd13297   87 -TVHGRKHSFRLYTKLQEEAMRWVNAI 112
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 751-841 2.26e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  751 STPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAI---PSPGPHSGAPPVPFRPGPLPPFPNSSDS 827
Cdd:PHA03307  295 SPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPgpsPSRSPSPSRPPPPADPSSPRKRPRPSRA 374

                          90
                  ....*....|....
gi 568910358  828 FGAPPQVPSRPTRA 841
Cdd:PHA03307  375 PSSPAASAGRPTRR 388
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 747-838 3.11e-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: 43.44  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  747 TATVSTPAPPPVDDSWLQHSRRSPPPSPTTqrrltISAPLPrPTSGRGPAPAIPSP-GPHSGAPPVPFRPGPLPPFPNSS 825
Cdd:pfam15822  15 TSAVSNPKPGQPPQGWPGSNPWNNPSAPPA-----VPSGLP-PSTAPSTVPFGPAPtGMYPSIPLTGPSPGPPAPFPPSG 88

                          90
                  ....*....|...
gi 568910358  826 DSfgAPPqvPSRP 838
Cdd:pfam15822  89 PS--CPP--PGGP 97
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 752-838 3.36e-04

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 43.84  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 752 TPAPPPVDDSwlqhsRRSPPPSPTTqrrltiSAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPF--PNSSDSFG 829
Cdd:PHA03264 274 SPAPPGDDRP-----EAKPEPGPVE------DGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDAdrPEGWPSLE 342

                         90
                 ....*....|..
gi 568910358 830 A---PPQVPSRP 838
Cdd:PHA03264 343 AitfPPPTPATP 354
TYA pfam01021
Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a ...
 745-836 3.71e-04

Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a fusion protein of TYA and TYB. The TYA protein is analogous to the gag protein of retroviruses. TYA a is cleaved to form 46kd protein which can form mature virion like particles. This entry corresponds to the capsid protein from Ty1 and Ty2 transposons.


Pssm-ID: 425992  Cd Length: 384  Bit Score: 43.79  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  745 INTATVSTPAPPPVDDSwlqHSRRSPPPSpttqrrltiSAPLPR--PTSGRG---PAPAIPSPGPHSGAP---------- 809
Cdd:pfam01021  34 ANSQQTTTPGSSAVPEN---HHHASPQPA---------SVPPPQngPYSQQCmmtPNQANPSGWPFYGHPsmmpytpyqm 101

                          90       100
                  ....*....|....*....|....*...
gi 568910358  810 -PVPFRPGPLPPFPNSSDSFGAPPQVPS 836
Cdd:pfam01021 102 sPMYFPPGPQSQFPQYPSSVGTPLSTPS 129
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 753-835 4.23e-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: 43.99  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  753 PAPPPVDDSWLQHSRRSPPPSPTTQrrltisapLPRPTSGRGPAPAiPSPGPHSGAPPvpfRPGPLPPFPNSSDSFGAPP 832
Cdd:pfam03154 292 PVPPQPFPLTPQSSQSQVPPGPSPA--------APGQSQQRIHTPP-SQSQLQSQQPP---REQPLPPAPLSMPHIKPPP 359


                  ...
gi 568910358  833 QVP 835
Cdd:pfam03154 360 TTP 362
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
 548-628 4.26e-04

Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of cytoplasmic protein tyrosine kinases that includes BMX, IL2-inducible T-cell kinase (Itk) and Tec. Btk plays a role in the maturation of B cells. Tec proteins general have an N-terminal PH domain, followed by a Tek homology (TH) domain, a SH3 domain, a SH2 domain and a kinase domain. The Btk PH domain binds phosphatidylinositol 3,4,5-trisphosphate and responds to signalling via phosphatidylinositol 3-kinase. The PH domain is also involved in membrane anchoring which is confirmed by the discovery of a mutation of a critical arginine residue in the BTK PH domain. This results in severe human immunodeficiency known as X-linked agammaglobulinemia (XLA) in humans and a related disorder is mice.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: 269944 [Multi-domain]  Cd Length: 140  Bit Score: 41.44  E-value: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 548 WFVLTAESLSWYKDDEEKEKKY--MLPLDnlKVRDVEK----GFMSSKHVFALfnteqrnVYKDYrFLELACDSQEDVDS 621
Cdd:cd01238   24 WFVLTKSSLSYYEGDGEKRGKEkgSIDLS--KVRCVEEvkdeAFFERKYPFQV-------VYDDY-TLYVFAPSEEDRDE 93


                 ....*..
gi 568910358 622 WKASLLR 628
Cdd:cd01238   94 WIAALRK 100
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
 519-626 5.22e-04

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275402  Cd Length: 116  Bit Score: 40.68  E-value: 5.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 519 LPPSRQIVIRKGWLTvsnigiMKGGSKG----YWFVLTAESLSWYKDDEEkekKYmLPLDNLKVRDV-----EKGFMSSK 589
Cdd:cd13215   14 LPKRSGAVIKSGYLS------KRSKRTLrytrYWFVLKGDTLSWYNSSTD---LY-FPAGTIDLRYAtsielSKSNGEAT 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568910358 590 HVFALFNTEQRnvykdYRFLelaCDSQEDVDSWKASL 626
Cdd:cd13215   84 TSFKIVTNSRT-----YKFK---ADSETSADEWVKAL 112
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 743-841 6.05e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.75  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  743 GDINTATVSTPAPPPVDDSwlQHSRRSPPPSPTTqrrlTISAPLPRPTSgrgPAPAIPSPGPHSGAP------------- 809
Cdd:pfam05109 480 GTTSGASPVTPSPSPRDNG--TESKAPDMTSPTS----AVTTPTPNATS---PTPAVTTPTPNATSPtlgktsptsavtt 550

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568910358  810 PVPFRPGPLP----PFPNSSdsfgAPPQVPSRPTRA 841
Cdd:pfam05109 551 PTPNATSPTPavttPTPNAT----IPTLGKTSPTSA 582
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
 526-574 8.63e-04

Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called Differentially expressed in FDCP 6/DEF-6 or IRF4-binding protein) functions in cellular signal transduction pathways (in conjunction with Rac), regulates cell motility through actin rearrangement, and contributes to the transformation and invasion activity of mouse embryo fibroblasts. Metazoan SWAP-70 is found in B lymphocytes, mast cells, and in a variety of organs. Metazoan SWAP-70 contains an N-terminal EF-hand motif, a centrally located PH domain, and a C-terminal coiled-coil domain. The PH domain of Metazoan SWAP-70 contains a phosphoinositide-binding site and a nuclear localization signal (NLS), which localize SWAP-70 to the plasma membrane and nucleus, respectively. The NLS is a sequence of four Lys residues located at the N-terminus of the C-terminal a-helix; this is a unique characteristic of the Metazoan SWAP-70 PH domain. The SWAP-70 PH domain binds PtdIns(3,4,5)P3 and PtdIns(4,5)P2 embedded in lipid bilayer vesicles. There are additional plant SWAP70 proteins, but these are not included in this hierarchy. Rice SWAP70 (OsSWAP70) exhibits GEF activity toward the its Rho GTPase, OsRac1, and regulates chitin-induced production of reactive oxygen species and defense gene expression in rice. Arabidopsis SWAP70 (AtSWAP70) plays a role in both PAMP- and effector-triggered immunity. Plant SWAP70 contains both DH and PH domains, but their arrangement is the reverse of that in typical DH-PH-type Rho GEFs, wherein the DH domain is flanked by a C-terminal 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: 270092  Cd Length: 110  Bit Score: 39.59  E-value: 8.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568910358 526 VIRKGWLtvsnigiMKGGSK-----GYWFVLTAESLSWYKDDEEKEKKYMLPLD 574
Cdd:cd13273    8 VIKKGYL-------WKKGHLlptwtERWFVLKPNSLSYYKSEDLKEKKGEIALD 54
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 748-847 1.23e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 41.77  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 748 ATVSTPAPP-PVD---DSWLQHSRRSPppSPTTQRRL-TISAPLPRPT--SGRGPAPAIPSPGPH--SGAPPVPFR---- 814
Cdd:PHA02682  32 ATIPAPAAPcPPDadvDPLDKYSVKEA--GRYYQSRLkANSACMQRPSgqSPLAPSPACAAPAPAcpACAPAAPAPavtc 109

