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Conserved domains on  [gi|1622827598|ref|XP_028706280|]
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dynamin-3 isoform X7 [Macaca mulatta]

Protein Classification

dynamin( domain architecture ID 11249456)

dynamin such as human dynamin-1, which is involved in clathrin-mediated endocytosis and other vesicular trafficking processes; contains an N-terminal GTPase domain that binds and hydrolyzes GTP, a middle domain involved in self-assembly and oligomerization, and a pleckstrin homology (PH) domain responsible for interactions with the GTPase effector domain (GED)

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 2.13e-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: 2.13e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598   86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  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 1.18e-139

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: 415.38  E-value: 1.18e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1622827598 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
526-635 6.27e-80

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: 252.63  E-value: 6.27e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 526 VIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKD 605
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 1622827598 606 YRFLELACDSQEDVDSWKASLLRAGVYPDK 635
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
655-745 1.98e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.47  E-value: 1.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 655 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1622827598 735 LKEALGIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
754-838 2.82e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 2.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  754 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFG 829
Cdd:PHA03247  2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEP 2638

                   ....*....
gi 1622827598  830 APPQVPSRP 838
Cdd:PHA03247  2639 DPHPPPTVP 2647
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
6-245 2.13e-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: 2.13e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598   86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  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 9.18e-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: 435.91  E-value: 9.18e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRHE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1622827598 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 1.18e-139

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: 415.38  E-value: 1.18e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1622827598 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
526-635 6.27e-80

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: 252.63  E-value: 6.27e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 526 VIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKD 605
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 1622827598 606 YRFLELACDSQEDVDSWKASLLRAGVYPDK 635
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 7.11e-70

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 227.88  E-value: 7.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRHEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirEMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146
                         170       180
                  ....*....|....*....|..
gi 1622827598 186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 1.98e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.47  E-value: 1.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 655 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1622827598 735 LKEALGIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 1.14e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 110.02  E-value: 1.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  654 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80
                           90
                   ....*....|..
gi 1622827598  734 ALKEALGIIGDI 745
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
526-629 1.14e-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: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  526 VIRKGWLTISNIGiMKGGSKGYWFVLTAESLSWYKDDEEKEK---KYMLPLDNLKVRD-VEKSFMSSKHIFALFNTEQRN 601
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKT 79
                           90       100
                   ....*....|....*....|....*...
gi 1622827598  602 VYkdyrfleLACDSQEDVDSWKASLLRA 629
Cdd:smart00233  80 LL-------LQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
526-629 2.46e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 64.12  E-value: 2.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 526 VIRKGWLTISNIGImKGGSKGYWFVLTAESLSWYKDD---EEKEKKYMLPLDNLKVRDVEKSFMSS-KHIFALFNTEQRN 601
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79
                          90       100
                  ....*....|....*....|....*...
gi 1622827598 602 VykdyRFLELACDSQEDVDSWKASLLRA 629
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
754-838 2.82e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 2.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  754 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFG 829
Cdd:PHA03247  2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEP 2638

                   ....*....
gi 1622827598  830 APPQVPSRP 838
Cdd:PHA03247  2639 DPHPPPTVP 2647
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
753-839 1.21e-06

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 50.76  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 753 PAPPPVDDSWiqHSRRSPPPSPTTQ-RRPTLSAPLTRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPSSS 825
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205
                          90       100
                  ....*....|....*....|...
gi 1622827598 826 DSFGAP---P------QVPSRPT 839
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPS 228
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
763-838 4.88e-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: 50.00  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 763 IQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGA----PPQVPSRP 838
Cdd:NF041121   18 AAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPgaalPVRVPAPP 97
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
753-838 2.81e-05

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: 47.20  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 753 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTlsapltrptsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSfgAPP 832
Cdd:NF040983   97 PPPPPPPPTPPPPPPPPPPPPPPSPPPPP-------------PPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPI--QPT 161

                  ....*.
gi 1622827598 833 QVPSRP 838
Cdd:NF040983  162 QLPSIP 167
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
747-838 7.77e-04

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 41.21  E-value: 7.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 747 TATVSTPAPPPVDDSwiqhsrrSPPPSPTTQRRPTLSAPLTRP---TSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPS 823
Cdd:cd21975    43 AKGPGPPGPAWKPDG-------ADSPGLVTAAPHLLAANVLAPlrgPSVEGSSLESGDADMGSDSDVAPASGAAASTSPE 115
                          90
                  ....*....|....*
gi 1622827598 824 SSDSFGAPPQVPSRP 838
Cdd:cd21975   116 SSSDAASSPSPLSLL 130
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
748-838 2.85e-03

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: 41.14  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 748 ATVSTPAPPPVDDSwiQHSRRSPPPSPTTQRRPTLSAPltrptsGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSSDS 827
Cdd:NF041121   20 APPSPEGPAPTAAS--QPATPPPPAAPPSPPGDPPEPP------APEPAPL-PAPYPGSLAPPPPPPPGPAGAAPGAALP 90
                          90
                  ....*....|..
gi 1622827598 828 FGAP-PQVPSRP 838
Cdd:NF041121   91 VRVPaPPALPNP 102
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
6-245 2.13e-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: 2.13e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598   86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  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 9.18e-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: 435.91  E-value: 9.18e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRHE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1622827598 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 1.18e-139

