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Conserved domains on  [gi|1622827600|ref|XP_014979586|]
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dynamin-3 isoform X8 [Macaca mulatta]

Protein Classification

dynamin; dynamin family protein( 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| dynamin family protein is a large mechanochemical GTPase similar to dynamins and dynamin-like proteins (DLPs), which catalyze membrane fission during clathrin-mediated endocytosis; contains a dynamin middle domain

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 1.27e-161

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


:

Pssm-ID: 197491  Cd Length: 240  Bit Score: 469.74  E-value: 1.27e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600   86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  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 4.02e-140

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: 416.53  E-value: 4.02e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1622827600 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
514-625 5.86e-82

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: 258.02  E-value: 5.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 514 NQVIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVY 593
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622827600 594 KDYRFLELACDSQEDVDSWKASLLRAGVYPDK 625
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
645-735 1.56e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.86  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 645 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 724
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1622827600 725 LKEALGIIGDI 735
Cdd:pfam02212  81 LKQAREILSEV 91
MISS super family cl25801
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
743-833 1.61e-08

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: 56.15  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 743 PAPPPVDDSWiqHSRRSPPPSPTTQ-RRPTLSAPLTRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPSSS 815
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205
                          90       100
                  ....*....|....*....|....*..
gi 1622827600 816 DSFGAP---P------QVPSRPTRAPP 833
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPSGAPP 232
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
6-245 1.27e-161

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 469.74  E-value: 1.27e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600   86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  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 3.85e-148

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


Pssm-ID: 206738  Cd Length: 278  Bit Score: 436.68  E-value: 3.85e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRHE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1622827600 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 4.02e-140

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: 416.53  E-value: 4.02e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1622827600 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
514-625 5.86e-82

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: 258.02  E-value: 5.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 514 NQVIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVY 593
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622827600 594 KDYRFLELACDSQEDVDSWKASLLRAGVYPDK 625
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 3.56e-70

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 228.65  E-value: 3.56e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRHEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirEMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146
                         170       180
                  ....*....|....*....|..
gi 1622827600 186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
645-735 1.56e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.86  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 645 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 724
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1622827600 725 LKEALGIIGDI 735
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
644-735 9.76e-29

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 110.02  E-value: 9.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  644 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 723
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80
                           90
                   ....*....|..
gi 1622827600  724 ALKEALGIIGDI 735
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
516-619 1.13e-12

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: 64.88  E-value: 1.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  516 VIRKGWLTISNIGiMKGGSKGYWFVLTAESLSWYKDDEEKEK---KYMLPLDNLKVRD-VEKSFMSSKHIFALFNTEQRN 591
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKT 79
                           90       100
                   ....*....|....*....|....*...
gi 1622827600  592 VYkdyrfleLACDSQEDVDSWKASLLRA 619
Cdd:smart00233  80 LL-------LQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
516-619 2.06e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 64.12  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 516 VIRKGWLTISNIGImKGGSKGYWFVLTAESLSWYKDD---EEKEKKYMLPLDNLKVRDVEKSFMSS-KHIFALFNTEQRN 591
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79
                          90       100
                  ....*....|....*....|....*...
gi 1622827600 592 VykdyRFLELACDSQEDVDSWKASLLRA 619
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
743-833 1.61e-08

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: 56.15  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 743 PAPPPVDDSWiqHSRRSPPPSPTTQ-RRPTLSAPLTRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPSSS 815
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205
                          90       100
                  ....*....|....*....|....*..
gi 1622827600 816 DSFGAP---P------QVPSRPTRAPP 833
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPSGAPP 232
PHA03247 PHA03247
large tegument protein UL36; Provisional
744-848 1.64e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.80  E-value: 1.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  744 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSS---- 815
Cdd:PHA03247  2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAanep 2638
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622827600  816 ---DSFGAPPQVPSRPTRAPPSV--PRFGAMKDEAAEP 848
Cdd:PHA03247  2639 dphPPPTVPPPERPRDDPAPGRVsrPRRARRLGRAAQA 2676
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
753-837 1.58e-06

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: 51.54  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 753 IQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRpTRAP 832
Cdd:NF041121   18 AAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAALPVR-VPAP 96

                  ....*
gi 1622827600 833 PSVPR 837
Cdd:NF041121   97 PALPN 101
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
743-834 2.17e-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: 51.06  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 743 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTlsapltrptsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSfgAPP 822
Cdd:NF040983   97 PPPPPPPPTPPPPPPPPPPPPPPSPPPPP-------------PPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPI--QPT 161
                          90
                  ....*....|..
gi 1622827600 823 QVPSRPTRAPPS 834
Cdd:NF040983  162 QLPSIPNATPTS 173
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
736-835 3.28e-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: 40.02  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 736 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPT-SGRGPAPAIPSPGPHSGAP------------PVP 802
Cdd:cd21577    30 SSPPSSSSSSSSSSSSSSSPSSRASPPSPYSKSSPPSPPQQRPLSpPLSLPPPVAPPPLSPGSVPgglpvispvmvqPVP 109
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622827600 803 FR-PGPLPPFPSSSDSFGAPPQVPSRPTRAPPSV 835
Cdd:cd21577   110 VLyPPHLHQPIMVSSSPPPDDDHHHHKASSMKPS 143
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
737-837 3.38e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.52  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 737 TATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTrptsgrGPAPAIPSPGPhsGAPPVPFRPGPLPPFPSSSD 816
Cdd:NF040712  228 ATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAA------EPDEATRDAGE--PPAPGAAETPEAAEPPAPAP 299
                          90       100
                  ....*....|....*....|....*.
gi 1622827600 817 SFGAPPQVPS-----RPTRAPPSVPR 837
Cdd:NF040712  300 AAPAAPAAPEaeepaRPEPPPAPKPK 325
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
6-245 1.27e-161

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 469.74  E-value: 1.27e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600   86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  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 3.85e-148

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


Pssm-ID: 206738  Cd Length: 278  Bit Score: 436.68  E-value: 3.85e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRHE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1622827600 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 4.02e-140

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: 416.53  E-value: 4.02e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1622827600 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
514-625 5.86e-82

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: 258.02  E-value: 5.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 514 NQVIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVY 593
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622827600 594 KDYRFLELACDSQEDVDSWKASLLRAGVYPDK 625
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 3.56e-70

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 228.65  E-value: 3.56e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRHEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirEMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146
                         170       180
                  ....*....|....*....|..
gi 1622827600 186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
645-735 1.56e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.86  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 645 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 724
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1622827600 725 LKEALGIIGDI 735
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
644-735 9.76e-29

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 110.02  E-value: 9.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  644 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 723
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80
                           90
                   ....*....|..
gi 1622827600  724 ALKEALGIIGDI 735
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
516-619 1.13e-12