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568910358 815 PGPLPPFPNSSDSFGAPPQV---PSRPTRAPPSVPS 847
Cdd:PHA02682 110 PAPAPACPPATAPTCPPPAVcpaPARPAPACPPSTR 145
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-838 1.41e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  747 TATVSTPAPPPVDDSWLQHSRRSPPPSPTT--QRRLTISAPLP-RPTSGRGPAPAIPSPGPHSGAPPVPFRPG---PLPP 820
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAPAPPAAPAAgpPRRLTRPAVASlSESRESLPSPWDPADPPAAVLAPAAALPPaasPAGP 2827

                          90
                  ....*....|....*...
gi 568910358  821 FPNSSDSFGAPPQVPSRP 838
Cdd:PHA03247 2828 LPPPTSAQPTAPPPPPGP 2845
PH_CNK_mammalian-like cd01260
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
 530-629 1.69e-03

Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and, with the exception of CNK3, a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from mammals, chickens, amphibians, fish, and crustacea. 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: 269962  Cd Length: 114  Bit Score: 38.93  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 530 GWLTV--SNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKV---RDVEKgfmssKHVFALfnteQRNVYK 604
Cdd:cd01260   17 GWLWKkkEAKSFFGQKWKKYWFVLKGSSLYWYSNQQDEKAEGFINLPDFKIeraSECKK-----KYAFKA----CHPKIK 87

                         90       100
                 ....*....|....*....|....*
gi 568910358 605 DYRFlelACDSQEDVDSWKASLLRA 629
Cdd:cd01260   88 TFYF---AAENLDDMNKWLSKLNMA 109
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
 526-629 1.81e-03

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the first PH domain repeat. 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: 270113  Cd Length: 108  Bit Score: 38.89  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 526 VIRKGWLtvsnigiMKGGS-----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQr 600
Cdd:cd13301    3 IIKEGYL-------VKKGHvvnnwKARWFVLKEDGLEYYKKKTDSSPKGMIPLKGCTITSPCLEYGKRPLVFKLTTAKG- 74

                         90       100
                 ....*....|....*....|....*....
gi 568910358 601 nvyKDYrFLElACdSQEDVDSWKASLLRA 629
Cdd:cd13301   75 ---QEH-FFQ-AC-SREERDAWAKDITKA 97
PHA03378 PHA03378
EBNA-3B; Provisional
 748-839 1.82e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.98  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 748 ATVSTPAPPPvddswlqhSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPfPNSSDS 827
Cdd:PHA03378 692 GTMQPPPRAP--------TPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARP-PAAAPG 762

                         90
                 ....*....|...
gi 568910358 828 FGAPPQ-VPSRPT 839
Cdd:PHA03378 763 RARPPAaAPGAPT 775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 750-844 1.98e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  750 VSTPAPPPVDDSWLQ-HSRRSPPPSPTTQRRLTISAPLPRPTSgrgPAPAIPSPG-PHSGAPPVP---FRPGPLPPFPNS 824
Cdd:PHA03247 2886 LARPAVSRSTESFALpPDQPERPPQPQAPPPPQPQPQPPPPPQ---PQPPPPPPPrPQPPLAPTTdpaGAGEPSGAVPQP 2962