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: 415.38  E-value: 1.18e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1622827598 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
526-635 6.27e-80

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: 252.63  E-value: 6.27e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 526 VIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKD 605
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 1622827598 606 YRFLELACDSQEDVDSWKASLLRAGVYPDK 635
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 7.11e-70

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 227.88  E-value: 7.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRHEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirEMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146
                         170       180
                  ....*....|....*....|..
gi 1622827598 186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 1.98e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.47  E-value: 1.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 655 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1622827598 735 LKEALGIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 1.14e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 110.02  E-value: 1.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  654 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80
                           90
                   ....*....|..
gi 1622827598  734 ALKEALGIIGDI 745
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
526-629 1.14e-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: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  526 VIRKGWLTISNIGiMKGGSKGYWFVLTAESLSWYKDDEEKEK---KYMLPLDNLKVRD-VEKSFMSSKHIFALFNTEQRN 601
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKT 79
                           90       100
                   ....*....|....*....|....*...
gi 1622827598  602 VYkdyrfleLACDSQEDVDSWKASLLRA 629
Cdd:smart00233  80 LL-------LQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
526-629 2.46e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 64.12  E-value: 2.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 526 VIRKGWLTISNIGImKGGSKGYWFVLTAESLSWYKDD---EEKEKKYMLPLDNLKVRDVEKSFMSS-KHIFALFNTEQRN 601
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79
                          90       100
                  ....*....|....*....|....*...
gi 1622827598 602 VykdyRFLELACDSQEDVDSWKASLLRA 629
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
528-626 7.22e-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: 7.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 528 RKGWLTISNIGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKY--MLPLDN-LKVRDVEKSfmSSKHIFALFNTEQRNVYk 604
Cdd:cd00821     1 KEGYLLKRGGGGLKSWKK-RWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76
                          90       100
                  ....*....|....*....|..
gi 1622827598 605 dyrfleLACDSQEDVDSWKASL 626
Cdd:cd00821    77 ------LQADSEEERQEWLKAL 92
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
526-629 1.08e-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: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 526 VIRKGWLTisnigiMKGGS----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSfmSSKHIFALFNTEQRN 601
Cdd:cd01252     3 PDREGWLL------KLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVEDK--KKPFCFELYSPSNGQ 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622827598 602 VYKD----------------YRfleLACDSQEDVDSWKASLLRA 629
Cdd:cd01252    75 VIKAcktdsdgkvvegnhtvYR---ISAASEEERDEWIKSIKAS 115
PHA03247 PHA03247
large tegument protein UL36; Provisional
754-838 2.82e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 2.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  754 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFG 829
Cdd:PHA03247  2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEP 2638

                   ....*....
gi 1622827598  830 APPQVPSRP 838
Cdd:PHA03247  2639 DPHPPPTVP 2647
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
526-629 1.15e-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: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 526 VIRKGWLTisnigimKGGSKGY------WFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSF-MSSKHIFALFNTE 598
Cdd:cd13248     7 VVMSGWLH-------KQGGSGLknwrkrWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHAN 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622827598 599 QRNVYkdyrfleLACDSQEDVDSWKASLLRA 629
Cdd:cd13248    80 MRTYY-------FAADTAEEMEQWMNAMSLA 103
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
753-839 1.21e-06

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 50.76  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 753 PAPPPVDDSWiqHSRRSPPPSPTTQ-RRPTLSAPLTRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPSSS 825
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205
                          90       100
                  ....*....|....*....|...
gi 1622827598 826 DSFGAP---P------QVPSRPT 839
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPS 228
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
748-838 1.89e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.71  E-value: 1.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  748 ATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRP------TSGRGPAPAIPSPGPHSGAPpvpfrPGPLPPF 821
Cdd:PHA03307   119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAavasdaASSRQAALPLSSPEETARAP-----SSPPAEP 193
                           90
                   ....*....|....*....
gi 1622827598  822 PSSSDSFGAP--PQVPSRP 838
Cdd:PHA03307   194 PPSTPPAAASprPPRRSSP 212
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
548-622 2.00e-06

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270110  Cd Length: 106  Bit Score: 47.24  E-value: 2.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622827598 548 WFVLTAESLSWYKDDEEKEKKYMLPLDNL----KVRDVEKsfmssKHIFALFNTEqrnvyKDYRFlelACDSQEDVDSW 622
Cdd:cd13298    26 WVVLRPCQLSYYKDEKEYKLRRVINLSELlavaPLKDKKR-----KNVFGIYTPS-----KNLHF---RATSEKDANEW 91
PHA03247 PHA03247
large tegument protein UL36; Provisional
752-839 2.26e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  752 TPaPPPVDD--SWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSG------RGPAPA-IPSPGPHSGAPPVPFRP-GPLPPF 821
Cdd:PHA03247   360 TP-PSSLEDlsAGRHHPKRASLPTRKRRSARHAATPFARGPGGddqtrpAAPVPAsVPTPAPTPVPASAPPPPaTPLPSA 438
                           90
                   ....*....|....*...
gi 1622827598  822 PSSSDSFGAPPQVPSRPT 839
Cdd:PHA03247   439 EPGSDDGPAPPPERQPPA 456
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
746-831 3.80e-06