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: 64.88  E-value: 1.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  516 VIRKGWLTISNIGiMKGGSKGYWFVLTAESLSWYKDDEEKEK---KYMLPLDNLKVRD-VEKSFMSSKHIFALFNTEQRN 591
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKT 79
                           90       100
                   ....*....|....*....|....*...
gi 1622827600  592 VYkdyrfleLACDSQEDVDSWKASLLRA 619
Cdd:smart00233  80 LL-------LQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
516-619 2.06e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 64.12  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 516 VIRKGWLTISNIGImKGGSKGYWFVLTAESLSWYKDD---EEKEKKYMLPLDNLKVRDVEKSFMSS-KHIFALFNTEQRN 591
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79
                          90       100
                  ....*....|....*....|....*...
gi 1622827600 592 VykdyRFLELACDSQEDVDSWKASLLRA 619
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
518-616 7.13e-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: 59.48  E-value: 7.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 518 RKGWLTISNIGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKY--MLPLDN-LKVRDVEKSfmSSKHIFALFNTEQRNVYk 594
Cdd:cd00821     1 KEGYLLKRGGGGLKSWKK-RWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76
                          90       100
                  ....*....|....*....|..
gi 1622827600 595 dyrfleLACDSQEDVDSWKASL 616
Cdd:cd00821    77 ------LQADSEEERQEWLKAL 92
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
516-619 1.06e-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: 56.94  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 516 VIRKGWLTisnigiMKGGS----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSfmSSKHIFALFNTEQRN 591
Cdd:cd01252     3 PDREGWLL------KLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVEDK--KKPFCFELYSPSNGQ 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622827600 592 VYKD----------------YRfleLACDSQEDVDSWKASLLRA 619
Cdd:cd01252    75 VIKAcktdsdgkvvegnhtvYR---ISAASEEERDEWIKSIKAS 115
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
743-833 1.61e-08

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: 56.15  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 743 PAPPPVDDSWiqHSRRSPPPSPTTQ-RRPTLSAPLTRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPSSS 815
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205
                          90       100
                  ....*....|....*....|....*..
gi 1622827600 816 DSFGAP---P------QVPSRPTRAPP 833
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPSGAPP 232
PHA03247 PHA03247
large tegument protein UL36; Provisional
744-848 1.64e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.80  E-value: 1.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  744 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSS---- 815
Cdd:PHA03247  2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAanep 2638
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622827600  816 ---DSFGAPPQVPSRPTRAPPSV--PRFGAMKDEAAEP 848
Cdd:PHA03247  2639 dphPPPTVPPPERPRDDPAPGRVsrPRRARRLGRAAQA 2676
PHA02682 PHA02682
ORF080 virion core protein; Provisional
738-836 2.74e-08

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 56.02  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 738 ATVSTPAPP--------PVDDSWIQHSRR---SPPPSPTT-QRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFrP 805
Cdd:PHA02682   32 ATIPAPAAPcppdadvdPLDKYSVKEAGRyyqSRLKANSAcMQRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVTC-P 110
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622827600 806 GPLPPFPSSSDSFGAPPQVPSRPTRAPPSVP 836
Cdd:PHA02682  111 APAPACPPATAPTCPPPAVCPAPARPAPACP 141
PHA03247 PHA03247
large tegument protein UL36; Provisional
742-846 5.90e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 5.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  742 TPaPPPVDD--SWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSG------RGPAPA-IPSPGPHSGAPPVPfrPGPLPPFP 812
Cdd:PHA03247   360 TP-PSSLEDlsAGRHHPKRASLPTRKRRSARHAATPFARGPGGddqtrpAAPVPAsVPTPAPTPVPASAP--PPPATPLP 436
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1622827600  813 SSSDSFGAPPQVPSRPTRAPPSVPRFGAMKDEAA 846
Cdd:PHA03247   437 SAEPGSDDGPAPPPERQPPAPATEPAPDDPDDAT 470
PHA03247 PHA03247
large tegument protein UL36; Provisional
733-836 7.80e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 7.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  733 GDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSgrGPAPAIPSPGPHSGAPPVPFRPGPLPPFP 812
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA--GPPRRLTRPAVASLSESRESLPSPWDPAD 2806
                           90       100
                   ....*....|....*....|....
gi 1622827600  813 SSSDSFGAPPQVPSRPTRAPPSVP 836
Cdd:PHA03247  2807 PPAAVLAPAAALPPAASPAGPLPP 2830
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
736-848 7.97e-08

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: 54.22  E-value: 7.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 736 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPT-LSAPltrPTSGRGPAPAIPSPGphsgaPPVPFrPGPLPPFPSS 814
Cdd:pfam15822  52 STAPSTVPFGPAPTGMYPSIPLTGPSPGPPAPFPPSgPSCP---PPGGPYPAPTVPGPG-----PIGPY-PTPNMPFPEL 122
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622827600 815 SDSFGAppqvPSRPTRAPPSVPRfGAMKDEAAEP 848
Cdd:pfam15822 123 PRPYGA----PTDPAAAAPSGPW-GSMSSGPWAP 151
PHA03247 PHA03247
large tegument protein UL36; Provisional
735-837 2.03e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  735 ISTATVSTPAPPPVddswiQHSRRSPPPSPTTQRRPTLSAPLTR----PTSGRGPAPAIPSPGPHSGAPPVPFRPGP--- 807
Cdd:PHA03247  2891 VSRSTESFALPPDQ-----PERPPQPQAPPPPQPQPQPPPPPQPqpppPPPPRPQPPLAPTTDPAGAGEPSGAVPQPwlg 2965
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1622827600  808 -LPPFPSSSDSFGAPPQVPSRPTRAPPSVPR 837
Cdd:PHA03247  2966 aLVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
PHA03247 PHA03247
large tegument protein UL36; Provisional
736-837 2.62e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  736 STATVSTPAPPPVDDSWIQHSRRSPPPSPTT------------QRRPTLSAPLTRP-TSGRGPAPAIPSPGPHSGAPPVP 802
Cdd:PHA03247  2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvapggdvRRRPPSRSPAAKPaAPARPPVRRLARPAVSRSTESFA 2899
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622827600  803 FRPGPLPPFPS----SSDSFGAPPQVPSRPTRAPPSVPR 837
Cdd:PHA03247  2900 LPPDQPERPPQpqapPPPQPQPQPPPPPQPQPPPPPPPR 2938
PHA03247 PHA03247
large tegument protein UL36; Provisional
744-848 3.02e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 3.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  744 APPPVDDswIQHSRRSPPPSPTTQRRPTLSAPLTR----PTSGRGPAPA-----IPSPGPHSGAPPVPFRPGPLPPFPSS 814
Cdd:PHA03247  2688 ARPTVGS--LTSLADPPPPPPTPEPAPHALVSATPlppgPAAARQASPAlpaapAPPAVPAGPATPGGPARPARPPTTAG 2765
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1622827600  815 SDSfGAPPQVPsrPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PHA03247  2766 PPA-PAPPAAP--AAGPPRRLTRPAVASLSESRE 2796
PHA03378 PHA03378
EBNA-3B; Provisional
745-848 3.55e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 54.30  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 745 PPPVDDSWIQHSRRSPPPSPT---TQRRPTlSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPfPSSSDSFGAP 821
Cdd:PHA03378  659 ITPYKPTWTQIGHIPYQPSPTganTMLPIQ-WAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARP-PAAAPGRARP 736
                          90       100
                  ....*....|....*....|....*..
gi 1622827600 822 PQvpSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PHA03378  737 PA--AAPGRARPPAAAPGRARPPAAAP 761
PHA03247 PHA03247
large tegument protein UL36; Provisional
741-846 6.46e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 6.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  741 STPAPPPVDDSWIQHSRR-SPPPSPTTQRRPtlsapltRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLP---------- 809
Cdd:PHA03247  2571 PRPAPRPSEPAVTSRARRpDAPPQSARPRAP-------VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPaanepdphpp 2643
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622827600  810 ---PFPSSSDSFGAPPQV--------PSRPTRA--PPSVPRFGAMKDEAA 846
Cdd:PHA03247  2644 ptvPPPERPRDDPAPGRVsrprrarrLGRAAQAssPPQRPRRRAARPTVG 2693
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
503-619 8.55e-07