                          90       100
                  ....*....|....*....|
gi 568910358  825 SDSFGAPPQVPSRPTRAPPS 844
Cdd:PHA03247 2963 WLGALVPGRVAVPRFRVPQP 2982
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 746-838 2.19e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 746 NTATVSTPAPPPVDDSwlqHSRRSPPPSPTTQRRLTiSAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSS 825
Cdd:PRK14951 382 ARPEAAAPAAAPVAQA---AAAPAPAAAPAAAASAP-AAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAP 457

                         90
                 ....*....|...
gi 568910358 826 DSFGAPPQVPSRP 838
Cdd:PRK14951 458 ETVAIPVRVAPEP 470
HpaP TIGR02557
type III secretion protein HpaP; This family of genes is always found in type III secretion ...
 771-831 2.32e-03

type III secretion protein HpaP; This family of genes is always found in type III secretion operons, althought its function in the processes of secretion and virulence is unclear. Hpa stands for Hrp-associated gene, where Hrp stands for hypersensitivity response and virulence.


Pssm-ID: 274200  Cd Length: 201  Bit Score: 40.26  E-value: 2.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568910358  771 PPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPvpfRPGPLPPFPnsSDSFGAP 831
Cdd:TIGR02557  14 DPARPARRRTPLAQLRRRDALAYAPPPRPEPPPPCDEDRP---EPRADTRAS--DPPPEAP 69
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
 526-629 2.40e-03

Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP2 contains two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. The members here are most sequence similar to TAPP2 proteins, but may not be actual TAPP2 proteins. 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: 270075  Cd Length: 110  Bit Score: 38.55  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 526 VIRKGWLtvsnigiMKGGS-----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLK-VRDVEKGfmSSKHVFALFnTEQ 599
Cdd:cd13255    6 VLKAGYL-------EKKGErrktwKKRWFVLRPTKLAYYKNDKEYRLLRLIDLTDIHtCTEVQLK--KHDNTFGIV-TPA 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 568910358 600 RNVYkdyrfleLACDSQEDVDSWKASLLRA 629
Cdd:cd13255   76 RTFY-------VQADSKAEMESWISAINLA 98
PH_Boi cd13316
Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally ...
 529-629 2.73e-03

Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally redundant and important for cell growth with Boi mutants displaying defects in bud formation and in the maintenance of cell polarity.They appear to be linked to Rho-type GTPase, Cdc42 and Rho3. Boi1 and Boi2 display two-hybrid interactions with the GTP-bound ("active") form of Cdc42, while Rho3 can suppress of the lethality caused by deletion of Boi1 and Boi2. These findings suggest that Boi1 and Boi2 are targets of Cdc42 that promote cell growth in a manner that is regulated by Rho3. Boi proteins contain a N-terminal SH3 domain, followed by a SAM (sterile alpha motif) domain, a proline-rich region, which mediates binding to the second SH3 domain of Bem1, and C-terminal PH domain. The PH domain is essential for its function in cell growth and is important for localization to the bud, while the SH3 domain is needed for localization to the neck. 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: 270126  Cd Length: 97  Bit Score: 38.12  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 529 KGWLTvsnigiMKGGSKGYW----FVLTAESLSWYKDDEEKEKKYMLPLDNLKV-RDVEKGFMSSKHVFALFNTEQRNVY 603
Cdd:cd13316    3 SGWMK------KRGERYGTWktryFVLKGTRLYYLKSENDDKEKGLIDLTGHRVvPDDSNSPFRGSYGFKLVPPAVPKVH 76