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: 49.21  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 746 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPT-LSAPltrPTSGRGPAPAIPSPGphsgaPPVPFrPGPLPPFPSS 824
Cdd:pfam15822  52 STAPSTVPFGPAPTGMYPSIPLTGPSPGPPAPFPPSgPSCP---PPGGPYPAPTVPGPG-----PIGPY-PTPNMPFPEL 122

                  ....*..
gi 1622827598 825 SDSFGAP 831
Cdd:pfam15822 123 PRPYGAP 129
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
763-838 4.88e-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: 50.00  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 763 IQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGA----PPQVPSRP 838
Cdd:NF041121   18 AAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPgaalPVRVPAPP 97
PHA02682 PHA02682
ORF080 virion core protein; Provisional
748-838 5.18e-06

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 49.09  E-value: 5.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 748 ATVSTPAPP--------PVDDSWIQHSRR---SPPPSPTT-QRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFrP 815
Cdd:PHA02682   32 ATIPAPAAPcppdadvdPLDKYSVKEAGRyyqSRLKANSAcMQRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVTC-P 110
                          90       100
                  ....*....|....*....|....*.
gi 1622827598 816 GPLPPFPSSSDSFGAPPQV---PSRP 838
Cdd:PHA02682  111 APAPACPPATAPTCPPPAVcpaPARP 136
PHA03247 PHA03247
large tegument protein UL36; Provisional
743-839 6.72e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 6.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  743 GDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSG---RGPAPAIPSPGPHSGAPPVPFRPGPLP 819
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpprRLTRPAVASLSESRESLPSPWDPADPP 2808
                           90       100
                   ....*....|....*....|...
gi 1622827598  820 ---PFPSSSDSFGAPPQVPSRPT 839
Cdd:PHA03247  2809 aavLAPAAALPPAASPAGPLPPP 2831
PHA03247 PHA03247
large tegument protein UL36; Provisional
754-838 7.13e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 7.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  754 APPPVDDswIQHSRRSPPPSPTTQRRPTLSAPLTR----PTSGRGPAPA-----IPSPGPHSGAPPVPFRPGPLPPFPSS 824
Cdd:PHA03247  2688 ARPTVGS--LTSLADPPPPPPTPEPAPHALVSATPlppgPAAARQASPAlpaapAPPAVPAGPATPGGPARPARPPTTAG 2765
                           90
                   ....*....|....
gi 1622827598  825 SDSfGAPPQVPSRP 838
Cdd:PHA03247  2766 PPA-PAPPAAPAAG 2778
PHA03247 PHA03247
large tegument protein UL36; Provisional
745-839 1.75e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  745 ISTATVSTPAPPPVddswiQHSRRSPPPSPTTQRRPTLSAPLTR----PTSGRGPAPAIPSPGPHSGAPPVPFRPGP--- 817
Cdd:PHA03247  2891 VSRSTESFALPPDQ-----PERPPQPQAPPPPQPQPQPPPPPQPqpppPPPPRPQPPLAPTTDPAGAGEPSGAVPQPwlg 2965
                           90       100
                   ....*....|....*....|...
gi 1622827598  818 -LPPFPSSSDSFGAPPQVPSRPT 839
Cdd:PHA03247  2966 aLVPGRVAVPRFRVPQPAPSREA 2988
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
753-838 2.81e-05

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: 47.20  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 753 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTlsapltrptsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSfgAPP 832
Cdd:NF040983   97 PPPPPPPPTPPPPPPPPPPPPPPSPPPPP-------------PPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPI--QPT 161

                  ....*.
gi 1622827598 833 QVPSRP 838
Cdd:NF040983  162 QLPSIP 167
PHA03247 PHA03247
large tegument protein UL36; Provisional
747-838 2.87e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  747 TATVSTPAPPPVDDSWIQHS-------------RRSPPP-----SPTTQRRPTLSApLTRPTSGRGPAP-AIPSPGPHS- 806
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSlplggsvapggdvRRRPPSrspaaKPAAPARPPVRR-LARPAVSRSTESfALPPDQPERp 2908
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622827598  807 GAPPVPFRPGPLPPFPSSSDSFGAPPQvPSRP 838
Cdd:PHA03247  2909 PQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRP 2939
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
526-628 3.89e-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: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 526 VIRKGWLTiSNIGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMS-SKHIFALF---NTEQRN 601
Cdd:cd13378     3 VLKAGWLK-KQRSIMKNWQQ-RWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNELPPNPEEpGKHLFEILpggAGDREK 80
                          90       100
                  ....*....|....*....|....*..
gi 1622827598 602 VYKDYRFLELACDSQEDVDSWKASLLR 628
Cdd:cd13378    81 VPMNHEAFLLMANSQSDMEDWVKAIRR 107
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
715-838 5.83e-05