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: 8.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 503 SSQVHKKTTIgnqviRKGWltisnigimkggsKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNL----KVRDVEKsfmss 578
Cdd:cd13298     9 SGYLLKRSRK-----TKNW-------------KKRWVVLRPCQLSYYKDEKEYKLRRVINLSELlavaPLKDKKR----- 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622827600 579 KHIFALFNTEqrnvyKDYRFlelACDSQEDVDSWkASLLRA 619
Cdd:cd13298    66 KNVFGIYTPS-----KNLHF---RATSEKDANEW-VEALRE 97
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
516-619 1.13e-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: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 516 VIRKGWLTisnigimKGGSKGY------WFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSF-MSSKHIFALFNTE 588
Cdd:cd13248     7 VVMSGWLH-------KQGGSGLknwrkrWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHAN 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622827600 589 QRNVYkdyrfleLACDSQEDVDSWKASLLRA 619
Cdd:cd13248    80 MRTYY-------FAADTAEEMEQWMNAMSLA 103
PHA03264 PHA03264
envelope glycoprotein D; Provisional
741-837 1.42e-06

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 51.54  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 741 STP-APPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPF--PSSSDS 817
Cdd:PHA03264  261 SKGyEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDAdrPEGWPS 340
                          90       100
                  ....*....|....*....|
gi 1622827600 818 FGAPPQVPsrPTRAPPSVPR 837
Cdd:PHA03264  341 LEAITFPP--PTPATPAVPR 358
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
753-837 1.58e-06

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: 51.54  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 753 IQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRpTRAP 832
Cdd:NF041121   18 AAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAALPVR-VPAP 96

                  ....*
gi 1622827600 833 PSVPR 837
Cdd:NF041121   97 PALPN 101
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
735-837 1.65e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  735 ISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRR------PTLSAPLTRPTSGRGPAPAIPSPGP---------HSGAP 799
Cdd:PHA03307   195 PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAAddagasSSDSSSSESSGCGWGPENECPLPRPapitlptriWEASG 274
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622827600  800 PVPFRPGPLPPFPSSSDSFGAPPQVPSRPtRAPPSVPR 837
Cdd:PHA03307   275 WNGPSSRPGPASSSSSPRERSPSPSPSSP-GSGPAPSS 311
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
743-834 2.17e-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: 51.06  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 743 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTlsapltrptsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSfgAPP 822
Cdd:NF040983   97 PPPPPPPPTPPPPPPPPPPPPPPSPPPPP-------------PPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPI--QPT 161
                          90
                  ....*....|..
gi 1622827600 823 QVPSRPTRAPPS 834
Cdd:NF040983  162 QLPSIPNATPTS 173
PHA03247 PHA03247
large tegument protein UL36; Provisional
738-841 2.72e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  738 ATVSTPAPPPVddswiqhsRR--SPPPSPTTQRRPTLSAPLTRPTSGRGPAPaiPSPGPHSGAPPVPFRPGPLPPFPSSS 815
Cdd:PHA03247  2873 AKPAAPARPPV--------RRlaRPAVSRSTESFALPPDQPERPPQPQAPPP--PQPQPQPPPPPQPQPPPPPPPRPQPP 2942
                           90       100
                   ....*....|....*....|....*.
gi 1622827600  816 DSFGAPPQVPSRPTRAPPSvPRFGAM 841
Cdd:PHA03247  2943 LAPTTDPAGAGEPSGAVPQ-PWLGAL 2967
PHA03378 PHA03378
EBNA-3B; Provisional
742-836 3.01e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 51.22  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 742 TPAPPPVddswIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPfPSSSDSFGAP 821
Cdd:PHA03378  702 TPMRPPA----APPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARP-PAAAPGAPTP 776
                          90
                  ....*....|....*...
gi 1622827600 822 ---PQVPSRPTRAPPSVP 836
Cdd:PHA03378  777 qppPQAPPAPQQRPRGAP 794
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
730-848 4.05e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.75  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 730 GIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPG--P 807
Cdd:PRK07764  661 DASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDpvP 740
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622827600 808 LPPFPSSSDSFG------------APPQVPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PRK07764  741 LPPEPDDPPDPAgapaqpppppapAPAAAPAAAPPPSPPSEEEEMAEDDAPSM 793
PHA03247 PHA03247
large tegument protein UL36; Provisional
736-836 6.50e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 6.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  736 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAP-----LTRPTSGRGPA------PAIPSPGPHSGAPPVPfr 804
Cdd:PHA03247  2762 TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdpadPPAAVLAPAAAlppaasPAGPLPPPTSAQPTAP-- 2839
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622827600  805 PGPLPPFPSSSDSFGA-PPQVPSR---PTRAPPSVP 836
Cdd:PHA03247  2840 PPPPGPPPPSLPLGGSvAPGGDVRrrpPSRSPAAKP 2875
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
739-836 6.60e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 49.81  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 739 TVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPtsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSF 818
Cdd:PRK14950  358 ALLVPVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIP-----PKEPVRETATPPPVPPRPVAPPVPHTPESAPKLT 432
                          90
                  ....*....|....*...
gi 1622827600 819 GAPPQVPSRPTRAPPSVP 836
Cdd:PRK14950  433 RAAIPVDEKPKYTPPAPP 450
PHA03377 PHA03377
EBNA-3C; Provisional
739-837 7.44e-06

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 49.67  E-value: 7.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  739 TVSTPAPP---PVDD---SWIQHSRRSPPP-SPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPV-------PFR 804
Cdd:PHA03377   525 SVTQPAKPhrkVQDGfqrSGRRQKRATPPKvSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPStgprqqaKCK 604
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1622827600  805 PGPlppfPSSSDSFGAPPQvpSRPTRAPPSVPR 837
Cdd:PHA03377   605 DGP----PASGPHEKQPPS--SAPRDMAPSVVR 631
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
705-835 8.90e-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: 48.38  E-value: 8.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 705 MEESAEQAQRRDemlRMYQALkeALGIIGDISTATVSTPA-----PPPVddswiqhsrrSPPPSPTTqrrptlSAPLTRP 779
Cdd:pfam07174   1 MDQVDPNSTRRK---GLWATL--AIAAVAGASAVAVALPAvahadPEPA----------PPPPSTAT------APPAPPP 59
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622827600 780 TSgrgPAPAIPSPGPhsgAPPVPFRPGPlPPFPSSSDSFGAPPQVPSRPtrAPPSV 835
Cdd:pfam07174  60 PP---PAPAAPAPPP---PPAAPNAPNA-PPPPADPNAPPPPPADPNAP--PPPAV 106
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
733-848 8.95e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.78  E-value: 8.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  733 GDISTATVSTPAPPPVDDSwiqhsrrsPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFR-------- 804
Cdd:PHA03307   107 TPPGPSSPDPPPPTPPPAS--------PPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRqaalplss 178
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622827600  805 --------PGPLPPFPSSSDSFGAP--PQVPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PHA03307   179 peetarapSSPPAEPPPSTPPAAASprPPRRSSPISASASSPAPAPGRSAADDA 232
PHA03247 PHA03247
large tegument protein UL36; Provisional
727-848 8.97e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 8.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  727 EALGIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPT-------------SGRGP---APAIP 790
Cdd:PHA03247  2796 ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSlplggsvapggdvRRRPPsrsPAAKP 2875
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622827600  791 SPGPHsgaPPVpfRPGPLPPFPSSSDSFGAPPQVPSR-PTRAPPSVPRFGAMKDEAAEP 848
Cdd:PHA03247  2876 AAPAR---PPV--RRLARPAVSRSTESFALPPDQPERpPQPQAPPPPQPQPQPPPPPQP 2929
PHA03321 PHA03321
tegument protein VP11/12; Provisional
735-848 1.15e-05