                         90       100
                 ....*....|....*....|....*.
gi 568910358 604 kdYrfleLACDSQEDVDSWKASLLRA 629
Cdd:cd13316   77 --Y----FAVDEKEELREWMKALMKA 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
 774-841 2.80e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  774 PTTQRRLTISAPL------PRPTSGRGPApAIPSPGPHSGAPPVPFRPGPLPPFPNSSDS--------FGAPPQVPSRPT 839
Cdd:PHA03247  236 PFVERRVVISHPLrgdiaaPAPPPVVGEG-ADRAPETARGATGPPPPPEAAAPNGAAAPPdgvwgaalAGAPLALPAPPD 314


                  ..
gi 568910358  840 RA 841
Cdd:PHA03247  315 PP 316
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
 763-837 3.04e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 41.27  E-value: 3.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568910358 763 LQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSF-GAPPQVPSR 837
Cdd:PRK14965 374 LEALERGAPAPPSAAWGAPTPAAPAAPPPAAAPPVPPAAPARPAAARPAPAPAPPAAAAPPARSADpAAAASAGDR 449
PHA03378 PHA03378
EBNA-3B; Provisional
 707-840 3.19e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.21  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 707 SSEDQNTLMEESAEQAQRRDEMLRMYQALKEALAIIGDINTATVSTPAPPP------VDDSWLQHSRRSPPPSPT--TQR 778
Cdd:PHA03378 605 TPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPHQPPqveitpYKPTWTQIGHIPYQPSPTgaNTM 684

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568910358 779 RLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPfPNSSDSFGAPPQVPSRPTR 840
Cdd:PHA03378 685 LPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARP-PAAAPGRARPPAAAPGRAR 745
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
 524-629 3.38e-03

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 270083  Cd Length: 114  Bit Score: 38.13  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 524 QIVIRKGWLTVSNiGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVE-KGFMSSKHVFALF----NTE 598
Cdd:cd13263    1 ERPIKSGWLKKQG-SIVKNWQQ-RWFVLRGDQLYYYKDEDDTKPQGTIPLPGNKVKEVPfNPEEPGKFLFEIIpgggGDR 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568910358 599 QRNVYKDYRfleLACDSQEDVDSWKASLLRA 629
Cdd:cd13263   79 MTSNHDSYL---LMANSQAEMEEWVKVIRRV 106
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
748-837 3.61e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 748 ATVSTPAPPPVDDSwlqhSRRSPPPSPTTQRRltiSAPLPRPTSGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPNSSDS 827
Cdd:PRK12323 410 PAAAAAARAVAAAP----ARRSPAPEALAAAR---QASARGPGGAPAPAPA-PAAAPAAAARPAAAGPRPVAAAAAAAPA 481

                         90
                 ....*....|
gi 568910358 828 FGAPPQVPSR 837
Cdd:PRK12323 482 RAAPAAAPAP 491
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 748-835 3.65e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 748 ATVSTPAPPPvddswlqhsRRSPPPSPTTqrrltiSAPLPRPTSGRGPAPAI---PSPGPHSGAPPVPFRPGPLPPFPNS 824
Cdd:PRK07764 391 AGAPAAAAPS---------AAAAAPAAAP------APAAAAPAAAAAPAPAAapqPAPAPAPAPAPPSPAGNAPAGGAPS 455

                         90
                 ....*....|.
gi 568910358 825 SDSFGAPPQVP 835
Cdd:PRK07764 456 PPPAAAPSAQP 466
PHA03247 PHA03247
large tegument protein UL36; Provisional
 753-841 3.73e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  753 PAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPgphsgappvpfRPGPLPPFPNSSDSFGAPP 832
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP-----------WLGALVPGRVAVPRFRVPQ 2981


                  ....*....
gi 568910358  833 QVPSRPTRA 841
Cdd:PHA03247 2982 PAPSREAPA 2990
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 751-839 3.77e-03

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 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 KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 39.64  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 751 STPAPPPVDDSWLQHSRRSPP--------PSPTTQRRLTISAPLPrptsgrgPAPAIPSPGPHSGAPPVPFRPGPLP--- 819
Cdd:cd21577   36 SSSSSSSSSSSSSPSSRASPPspysksspPSPPQQRPLSPPLSLP-------PPVAPPPLSPGSVPGGLPVISPVMVqpv 108