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: 46.07  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 715 MEESAEQAQRRDemlRMYQALkeALGIIGDISTATVSTPApppvddswIQHSRRSP-PPSPTTQRRPTLSAPLTRPTSGR 793
Cdd:pfam07174   1 MDQVDPNSTRRK---GLWATL--AIAAVAGASAVAVALPA--------VAHADPEPaPPPPSTATAPPAPPPPPPAPAAP 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622827598 794 GPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRP 838
Cdd:pfam07174  68 APPPP-PAAPNAPNAPPPPADPNAPPPPPADPNAPPPPAVDPNAP 111
PHA03264 PHA03264
envelope glycoprotein D; Provisional
751-838 7.09e-05

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 46.15  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 751 STP-APPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPF--PSSSDS 827
Cdd:PHA03264  261 SKGyEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDAdrPEGWPS 340
                          90
                  ....*....|....
gi 1622827598 828 FGA---PPQVPSRP 838
Cdd:PHA03264  341 LEAitfPPPTPATP 354
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
707-839 8.21e-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: 46.30  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 707 SSEDQNTLMEESAEQAQRRDEMLrmyqALKEALGII-----GDISTATVSTPAPPPVDDSwiQHSRRSPPPSPTTQRRPT 781
Cdd:pfam03154 150 SPQDNESDSDSSAQQQILQTQPP----VLQAQSGAAsppspPPPGTTQAATAGPTPSAPS--VPPQGSPATSQPPNQTQS 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 782 LSAPLTRPTSG------RGPAP-------------------AIPSPGPHSGAPPVPFR--------PGPLPPFPSSSDSF 828
Cdd:pfam03154 224 TAAPHTLIQQTptlhpqRLPSPhpplqpmtqppppsqvspqPLPQPSLHGQMPPMPHSlqtgpshmQHPVPPQPFPLTPQ 303
                         170
                  ....*....|.
gi 1622827598 829 GAPPQVPSRPT 839
Cdd:pfam03154 304 SSQSQVPPGPS 314
PH2_PH_fungal cd13299
Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal ...
545-626 9.63e-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: 9.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 545 KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLkVRDVEKSFMSSKHIFAL-FNTEQrnvyKDYRFlelACDSQEDVDSWK 623
Cdd:cd13299    24 KKYWLVLRNRSLSFYKDQSEYSPVKIIPIDDI-IDVVELDPLSKSKKWCLqIITPE----KRIRF---CADDEESLIKWL 95