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 49.19  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 735 ISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAI-------PSPGPHSGAP-------P 800
Cdd:PHA03321  404 LATELFRTGVPSEHYEASLRLLSSRQPPGAPAPRRDNDPPPPPRARPGSTPACARraraqraRDAGPEYVDPlgalrrlP 483
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622827600 801 VPFRPGPLPPFPSSSDSF-----GAPPQVPSRPTRAPPSVPRFGAmkDEAAEP 848
Cdd:PHA03321  484 AGAAPPPEPAAAPSPATYytrmgGGPPRLPPRNRATETLRPDWGP--PAAAPP 534
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
736-848 1.62e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.72  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 736 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRptlSAPLTRPTSGRGPAPAiPSPGPHSGAPPVPfrPGPLPPfPSSS 815
Cdd:PRK12323  404 AAPAAAPAAAAAARAVAAAPARRSPAPEALAAAR---QASARGPGGAPAPAPA-PAAAPAAAARPAA--AGPRPV-AAAA 476
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622827600 816 DSFGAPPQVPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PRK12323  477 AAAPARAAPAAAPAPADDDPPPWEELPPEFASP 509
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
738-848 1.68e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  738 ATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPlTRPTSGRGPAPAIPSPGPHSGAP----------------PV 801
Cdd:PHA03307   261 APITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP-SPSSPGSGPAPSSPRASSSSSSSressssstssssessrGA 339
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1622827600  802 PFRPGPlPPFPSSSDSFGAPPQVPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PHA03307   340 AVSPGP-SPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP 385
PHA03247 PHA03247
large tegument protein UL36; Provisional
745-836 1.89e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  745 PPPVDDSWIQHSRRSPPPSPTTQRRPTL-SAPLTRPTSGRGPAPAI--------PSPGPHSGAPPVPFRPG-PLPPFPSS 814
Cdd:PHA03247  2648 PPERPRDDPAPGRVSRPRRARRLGRAAQaSSPPQRPRRRAARPTVGsltsladpPPPPPTPEPAPHALVSAtPLPPGPAA 2727
                           90       100
                   ....*....|....*....|..
gi 1622827600  815 SDsfGAPPQVPSRPtrAPPSVP 836
Cdd:PHA03247  2728 AR--QASPALPAAP--APPAVP 2745
PHA03247 PHA03247
large tegument protein UL36; Provisional
741-833 2.31e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  741 STPAPPPVDDswiqHSRRSPPPSP----TTQRRPTLSAPLTRPTSGRGPAPA---------IPSPGPHSGAPPVPFRPGP 807
Cdd:PHA03247  2612 APPSPLPPDT----HAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGrvsrprrarRLGRAAQASSPPQRPRRRA 2687
                           90       100
                   ....*....|....*....|....*.
gi 1622827600  808 LPPFPSSSDSFGAPPQVPSRPTRAPP 833
Cdd:PHA03247  2688 ARPTVGSLTSLADPPPPPPTPEPAPH 2713
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
736-836 2.60e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 736 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPtlsAPLTRPTSGRGPAPAIPSPGP-HSGAPPVPFRPGPLPPFPSS 814
Cdd:PRK07764  401 AAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAP---APAPAPPSPAGNAPAGGAPSPpPAAAPSAQPAPAPAAAPEPT 477
                          90       100
                  ....*....|....*....|...
gi 1622827600 815 SDSFGAPPQVPSRPTR-APPSVP 836
Cdd:PRK07764  478 AAPAPAPPAAPAPAAApAAPAAP 500
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
697-833 2.79e-05

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.84  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 697 SSEDQNTLMEESAEQAQRRDEMLrmyqALKEALGII-----GDISTATVSTPAPPPVDDSwiQHSRRSPPPSPTTQRRPT 771
Cdd:pfam03154 150 SPQDNESDSDSSAQQQILQTQPP----VLQAQSGAAsppspPPPGTTQAATAGPTPSAPS--VPPQGSPATSQPPNQTQS 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 772 LSAPLTRPTSG------RGPAP-------------------AIPSPGPHSGAPPVPFR--------PGPLPPFPSSSDSF 818
Cdd:pfam03154 224 TAAPHTLIQQTptlhpqRLPSPhpplqpmtqppppsqvspqPLPQPSLHGQMPPMPHSlqtgpshmQHPVPPQPFPLTPQ 303
                         170
                  ....*....|....*
gi 1622827600 819 GAPPQVPSRPTRAPP 833
Cdd:pfam03154 304 SSQSQVPPGPSPAAP 318
PHA03247 PHA03247
large tegument protein UL36; Provisional
736-841 3.16e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  736 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTS-GRGPAPAIPSPGPHSGA-----PPVPFRPGPLP 809
Cdd:PHA03247  2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSeSRESLPSPWDPADPPAAvlapaAALPPAASPAG 2826
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622827600  810 PFPSSSDSFGAPPQVPSRPTraPPSVPRFGAM 841
Cdd:PHA03247  2827 PLPPPTSAQPTAPPPPPGPP--PPSLPLGGSV 2856
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
743-836 3.35e-05