                         90       100
                 ....*....|....*....|
gi 568910358 820 PFPNSSdSFGAPPQVPSRPT 839
Cdd:cd21577  109 PVLYPP-HLHQPIMVSSSPP 127
PH2_TAPP1_2 cd13271
Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal ...
 520-622 3.80e-03

Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal repeat; The binding of TAPP1 (also called PLEKHA1/pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 1) and TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP1 and TAPP2 contain two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. 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: 270090  Cd Length: 114  Bit Score: 38.10  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 520 PPSRQIVIRKGWlTVSNIGIMKGGSKGYwFVLTAESLSWYKDDEEKEKKYMLPL-DNLKVRDVE-KGFMSSKHVFALFnT 597
Cdd:cd13271    2 QRAGRNVIKSGY-CVKQGAVRKNWKRRF-FILDDNTISYYKSETDKEPLRTIPLrEVLKVHECLvKSLLMRDNLFEII-T 78

                         90       100
                 ....*....|....*....|....*
gi 568910358 598 EQRNVYkdyrfleLACDSQEDVDSW 622
Cdd:cd13271   79 TSRTFY-------IQADSPEEMHSW 96
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 749-836 4.11e-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: 37.40  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  749 TVSTPAP-PPVDDSwlqhsrrSPPPSPTTqrrLTISAPLPRPTSGRGPAPAIPSpgpHSGAPPvpfrpgPLPPfpnsSDS 827
Cdd:pfam16058   3 SSITEPPrDPSGSY-------GEPPRAPS---SSYTEPQRDPSSSITEPPADPS---SSYTEP------PRDP----SGS 59


                  ....*....
gi 568910358  828 FGAPPQVPS 836
Cdd:pfam16058  60 YTEPQRDPS 68
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 752-841 4.11e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 752 TPAPPPVDDSWLQHSRRSPPPSPTTQRRltiSAPLPRPTSGRGPAPAIPSPG-PHSGAPPVPFRPGPLPPFPNSSDSFGA 830
Cdd:PRK07764 407 AAAPAPAAAAPAAAAAPAPAAAPQPAPA---PAPAPAPPSPAGNAPAGGAPSpPPAAAPSAQPAPAPAAAPEPTAAPAPA 483

                         90
                 ....*....|.
gi 568910358 831 PPQVPSRPTRA 841
Cdd:PRK07764 484 PPAAPAPAAAP 494
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 740-839 4.83e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 740 AIIGDINTATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPG--P 817
Cdd:PRK07764 661 DASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDpvP 740

                         90       100
                 ....*....|....*....|..
gi 568910358 818 LPPFPnssDSFGAPPQVPSRPT 839
Cdd:PRK07764 741 LPPEP---DDPPDPAGAPAQPP 759
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
 528-566 4.96e-03

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. 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: 270094  Cd Length: 104  Bit Score: 37.31  E-value: 4.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568910358 528 RKGWLtvsnigiMKGGSKG-----YWFVLTAESLSWYKD--DEEKE 566
Cdd:cd13275    1 KKGWL-------MKQGSRQgewskHWFVLRGAALKYYRDpsAEEAG 39
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 744-832 5.60e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.52  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  744 DINTATVSTPAP----PPVDDSWLQHSRRSPPPSPTTQrrltiSAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLP 819
Cdd:pfam03154 140 DNRSTSPSIPSPqdneSDSDSSAQQQILQTQPPVLQAQ-----SGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT 214

                          90
                  ....*....|...
gi 568910358  820 PFPNSSDSFGAPP 832
Cdd:pfam03154 215 SQPPNQTQSTAAP 227
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 747-839 5.82e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 747 TATVSTPAPPPVDDswlQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAiPSPGPHSGAPPVPfRPGPLPPFPNSSD 826
Cdd:PRK07764 417 PAAAAAPAPAAAPQ---PAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ-PAPAPAAAPEPTA-APAPAPPAAPAPA 491