                  ...
gi 1622827598 624 ASL 626
Cdd:cd13299    96 GAL 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
755-838 1.25e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  755 PPPVDDSWIQHSRRSPPPSPTTQRRPTL-SAPLTRPTSGRGPAPAI--------PSPGPHSGAPPVPFRPG-PLPPFPSS 824
Cdd:PHA03247  2648 PPERPRDDPAPGRVSRPRRARRLGRAAQaSSPPQRPRRRAARPTVGsltsladpPPPPPTPEPAPHALVSAtPLPPGPAA 2727
                           90
                   ....*....|....*
gi 1622827598  825 S-DSFGAPPQVPSRP 838
Cdd:PHA03247  2728 ArQASPALPAAPAPP 2742
PHA03378 PHA03378
EBNA-3B; Provisional
752-838 1.53e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 752 TPAPPPVddswIQHSRRSPPPSPTTQRRPTLSAP--LTRPTSGRGPAPAiPSPGPHSGAPPVPfRPGPLPPfPSSSDSFG 829
Cdd:PHA03378  702 TPMRPPA----APPGRAQRPAAATGRARPPAAAPgrARPPAAAPGRARP-PAAAPGRARPPAA-APGRARP-PAAAPGAP 774
                          90
                  ....*....|..
gi 1622827598 830 AP---PQVPSRP 838
Cdd:PHA03378  775 TPqppPQAPPAP 786
PH_Boi cd13316
Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally ...
529-629 1.92e-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: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 529 KGWLTisnigiMKGGSKGYW----FVLTAESLSWYKDDEEKEKKYMLPLDNLKV-RDVEKSFMSSKHIFALFNTEQRNVY 603
Cdd:cd13316     3 SGWMK------KRGERYGTWktryFVLKGTRLYYLKSENDDKEKGLIDLTGHRVvPDDSNSPFRGSYGFKLVPPAVPKVH 76
                          90       100
                  ....*....|....*....|....*.
gi 1622827598 604 kdYrfleLACDSQEDVDSWKASLLRA 629
Cdd:cd13316    77 --Y----FAVDEKEELREWMKALMKA 96
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
745-839 2.11e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.91  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 745 ISTATVSTPAPPPVDDSwiqHSRRSPPPSP----TTQRRPTLSAP---LTRPT-SGRGPAPAIPSPGPHSGAP------- 809
Cdd:pfam05109 468 VSTADVTSPTPAGTTSG---ASPVTPSPSPrdngTESKAPDMTSPtsaVTTPTpNATSPTPAVTTPTPNATSPtlgktsp 544
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622827598 810 ------PVPFRPGPLPPFPSSSDSFGAPPQVPSRPT 839
Cdd:pfam05109 545 tsavttPTPNATSPTPAVTTPTPNATIPTLGKTSPT 580
PHA03247 PHA03247
large tegument protein UL36; Provisional
746-838 2.52e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  746 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTS-GRGPAPAIPSPGPHSGA-----PPVPFRPGPLP 819
Cdd:PHA03247  2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSeSRESLPSPWDPADPPAAvlapaAALPPAASPAG 2826
                           90
                   ....*....|....*....
gi 1622827598  820 PFPSSSDSFGAPPQVPSRP 838
Cdd:PHA03247  2827 PLPPPTSAQPTAPPPPPGP 2845
PHA03321 PHA03321
tegument protein VP11/12; Provisional
745-837 2.92e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 44.56  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 745 ISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAI-------PSPGPHSGAP-------P 810
Cdd:PHA03321  404 LATELFRTGVPSEHYEASLRLLSSRQPPGAPAPRRDNDPPPPPRARPGSTPACARraraqraRDAGPEYVDPlgalrrlP 483
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622827598 811 VPFRPGPLPPFPSSSDSF-----GAPPQVPSR 837
Cdd:PHA03321  484 AGAAPPPEPAAAPSPATYytrmgGGPPRLPPR 515
PHA03377 PHA03377
EBNA-3C; Provisional
749-838 2.92e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 44.66  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  749 TVSTPAPP---PVDD---SWIQHSRRSPPP-SPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSGAPPV-------PFR 814
Cdd:PHA03377   525 SVTQPAKPhrkVQDGfqrSGRRQKRATPPKvSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPStgprqqaKCK 604
                           90       100
                   ....*....|....*....|....
gi 1622827598  815 PGPlppfPSSSDSFGAPPQvpSRP 838
Cdd:PHA03377   605 DGP----PASGPHEKQPPS--SAP 622
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
740-839 3.28e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 740 GIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTlSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLP 819
Cdd:PRK07764  661 DASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA-PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPV 739
                          90       100
                  ....*....|....*....|
gi 1622827598 820 PFPSSSDSFGAPPQVPSRPT 839
Cdd:PRK07764  740 PLPPEPDDPPDPAGAPAQPP 759
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
749-839 3.58e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 44.03  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 749 TVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPtsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSF 828
Cdd:PRK14950  358 ALLVPVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIP-----PKEPVRETATPPPVPPRPVAPPVPHTPESAPKLT 432
                          90
                  ....*....|.
gi 1622827598 829 GAPPQVPSRPT 839
Cdd:PRK14950  433 RAAIPVDEKPK 443
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
746-839 3.66e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 746 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPtlsAPLTRPTSGRGPAPAIPSPGP-HSGAPPVPFRPGPLPPFPSS 824
Cdd:PRK07764  401 AAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAP---APAPAPPSPAGNAPAGGAPSPpPAAAPSAQPAPAPAAAPEPT 477
                          90
                  ....*....|....*
gi 1622827598 825 SDSFGAPPQVPSRPT 839
Cdd:PRK07764  478 AAPAPAPPAAPAPAA 492
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
526-576 3.79e-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: 41.27  E-value: 3.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622827598 526 VIRKGWLTISNIGIMKGGS---KGYWFVLTAESLSWYKD-DEEKEKKYMLPLDNL 576
Cdd:cd13297    13 VIERGWLYKEGGKGGARGNltkKKRWFVLTGNSLDYYKSsEKNSLKLGTLVLNSL 67
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
519-626 4.63e-04

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


Pssm-ID: 275402  Cd Length: 116  Bit Score: 40.68  E-value: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 519 LPPSRQIVIRKGWLTisnigiMKGGSKG----YWFVLTAESLSWYKDDEEkekKYmLPLDNLKVRDV-----EKSFMSSK 589
Cdd:cd13215    14 LPKRSGAVIKSGYLS------KRSKRTLrytrYWFVLKGDTLSWYNSSTD---LY-FPAGTIDLRYAtsielSKSNGEAT 83
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622827598 590 HIFALFNTEQRnvykdYRFLelaCDSQEDVDSWKASL 626
Cdd:cd13215    84 TSFKIVTNSRT-----YKFK---ADSETSADEWVKAL 112
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
747-838 5.69e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.55  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 747 TATVSTPAPPPVddswiQHSRRSPPPSPTTQRRPTlSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSD 826
Cdd:PRK14951  385 EAAAPAAAPVAQ-----AAAAPAPAAAPAAAASAP-AAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPE 458
                          90
                  ....*....|..
gi 1622827598 827 SFGAPPQVPSRP 838
Cdd:PRK14951  459 TVAIPVRVAPEP 470
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
767-837 5.72e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 43.58  E-value: 5.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622827598 767 RRSPPPSPTTQRRPTlSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSF-GAPPQVPSR 837
Cdd:PRK14965  379 RGAPAPPSAAWGAPT-PAAPAAPPPAAAPPVPPAAPARPAAARPAPAPAPPAAAAPPARSADpAAAASAGDR 449
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
747-838 7.77e-04