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 44.86  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 743 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPApaIPSPGPHSGA---PPVPFRPG-----PLPPFPSS 814
Cdd:pfam06346   1 PPPPPLPGDSSTIPLPPGACIPTPPPLPGGGGPPPPPPLPGSAA--IPPPPPLPGGtsiPPPPPLPGaasipPPPPLPGS 78
                          90       100
                  ....*....|....*....|..
gi 1622827600 815 SDsFGAPPQVPSRPTRAPPSVP 836
Cdd:pfam06346  79 TG-IPPPPPLPGGAGIPPPPPP 99
PHA03378 PHA03378
EBNA-3B; Provisional
736-836 3.63e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 47.75  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 736 STATVSTPAPPpvddSWIQHSRRSPPPSPTTQRRPTLS-APLTRPTSGRGPAPAiPSPGPHSGAPPVPfRPGPLPPfPSS 814
Cdd:PHA03378  677 SPTGANTMLPI----QWAPGTMQPPPRAPTPMRPPAAPpGRAQRPAAATGRARP-PAAAPGRARPPAA-APGRARP-PAA 749
                          90       100
                  ....*....|....*....|..
gi 1622827600 815 SDSFGAPPQVPSRPTRAPPSVP 836
Cdd:PHA03378  750 APGRARPPAAAPGRARPPAAAP 771
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
516-618 3.84e-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: 43.78  E-value: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 516 VIRKGWLTiSNIGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMS-SKHIFALF---NTEQRN 591
Cdd:cd13378     3 VLKAGWLK-KQRSIMKNWQQ-RWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNELPPNPEEpGKHLFEILpggAGDREK 80
                          90       100
                  ....*....|....*....|....*..
gi 1622827600 592 VYKDYRFLELACDSQEDVDSWKASLLR 618
Cdd:cd13378    81 VPMNHEAFLLMANSQSDMEDWVKAIRR 107
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
712-848 4.04e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 712 AQRRDEMLRmyQALKEALGIIGDIsTATVSTP---APPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPA 788
Cdd:PRK07764  563 SPGNAEVLV--TALAEELGGDWQV-EAVVGPApgaAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEA 639
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622827600 789 IPSPGPHSGAPPVPFRPGPLPPFPSSSDSFG------APPQVPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PRK07764  640 SAAPAPGVAAPEHHPKHVAVPDASDGGDGWPakaggaAPAAPPPAPAPAAPAAPAGAAPAQPAPAP 705
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
737-840 5.24e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.02  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 737 TATVSTPAPPPVddswiQHSRRSPPPSPTTQRRPTlSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSD 816
Cdd:PRK14951  385 EAAAPAAAPVAQ-----AAAAPAPAAAPAAAASAP-AAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPE 458
                          90       100
                  ....*....|....*....|....
gi 1622827600 817 SFGAPPQVPSRPTRAPPSVPRFGA 840
Cdd:PRK14951  459 TVAIPVRVAPEPAVASAAPAPAAA 482
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
735-831 7.94e-05

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: 46.45  E-value: 7.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 735 ISTATVSTPAPPPVDDSwiqHSRRSPPPSP----TTQRRPTLSAP---LTRPT-SGRGPAPAIPSPGPHSGAP------- 799
Cdd:pfam05109 468 VSTADVTSPTPAGTTSG---ASPVTPSPSPrdngTESKAPDMTSPtsaVTTPTpNATSPTPAVTTPTPNATSPtlgktsp 544
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622827600 800 ------PVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRA 831
Cdd:pfam05109 545 tsavttPTPNATSPTPAVTTPTPNATIPTLGKTSPTSA 582
PH2_PH_fungal cd13299
Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal ...
535-616 8.38e-05

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: 42.23  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 535 KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLkVRDVEKSFMSSKHIFAL-FNTEQrnvyKDYRFlelACDSQEDVDSWK 613
Cdd:cd13299    24 KKYWLVLRNRSLSFYKDQSEYSPVKIIPIDDI-IDVVELDPLSKSKKWCLqIITPE----KRIRF---CADDEESLIKWL 95

                  ...
gi 1622827600 614 ASL 616
Cdd:cd13299    96 GAL 98
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
736-833 1.22e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 45.48  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 736 STATVSTPAPPPVddswiqhSRRSPPPSPTTQRRP--TLSAPLTRPTSGRGPAPAIPSPGPHSGAPP------VPFRPGP 807
Cdd:PRK14951  396 QAAAAPAPAAAPA-------AAASAPAAPPAAAPPapVAAPAAAAPAAAPAAAPAAVALAPAPPAQAapetvaIPVRVAP 468
                          90       100
                  ....*....|....*....|....*.
gi 1622827600 808 LPPFPSSSDSfGAPPQVPSRPTRAPP 833
Cdd:PRK14951  469 EPAVASAAPA-PAAAPAAARLTPTEE 493
PHA03247 PHA03247
large tegument protein UL36; Provisional
737-848 1.27e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  737 TATVSTPAPPPVDDSWIQHS-----RRSPPPSPTTQRRPTLSAPLTRPtsgrgPAPAIP-SPGPHSGAPPVPFRPGPLPP 810
Cdd:PHA03247  2713 HALVSATPLPPGPAAARQASpalpaAPAPPAVPAGPATPGGPARPARP-----PTTAGPpAPAPPAAPAAGPPRRLTRPA 2787
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622827600  811 FPSSSDSFGAPPQvPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PHA03247  2788 VASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASP 2824
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
703-825 1.34e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 45.22  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 703 TLMEESAEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPvddswiqhsrrsPPPSPTTQRRPTLSAPL-TRPTS 781
Cdd:PRK14963  313 TALDEQMERFARRSDALSLELALLHALLALGGAPSEGVAAVAPPA------------PAPADLTQRLNRLEKEVrSLRSA 380
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622827600 782 GRGPAPAIPSPGPHSGapPVPFR-PGPLPPFPSSSDSFGAPPQVP 825
Cdd:PRK14963  381 PTAAATAAGAPLPDFD--PRPRGpPAPEPARSAEAPPLVAPAAAP 423
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
514-616 1.59e-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: 41.84  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 514 NQVIRKGWLTisnigiMKGGSKG----YWFVLTAESLSWYKDDEEkekKYmLPLDNLKVRDV-----EKSFMSSKHIFAL 584
Cdd:cd13215    19 GAVIKSGYLS------KRSKRTLrytrYWFVLKGDTLSWYNSSTD---LY-FPAGTIDLRYAtsielSKSNGEATTSFKI 88
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622827600 585 FNTEQRnvykdYRFLelaCDSQEDVDSWKASL 616
Cdd:cd13215    89 VTNSRT-----YKFK---ADSETSADEWVKAL 112
PHA03247 PHA03247
large tegument protein UL36; Provisional
743-848 1.67e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  743 PAPPPVDDswiqhsrrspPPSPTTQRrptlSAPLTRPTSgRGPAPAIPSPGPHSGAPPVPFRP----GPLPPFPSSSDSF 818
Cdd:PHA03247  2551 PPPPLPPA----------APPAAPDR----SVPPPRPAP-RPSEPAVTSRARRPDAPPQSARPrapvDDRGDPRGPAPPS 2615
                           90       100       110
                   ....*....|....*....|....*....|
gi 1622827600  819 GAPPQVPsrPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PHA03247  2616 PLPPDTH--APDPPPPSPSPAANEPDPHPP 2643
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
760-836 1.71e-04

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


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 41.25  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 760 PPPSPTT-QRRPTLS--APLTRPTSGRGPAPAIPSPGphSGAPPVPfrpgplppfPSSSdsFGAPPQVPSRPTRAPPSVP 836
Cdd:pfam16058   1 PSSSITEpPRDPSGSygEPPRAPSSSYTEPQRDPSSS--ITEPPAD---------PSSS--YTEPPRDPSGSYTEPQRDP 67
PHA03378 PHA03378
EBNA-3B; Provisional
738-836 1.80e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 738 ATVSTPAPPPV-DDSWIQHSRRSPPPSPTTQRRPT-LSAPLTRPTSGRGP--APAIPSPGPHSGAPPVPF---RPGPLPP 810
Cdd:PHA03378  718 AAATGRARPPAaAPGRARPPAAAPGRARPPAAAPGrARPPAAAPGRARPPaaAPGAPTPQPPPQAPPAPQqrpRGAPTPQ 797
                          90       100
                  ....*....|....*....|....*..
gi 1622827600 811 fpsssdsfgAPPQVPSRPTR-APPSVP 836
Cdd:PHA03378  798 ---------PPPQAGPTSMQlMPRAAP 815
PH_Boi cd13316
Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally ...
519-619 1.90e-04