                         90
                 ....*....|...
gi 568910358 827 sfgAPPQVPSRPT 839
Cdd:PRK07764 492 ---AAPAAPAAPA 501
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 728-837 6.23e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.08  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 728 MLRMYqALKEALAIIGDINTATvSTPAPPPVddswlqhsrrsPPPSPttqrrltisAPLPRPTSGRGPAPAIPSPGPHSG 807
Cdd:PRK14951 358 LLRLL-AFKPAAAAEAAAPAEK-KTPARPEA-----------AAPAA---------APVAQAAAAPAPAAAPAAAASAPA 415

                         90       100       110
                 ....*....|....*....|....*....|
gi 568910358 808 APPVPFRPGPLPPfPNSSDSFGAPPQVPSR 837
Cdd:PRK14951 416 APPAAAPPAPVAA-PAAAAPAAAPAAAPAA 444
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 748-841 7.49e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  748 ATVSTPAPPPVDDSWLQHSRRSPPPSPTTqrrlTISAPLPRPTSGRGPAPAIPSPGPHSG---------------APPVP 812
Cdd:PHA03307  261 APITLPTRIWEASGWNGPSSRPGPASSSS----SPRERSPSPSPSSPGSGPAPSSPRASSsssssressssstssSSESS 336

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568910358  813 ----FRPGPlPPFPNSSDSFGAPPQVPSRPTRA 841
Cdd:PHA03307  337 rgaaVSPGP-SPSRSPSPSRPPPPADPSSPRKR 368
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 747-851 8.74e-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: 38.13  E-value: 8.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 747 TATVSTPAPPPVDDSwlqhsrrSPPPSPTTQRR----LTISAPLPRPtSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFP 822
Cdd:cd21975   43 AKGPGPPGPAWKPDG-------ADSPGLVTAAPhllaANVLAPLRGP-SVEGSSLESGDADMGSDSDVAPASGAAASTSP 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568910358 823 NSSDSFGAPPQ------------VPSRPTRAPPSVPSRRPP 851
Cdd:cd21975  115 ESSSDAASSPSplsllhpgeaglEPERPRPRVRRGVRRRGV 155
PHA03378 PHA03378
EBNA-3B; Provisional
 748-838 8.85e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 8.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358 748 ATVSTPAPPPVDDSWLQH------SRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHsgAPPVPF---RPGPL 818
Cdd:PHA03378 718 AAATGRARPPAAAPGRARppaaapGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQ--APPAPQqrpRGAPT 795

                         90       100
                 ....*....|....*....|
gi 568910358 819 PPfpnssdsfgAPPQVPSRP 838
Cdd:PHA03378 796 PQ---------PPPQAGPTS 806
Tymo_45kd_70kd pfam03251
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a ...
 755-838 9.77e-03

Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a protein of unknown function that has been named based on its molecular weight. Tymoviruses such as the ononis yellow mosaic tymovirus encode only three proteins. Of these two are overlapping this protein overlaps a larger ORF that is thought to be the polymerase.


Pssm-ID: 281269 [Multi-domain]  Cd Length: 468  Bit Score: 39.39  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910358  755 PPPVDDS--------WLQHSRRSPPPSPTTqrrltisaPLPRPTSGRGPAPAIPSPGPHSGAPPVPFR----PGPLPPFP 822
Cdd:pfam03251 231 PPPLSDDpgilgprpLAPHSTRDPPPRPIT--------PGPSNTHDLRPLSVLPRTSPRRGLLPNPRRhrtsTGHIPPTT 302

                          90
                  ....*....|....*.
gi 568910358  823 NSSDSfgAPPQVPSRP 838
Cdd:pfam03251 303 TSRPT--GPPSRLQRP 316
 
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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