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 41.21  E-value: 7.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 747 TATVSTPAPPPVDDSwiqhsrrSPPPSPTTQRRPTLSAPLTRP---TSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPS 823
Cdd:cd21975    43 AKGPGPPGPAWKPDG-------ADSPGLVTAAPHLLAANVLAPlrgPSVEGSSLESGDADMGSDSDVAPASGAAASTSPE 115
                          90
                  ....*....|....*
gi 1622827598 824 SSDSFGAPPQVPSRP 838
Cdd:cd21975   116 SSSDAASSPSPLSLL 130
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
752-838 8.13e-04

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 42.57  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 752 TPAPPPvddswiqhSRRSPPPSPTTQRRPTLSAPLTRPTSgrgPAPAIPSPGPHSGAPPVPF-RPGPLPPfpssSDSFGA 830
Cdd:PHA03201    6 SRSPSP--------PRRPSPPRPTPPRSPDASPEETPPSP---PGPGAEPPPGRAAGPAAPRrRPRGCPA----GVTFSS 70

                  ....*...
gi 1622827598 831 PPqvPSRP 838
Cdd:PHA03201   71 SA--PPRP 76
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
526-574 8.51e-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: 8.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622827598 526 VIRKGWLtisnigiMKGGSK-----GYWFVLTAESLSWYKDDEEKEKKYMLPLD 574
Cdd:cd13273     8 VIKKGYL-------WKKGHLlptwtERWFVLKPNSLSYYKSEDLKEKKGEIALD 54
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
753-838 8.70e-04

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: 40.62  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 753 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPApaIPSPGPHSGAPPVPfrpgPLPPFPSSSdSFGAPP 832
Cdd:pfam06346   1 PPPPPLPGDSSTIPLPPGACIPTPPPLPGGGGPPPPPPLPGSAA--IPPPPPLPGGTSIP----PPPPLPGAA-SIPPPP 73

                  ....*.
gi 1622827598 833 QVPSRP 838
Cdd:pfam06346  74 PLPGST 79
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
745-852 9.24e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  745 ISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRR------PTLSAPLTRPTSGRGPAPAIPSPGP---------HSGAP 809
Cdd:PHA03307   195 PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAAddagasSSDSSSSESSGCGWGPENECPLPRPapitlptriWEASG 274
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1622827598  810 PVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRAPPSVPRRPPPA 852
Cdd:PHA03307   275 WNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSS 317
PHA03378 PHA03378
EBNA-3B; Provisional
755-838 9.33e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 755 PPPVDDSWIQHSRRSPPPSPT---TQRRPTlSAPLTRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPfPSSSDSFGAP 831
Cdd:PHA03378  659 ITPYKPTWTQIGHIPYQPSPTganTMLPIQ-WAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARP-PAAAPGRARP 736
                          90
                  ....*....|
gi 1622827598 832 PQV---PSRP 838
Cdd:PHA03378  737 PAAapgRARP 746
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
733-827 1.13e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 42.64  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 733 QALKEALG-------IIGDISTATVSTPAPPPVDDSwIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPH 805
Cdd:PRK14948  496 QAFAKVLGrsiklnlESQSGSASNTAKTPPPPQKSP-PPPAPTPPLPQPTATAPPPTPPPPPPTATQASSNAPAQIPADS 574
                          90       100
                  ....*....|....*....|..
gi 1622827598 806 SGAPPVPFRPGPLPPFPSSSDS 827
Cdd:PRK14948  575 SPPPPIPEEPTPSPTKDSSPEE 596
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
548-628 1.30e-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: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 548 WFVLTAESLSWYKDDEEKEKKY--MLPLDnlKVRDVEK----SFMSSKHIFALfnteqrnVYKDYrFLELACDSQEDVDS 621
Cdd:cd01238    24 WFVLTKSSLSYYEGDGEKRGKEkgSIDLS--KVRCVEEvkdeAFFERKYPFQV-------VYDDY-TLYVFAPSEEDRDE 93