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: 41.20  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 519 KGWLTisnigiMKGGSKGYW----FVLTAESLSWYKDDEEKEKKYMLPLDNLKV-RDVEKSFMSSKHIFALFNTEQRNVY 593
Cdd:cd13316     3 SGWMK------KRGERYGTWktryFVLKGTRLYYLKSENDDKEKGLIDLTGHRVvPDDSNSPFRGSYGFKLVPPAVPKVH 76
                          90       100
                  ....*....|....*....|....*.
gi 1622827600 594 kdYrfleLACDSQEDVDSWKASLLRA 619
Cdd:cd13316    77 --Y----FAVDEKEELREWMKALMKA 96
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
732-846 1.96e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  732 IGDISTATVSTPAPPPVDDSwiqhsRRSPPPSP--------TTQRRPTLSAPLTRPT-------SGRGPAPAIPSPGPHS 796
Cdd:PHA03307   273 SGWNGPSSRPGPASSSSSPR-----ERSPSPSPsspgsgpaPSSPRASSSSSSSRESsssstssSSESSRGAAVSPGPSP 347
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622827600  797 GAPPVPFRPGPlPPFPSSSDSFGAPPQVPSRPTRAPPSVPRFGAMKDEAA 846
Cdd:PHA03307   348 SRSPSPSRPPP-PADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAG 396
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
513-566 2.02e-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: 2.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622827600 513 GNQVIRKGWLTISNIGIMKGGS---KGYWFVLTAESLSWYKD-DEEKEKKYMLPLDNL 566
Cdd:cd13297    10 GQDVIERGWLYKEGGKGGARGNltkKKRWFVLTGNSLDYYKSsEKNSLKLGTLVLNSL 67
PHA03377 PHA03377
EBNA-3C; Provisional
752-836 2.03e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 45.04  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  752 WIQHSRRSPPPSPTTQRRPTLSaPLTRPTSGrgPAPAIPSPGPHSGAPPVPFRP----GPLPPFPSSSDSFGAP------ 821
Cdd:PHA03377   813 WSQYPGHGHPQGPWAPRPPHLP-PQWDGSAG--HGQDQVSQFPHLQSETGPPRLqlsqVPQLPYSQTLVSSSAPswsspq 889
                           90
                   ....*....|....*...
gi 1622827600  822 PQVPSR--PTRAP-PSVP 836
Cdd:PHA03377   890 PRAPIRpiPTRFPpPPMP 907
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
697-839 2.06e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 42.72  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 697 SSEDQNTLMEESAEQAQRRDEmlrmyQALKEALGIIGDISTATVSTPAPPPVDDSwiqHSRRSPPPSPTTQRRPTLSAPL 776
Cdd:pfam15240  24 SQEDSPSLISEEEGQSQQGGQ-----GPQGPPPGGFPPQPPASDDPPGPPPPGGP---QQPPPQGGKQKPQGPPPQGGPR 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622827600 777 TRPTSGRGPAPaipSPGPHSGAPPVPFRP-GPLP----PFPSSSDSFGAPPQVPSRPTRAPPSVPRFG 839
Cdd:pfam15240  96 PPPGKPQGPPP---QGGNQQQGPPPPGKPqGPPPqgggPPPQGGNQQGPPPPPPGNPQGPPQRPPQPG 160
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
736-848 2.18e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 736 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSG-----RGPAPAIPSPGPHSGAPPVPfRPGPLPP 810
Cdd:PRK07764  642 APAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAapaapAGAAPAQPAPAPAATPPAGQ-ADDPAAQ 720
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622827600 811 FPSSSDSFGAPPQVPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PRK07764  721 PPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP 758
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
759-837 2.35e-04

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


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 41.60  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 759 SPPPSPTTQRRPTLSAPLTRPTSGRGPAPAI--PSPGPHSGAPPVPfrPGPLPPFPSSSDSFGAPPqVPSRPTRAPPSVP 836
Cdd:pfam12526  30 SPPESAHPDPPPPVGDPRPPVVDTPPPVSAVwvLPPPSEPAAPEPD--LVPPVTGPAGPPSPLAPP-APAQKPPLPPPRP 106

                  .
gi 1622827600 837 R 837
Cdd:pfam12526 107 Q 107
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
738-847 2.80e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  738 ATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRP------TSGRGPAPAI---------PSPGPHS---GAP 799
Cdd:PHA03307   119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAavasdaASSRQAALPLsspeetaraPSSPPAEpppSTP 198
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622827600  800 PVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRAPPSVPRFGAMKDEAAE 847
Cdd:PHA03307   199 PAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSG 246
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
757-841 3.04e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 44.35  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 757 RRSPPPSPTTQRRPTlSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSF-GAPPQVPSRPTRAPPSV 835
Cdd:PRK14965  379 RGAPAPPSAAWGAPT-PAAPAAPPPAAAPPVPPAAPARPAAARPAPAPAPPAAAAPPARSADpAAAASAGDRWRAFVAFV 457
                          90
                  ....*....|
gi 1622827600 836 ----PRFGAM 841
Cdd:PRK14965  458 kgkkPALGAS 467
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
709-848 3.94e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.10  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 709 AEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPVDdswiqhsrRSPPPSPTTQRRP-TLSAPLTRPTSGRGPAP 787
Cdd:PRK12323  420 AAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAA--------AARPAAAGPRPVAaAAAAAPARAAPAAAPAP 491
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622827600 788 AIPSPGPHSGAPPVPFRPGPLPPFP--------SSSDSFGAPPQvPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PRK12323  492 ADDDPPPWEELPPEFASPAPAQPDAapagwvaeSIPDPATADPD-DAFETLAPAPAAAPAPRAAAATEP 559
PHA03247 PHA03247
large tegument protein UL36; Provisional
764-847 5.05e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  764 PTTQRRPTLSAPLTRPTSGRGPAPAIP-----SPGPHSGAPPVPFRPGPLPPFPSSSDS--------FGAPPQVPSRPTR 830
Cdd:PHA03247   236 PFVERRVVISHPLRGDIAAPAPPPVVGegadrAPETARGATGPPPPPEAAAPNGAAAPPdgvwgaalAGAPLALPAPPDP 315
                           90
                   ....*....|....*..
gi 1622827600  831 APPsvPRFGAMKDEAAE 847
Cdd:PHA03247   316 PPP--APAGDAEEEDDE 330
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
741-848 5.29e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  741 STPAPPPVDDSWIQHSRRSPPPSPT-TQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAP---PVPFRPGPLPPFPSSSD 816
Cdd:PHA03307    67 PPTGPPPGPGTEAPANESRSTPTWSlSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPppsPAPDLSEMLRPVGSPGP 146
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622827600  817 SF---GAPPQVPSRPTRAPPSVPR----FGAMKDEAAEP 848
Cdd:PHA03307   147 PPaasPPAAGASPAAVASDAASSRqaalPLSSPEETARA 185
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
736-837 6.67e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 736 STATVSTPAPPPVDDSWIQHSRRSPPPSP----TTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPF 811
Cdd:PRK07764  608 PPEEAARPAAPAAPAAPAAPAPAGAAAAPaeasAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAP 687
                          90       100
                  ....*....|....*....|....*.
gi 1622827600 812 PSSSDSFGAPPQVPSRPTRAPPSVPR 837
Cdd:PRK07764  688 AAPAAPAGAAPAQPAPAPAATPPAGQ 713
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
741-840 6.84e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 741 STPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSfGA 820
Cdd:PRK07764  627 PAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP-AP 705
                          90       100
                  ....*....|....*....|
gi 1622827600 821 PPQVPSRPTRAPPSVPRFGA 840
Cdd:PRK07764  706 AATPPAGQADDPAAQPPQAA 725
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
738-848 8.18e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 8.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 738 ATVSTPAPPPVddswiqhSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPfrpgPLPPFPSSSDS 817
Cdd:PRK07764  391 AGAPAAAAPSA-------AAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNA----PAGGAPSPPPA 459
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622827600 818 FGAPPQVPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PRK07764  460 AAPSAQPAPAPAAAPEPTAAPAPAPPAAPAP 490
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
516-564 8.40e-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: 8.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622827600 516 VIRKGWLtisnigiMKGGSK-----GYWFVLTAESLSWYKDDEEKEKKYMLPLD 564
Cdd:cd13273     8 VIKKGYL-------WKKGHLlptwtERWFVLKPNSLSYYKSEDLKEKKGEIALD 54
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
742-836 9.56e-04