                  ....*..
gi 1622827598 622 WKASLLR 628
Cdd:cd01238    94 WIAALRK 100
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
753-834 1.68e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 753 PAPPPVDDSWIQHSRRSPPPSPTT------QRRPTLSAPLTRPTSGR----GPAPAIPSPGPHSGAPPVPfrpgPLPPFP 822
Cdd:pfam03154 292 PVPPQPFPLTPQSSQSQVPPGPSPaapgqsQQRIHTPPSQSQLQSQQppreQPLPPAPLSMPHIKPPPTT----PIPQLP 367
                          90
                  ....*....|..
gi 1622827598 823 SSSdSFGAPPQV 834
Cdd:pfam03154 368 NPQ-SHKHPPHL 378
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
770-838 1.71e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.97  E-value: 1.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622827598 770 PPPSpttQRRPTLSAPLTRPTSGRG----PAPA-IPSPG-PHSGAPPVPFRPGpLPPFPSSSdsFGAPPQVPSRP 838
Cdd:PRK14959  398 PTPG---TQGPQGTAPAAGMTPSSAapatPAPSaAPSPRvPWDDAPPAPPRSG-IPPRPAPR--MPEASPVPGAP 466
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
524-629 1.75e-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: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 524 QIVIRKGWLTISNiGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVE-KSFMSSKHIFALF----NTE 598
Cdd:cd13263     1 ERPIKSGWLKKQG-SIVKNWQQ-RWFVLRGDQLYYYKDEDDTKPQGTIPLPGNKVKEVPfNPEEPGKFLFEIIpgggGDR 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622827598 599 QRNVYKDYRfleLACDSQEDVDSWKASLLRA 629
Cdd:cd13263    79 MTSNHDSYL---LMANSQAEMEEWVKVIRRV 106
PHA03247 PHA03247
large tegument protein UL36; Provisional
746-836 1.90e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  746 STATVSTPAPPPVDdswiqhSRRSPPPSPTTQRRPTLS-----AP----LTRPTSGrgPAPAIPSPGPHsgaPPVpfRPG 816
Cdd:PHA03247  2820 PAASPAGPLPPPTS------AQPTAPPPPPGPPPPSLPlggsvAPggdvRRRPPSR--SPAAKPAAPAR---PPV--RRL 2886
                           90       100
                   ....*....|....*....|
gi 1622827598  817 PLPPFPSSSDSFGAPPQVPS 836
Cdd:PHA03247  2887 ARPAVSRSTESFALPPDQPE 2906
PHA03247 PHA03247
large tegument protein UL36; Provisional
734-838 1.92e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  734 ALKEALGIIGDISTATVSTPAPPPVDDSWI---------QHSRRSPPPSPTTQ-RRPTLSAPLTRPTSGRGPAPAIPSpG 803
Cdd:PHA03247  2687 AARPTVGSLTSLADPPPPPPTPEPAPHALVsatplppgpAAARQASPALPAAPaPPAVPAGPATPGGPARPARPPTTA-G 2765
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622827598  804 PHSGAPPV-----PFRPGPLPPFPSSSDSFGAPPQvPSRP 838
Cdd:PHA03247  2766 PPAPAPPAapaagPPRRLTRPAVASLSESRESLPS-PWDP 2804
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
738-836 2.15e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 738 ALGIIGDISTATVSTPAPPPVddSWIQHSRRSPPPS---PTTQRRPTLSAPLTR--PTSGRGPAPAIPSPGPHSGAPPVP 812
Cdd:pfam03154 395 ALKPLSSLSTHHPPSAHPPPL--QLMPQSQQLPPPPaqpPVLTQSQSLPPPAAShpPTSGLHQVPSQSPFPQHPFVPGGP 472
                          90       100
                  ....*....|....*....|....*.
gi 1622827598 813 frPGPLPPF--PSSSDSFGAPPQVPS 836
Cdd:pfam03154 473 --PPITPPSgpPTSTSSAMPGIQPPS 496
PH2_TAPP1_2 cd13271
Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal ...
520-622 2.25e-03

Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal repeat; The binding of TAPP1 (also called PLEKHA1/pleckstrin homology domain containing, family A (phosphoinositide binding specific) member 1) and TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP1 and TAPP2 contain two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270090  Cd Length: 114  Bit Score: 38.49  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 520 PPSRQIVIRKGWLTISNIgIMKGGSKGYwFVLTAESLSWYKDDEEKEKKYMLPL-DNLKVRDVE-KSFMSSKHIFALFnT 597
Cdd:cd13271     2 QRAGRNVIKSGYCVKQGA-VRKNWKRRF-FILDDNTISYYKSETDKEPLRTIPLrEVLKVHECLvKSLLMRDNLFEII-T 78
                          90       100
                  ....*....|....*....|....*
gi 1622827598 598 EQRNVYkdyrfleLACDSQEDVDSW 622
Cdd:cd13271    79 TSRTFY-------IQADSPEEMHSW 96
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
751-838 2.32e-03