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 42.19  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 742 TPAPPPvddswiqhSRRSPPPSPTTQRRPTLSAPLTRPTSgrgPAPAIPSPGPHSGAPPVPF-RPGPLPPfpssSDSFGA 820
Cdd:PHA03201    6 SRSPSP--------PRRPSPPRPTPPRSPDASPEETPPSP---PGPGAEPPPGRAAGPAAPRrRPRGCPA----GVTFSS 70
                          90       100
                  ....*....|....*....|..
gi 1622827600 821 PPqvPSRP------TRAPPSVP 836
Cdd:PHA03201   71 SA--PPRPplglddAPAATPPP 90
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
723-817 1.09e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 42.64  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 723 QALKEALG-------IIGDISTATVSTPAPPPVDDSwIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPH 795
Cdd:PRK14948  496 QAFAKVLGrsiklnlESQSGSASNTAKTPPPPQKSP-PPPAPTPPLPQPTATAPPPTPPPPPPTATQASSNAPAQIPADS 574
                          90       100
                  ....*....|....*....|..
gi 1622827600 796 SGAPPVPFRPGPLPPFPSSSDS 817
Cdd:PRK14948  575 SPPPPIPEEPTPSPTKDSSPEE 596
DUF4639 pfam15479
Domain of unknown function (DUF4639); This family of proteins is found in eukaryotes. Proteins ...
764-837 1.12e-03

Domain of unknown function (DUF4639); This family of proteins is found in eukaryotes. Proteins in this family are typically between 161 and 601 amino acids in length.


Pssm-ID: 464739  Cd Length: 580  Bit Score: 42.49  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 764 PTTQRRPtLSAPLTRPTSGRGPAPAIP-SPGPHSGAPP---------VPFR---PGPLPPFPS-----SSDSFGAPPQVP 825
Cdd:pfam15479 361 PDSEARP-LEAYRGRQRSEKTKARAGPqAPGPGVRVSPaaffplppgVPFRalgPGPGLQFPTlnlglPSPSFGSKLPFP 439
                          90
                  ....*....|....*...
gi 1622827600 826 SR------PTRAPPSVPR 837
Cdd:pfam15479 440 SPglrflaTHPVLPDVAR 457
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
538-618 1.28e-03

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: 39.90  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 538 WFVLTAESLSWYKDDEEKEKKY--MLPLDnlKVRDVEK----SFMSSKHIFALfnteqrnVYKDYrFLELACDSQEDVDS 611
Cdd:cd01238    24 WFVLTKSSLSYYEGDGEKRGKEkgSIDLS--KVRCVEEvkdeAFFERKYPFQV-------VYDDY-TLYVFAPSEEDRDE 93

                  ....*..
gi 1622827600 612 WKASLLR 618
Cdd:cd01238    94 WIAALRK 100
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
725-848 1.30e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  725 LKEALGIIGDISTATVSTPAPPPVDD--------SWIQHSRRSPPPSPTTQrrptlSAPLTRPTSGRGPAPAIPSPGPHS 796
Cdd:PHA03307    10 LIEAAAEGGEFFPRPPATPGDAADDLlsgsqgqlVSDSAELAAVTVVAGAA-----ACDRFEPPTGPPPGPGTEAPANES 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  797 GAPPVPFRPGPLP--------PFPSSSDSFGAPPQVPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PHA03307    85 RSTPTWSLSTLAPasparegsPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSP 144
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
737-848 1.76e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 737 TATVSTPAPPPVddswiqhsRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPsssd 816
Cdd:PRK07003  416 AAAAATRAEAPP--------AAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASD---- 483
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622827600 817 sfgAPPQVPSRPtrAPPSVPRFGAMKDEAAEP 848
Cdd:PRK07003  484 ---APPDAAFEP--APRAAAPSAATPAAVPDA 510
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
516-619 1.79e-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: 38.90  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 516 VIRKGWLTISNiGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVE-KSFMSSKHIFALF----NTEQR 590
Cdd:cd13263     3 PIKSGWLKKQG-SIVKNWQQ-RWFVLRGDQLYYYKDEDDTKPQGTIPLPGNKVKEVPfNPEEPGKFLFEIIpgggGDRMT 80
                          90       100
                  ....*....|....*....|....*....
gi 1622827600 591 NVYKDYRfleLACDSQEDVDSWKASLLRA 619
Cdd:cd13263    81 SNHDSYL---LMANSQAEMEEWVKVIRRV 106
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
759-848 1.79e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.84  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 759 SPPPSPTTQRRPTLSAPLTRPTSGRGP---------APAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRPT 829
Cdd:PLN03209  452 SPSPTAPTGVSPSVSSTSSVPAVPDTApataatdaaAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVK 531
                          90
                  ....*....|....*....
gi 1622827600 830 RAPPSVPRFGAMKDEAAEP 848
Cdd:PLN03209  532 VGNSAPPTALADEQHHAQP 550
PHA02030 PHA02030
hypothetical protein
760-848 1.84e-03

hypothetical protein


Pssm-ID: 222843 [Multi-domain]  Cd Length: 336  Bit Score: 41.50  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 760 PPPSPTTQRRPTLSA-PLTRPTSGRGPAPAIPSPgPHSGAPPVPFRPGpLPPFPsssdsfgAPPQVPSRPTRAPPSVPRF 838
Cdd:PHA02030  254 IIKPKSKAAGSNLPAvPNVAADAGSAAAPAVPAA-AAAVAQAAPSVPQ-VPNVA-------VLPDVPQVAPVAAPAAPEV 324
                          90
                  ....*....|
gi 1622827600 839 GAMKDEAAEP 848
Cdd:PHA02030  325 PAVPVVPAAP 334
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
725-834 2.24e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600  725 LKEALGIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPhsgaPPVPFR 804
Cdd:PHA03307    50 LAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPP----TPPPAS 125
                           90       100       110
                   ....*....|....*....|....*....|
gi 1622827600  805 PGPLPPFPSSSDSFGAPPQVPSRPTRAPPS 834
Cdd:PHA03307   126 PPPSPAPDLSEMLRPVGSPGPPPAASPPAA 155
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
515-619 2.26e-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: 38.51  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 515 QVIRKGWLtisnigiMKGGS-----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQ 589
Cdd:cd13301     2 GIIKEGYL-------VKKGHvvnnwKARWFVLKEDGLEYYKKKTDSSPKGMIPLKGCTITSPCLEYGKRPLVFKLTTAKG 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 1622827600 590 rnvyKDYrFLElACdSQEDVDSWKASLLRA 619
Cdd:cd13301    75 ----QEH-FFQ-AC-SREERDAWAKDITKA 97
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
741-848 2.76e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 741 STPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLT----RPTSGRGPAPAIPSPGPHSGAPPVPF---------RPGP 807
Cdd:PRK07764  628 APAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDggdgWPAKAGGAAPAAPPPAPAPAAPAAPAgaapaqpapAPAA 707
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622827600 808 LPPFPSSSDSFGAPPQVPSRPTRAPPSVPRFGAMKDEAAEP 848
Cdd:PRK07764  708 TPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
736-835 3.28e-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: 40.02  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 736 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPT-SGRGPAPAIPSPGPHSGAP------------PVP 802
Cdd:cd21577    30 SSPPSSSSSSSSSSSSSSSPSSRASPPSPYSKSSPPSPPQQRPLSpPLSLPPPVAPPPLSPGSVPgglpvispvmvqPVP 109
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622827600 803 FR-PGPLPPFPSSSDSFGAPPQVPSRPTRAPPSV 835
Cdd:cd21577   110 VLyPPHLHQPIMVSSSPPPDDDHHHHKASSMKPS 143
Tymo_45kd_70kd pfam03251
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a ...
755-837 3.29e-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: 40.93  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 755 HSRRSPPPSPTTQRRPTLSAPLTRPT---SGRGPAPAIPSPG--------PHS--GAPPVPFRPG--------PLPPFPS 813
Cdd:pfam03251 198 HSSLRPRGSRSRQLQPTVRRPLLAPNqfhSPRQPPPLSDDPGilgprplaPHStrDPPPRPITPGpsnthdlrPLSVLPR 277
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622827600 814 SSDSFG--------------APPQVPSRPTRAPPSVPR 837
Cdd:pfam03251 278 TSPRRGllpnprrhrtstghIPPTTTSRPTGPPSRLQR 315
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
737-837 3.38e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.52  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 737 TATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTrptsgrGPAPAIPSPGPhsGAPPVPFRPGPLPPFPSSSD 816
Cdd:NF040712  228 ATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAA------EPDEATRDAGE--PPAPGAAETPEAAEPPAPAP 299
                          90       100
                  ....*....|....*....|....*.
gi 1622827600 817 SFGAPPQVPS-----RPTRAPPSVPR 837
Cdd:NF040712  300 AAPAAPAAPEaeepaRPEPPPAPKPK 325
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
738-810 3.73e-03

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


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 38.13  E-value: 3.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622827600 738 ATVSTPAPPPVDdswiqhsrrSPPPSPTTQRRPTLSAPlTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPP 810
Cdd:pfam12526  41 PPVGDPRPPVVD---------TPPPVSAVWVLPPPSEP-AAPEPDLVPPVTGPAGPPSPLAPPAPAQKPPLPP 103
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
762-847 4.78e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 40.70  E-value: 4.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 762 PSPTTQRRPTLSAPLTRptsgRGPAPAIPSPgPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPsrPTRAPPSVPRFGAM 841
Cdd:PRK14954  376 NDGGVAPSPAGSPDVKK----KAPEPDLPQP-DRHPGPAKPEAPGARPAELPSPASAPTPEQQP--PVARSAPLPPSPQA 448

                  ....*.
gi 1622827600 842 KDEAAE 847
Cdd:PRK14954  449 SAPRNV 454
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
518-556 4.84e-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: 4.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622827600 518 RKGWLtisnigiMKGGSKG-----YWFVLTAESLSWYKD--DEEKE 556
Cdd:cd13275     1 KKGWL-------MKQGSRQgewskHWFVLRGAALKYYRDpsAEEAG 39
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
737-836 4.85e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 737 TATVSTPAPPPVDDswiQHSRRSPPPSPTTQRR-PTLSAPLTRPTSGRGPAPAIPSPGPhsgAPPVPFRPGPLPPFPSSS 815
Cdd:PRK07764  417 PAAAAAPAPAAAPQ---PAPAPAPAPAPPSPAGnAPAGGAPSPPPAAAPSAQPAPAPAA---APEPTAAPAPAPPAAPAP 490
                          90       100
                  ....*....|....*....|.
gi 1622827600 816 DsfgAPPQVPSRPTRAPPSVP 836
Cdd:PRK07764  491 A---AAPAAPAAPAAPAGADD 508
PH_CNK_mammalian-like cd01260
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
520-619 5.36e-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: 37.39  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 520 GWLTI--SNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSfmSSKHIFALfnteQRNVYKDYR 597
Cdd:cd01260    17 GWLWKkkEAKSFFGQKWKKYWFVLKGSSLYWYSNQQDEKAEGFINLPDFKIERASEC--KKKYAFKA----CHPKIKTFY 90
                          90       100
                  ....*....|....*....|..
gi 1622827600 598 FlelACDSQEDVDSWKASLLRA 619
Cdd:cd01260    91 F---AAENLDDMNKWLSKLNMA 109
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
512-619 6.59e-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: 37.01  E-value: 6.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 512 IGNQVIRKGWLtisnigiMKGGS-----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRdVEKSFMSSKHIFALFn 586
Cdd:cd13255     2 ISEAVLKAGYL-------EKKGErrktwKKRWFVLRPTKLAYYKNDKEYRLLRLIDLTDIHTC-TEVQLKKHDNTFGIV- 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622827600 587 TEQRNVYkdyrfleLACDSQEDVDSWKASLLRA 619
Cdd:cd13255    73 TPARTFY-------VQADSKAEMESWISAINLA 98
PH2_TAPP1_2 cd13271
Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal ...
513-612 7.87e-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: 36.95  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827600 513 GNQVIRKGWLTISNIgIMKGGSKGYwFVLTAESLSWYKDDEEKEKKYMLPL-DNLKVRDVE-KSFMSSKHIFALFnTEQR 590
Cdd:cd13271     5 GRNVIKSGYCVKQGA-VRKNWKRRF-FILDDNTISYYKSETDKEPLRTIPLrEVLKVHECLvKSLLMRDNLFEII-TTSR 81
                          90       100
                  ....*....|....*....|..
gi 1622827600 591 NVYkdyrfleLACDSQEDVDSW 612
Cdd:cd13271    82 TFY-------IQADSPEEMHSW 96
 
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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