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


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 40.95  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 751 STPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPG--PHSGAPPVPFRPGPLPPFPSSSDS- 827
Cdd:pfam15279 136 LPPPPLPPKKGRRHRPGLHPPLGRPPGSPPMSMTPRGLLGKPQQHPPPSPLPAfmEPSSMPPPFLRPPPSIPQPNSPLSn 215
                          90
                  ....*....|....*
gi 1622827598 828 ----FGAPPQVPSRP 838
Cdd:pfam15279 216 pmlpGIGPPPKPPRN 230
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
746-837 2.48e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 746 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRptlSAPLTRPTSGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSS 825
Cdd:PRK12323  404 AAPAAAPAAAAAARAVAAAPARRSPAPEALAAAR---QASARGPGGAPAPAPA-PAAAPAAAARPAAAGPRPVAAAAAAA 479
                          90
                  ....*....|..
gi 1622827598 826 DSFGAPPQVPSR 837
Cdd:PRK12323  480 PARAAPAAAPAP 491
PHA03247 PHA03247
large tegument protein UL36; Provisional
746-839 2.73e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  746 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAP-----LTRPTSGRGPA------PAIPSPGPHSG---APPV 811
Cdd:PHA03247  2762 TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdpadPPAAVLAPAAAlppaasPAGPLPPPTSAqptAPPP 2841
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622827598  812 PfrPGPLPPFPSSSDSF------------GAPPQVPSRPT 839
Cdd:PHA03247  2842 P--PGPPPPSLPLGGSVapggdvrrrppsRSPAAKPAAPA 2879
PHA03379 PHA03379
EBNA-3A; Provisional
746-835 2.75e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.58  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 746 STATVSTPAPPPVDDSWIQ--HSRRSPPPSPTTQRRPTLSAPLTR-------PTSGRG---PAPAI---------PSPGP 804
Cdd:PHA03379  436 SHGSAQVPEPPPVHDLEPGplHDQHSMAPCPVAQLPPGPLQDLEPgdqlpgvVQDGRPacaPVPAPagpivrpweASLSQ 515
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622827598 805 HSGAPPVPFRPGPLP----PFPSSSDSFGAPPQVP 835
Cdd:PHA03379  516 VPGVAFAPVMPQPMPvepvPVPTVALERPVCPAPP 550
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
747-839 2.83e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 747 TATVSTPAPPPVDDswiQHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAiPSPGPHSGAPPVPfRPGPLPPFPSSSD 826
Cdd:PRK07764  417 PAAAAAPAPAAAPQ---PAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ-PAPAPAAAPEPTA-APAPAPPAAPAPA 491
                          90
                  ....*....|...
gi 1622827598 827 sfgAPPQVPSRPT 839
Cdd:PRK07764  492 ---AAPAAPAAPA 501
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
748-838 2.85e-03

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: 41.14  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 748 ATVSTPAPPPVDDSwiQHSRRSPPPSPTTQRRPTLSAPltrptsGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSSDS 827
Cdd:NF041121   20 APPSPEGPAPTAAS--QPATPPPPAAPPSPPGDPPEPP------APEPAPL-PAPYPGSLAPPPPPPPGPAGAAPGAALP 90
                          90
                  ....*....|..
gi 1622827598 828 FGAP-PQVPSRP 838
Cdd:NF041121   91 VRVPaPPALPNP 102
TYA pfam01021
Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a ...
751-836 3.43e-03

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


Pssm-ID: 425992  Cd Length: 384  Bit Score: 40.71  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 751 STPAPPPVDDSwiqHSRRSPPP--SPTTQRRPTLSAPLTRP----TSGRgPAPAIPS--PGPHSGAPPVPFRPGPLPPFP 822
Cdd:pfam01021  40 TTPGSSAVPEN---HHHASPQPasVPPPQNGPYSQQCMMTPnqanPSGW-PFYGHPSmmPYTPYQMSPMYFPPGPQSQFP 115
                          90
                  ....*....|....
gi 1622827598 823 SSSDSFGAPPQVPS 836
Cdd:pfam01021 116 QYPSSVGTPLSTPS 129
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
722-836 3.84e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 722 AQRRDEMLRmyQALKEALGIigdisTATVS-TPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLS-APLTRPTSGRGPAPAI 799
Cdd:PRK07764  563 SPGNAEVLV--TALAEELGG-----DWQVEaVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPaAPAAPAAPAPAGAAAA 635
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622827598 800 PSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPS 836
Cdd:PRK07764  636 PAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAK 672
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
526-629 4.31e-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: 37.74  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 526 VIRKGWLtisnigiMKGGS-----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQr 600
Cdd:cd13301     3 IIKEGYL-------VKKGHvvnnwKARWFVLKEDGLEYYKKKTDSSPKGMIPLKGCTITSPCLEYGKRPLVFKLTTAKG- 74
                          90       100
                  ....*....|....*....|....*....
gi 1622827598 601 nvyKDYrFLElACdSQEDVDSWKASLLRA 629
Cdd:cd13301    75 ---QEH-FFQ-AC-SREERDAWAKDITKA 97
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
528-566 4.90e-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: 4.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622827598 528 RKGWLtisnigiMKGGSKG-----YWFVLTAESLSWYKD--DEEKE 566
Cdd:cd13275     1 KKGWL-------MKQGSRQgewskHWFVLRGAALKYYRDpsAEEAG 39
DUF4639 pfam15479
Domain of unknown function (DUF4639); This family of proteins is found in eukaryotes. Proteins ...
774-839 5.04e-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: 40.56  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 774 PTTQRRPtLSAPLTRPTSGRGPAPAIP-SPGPHSGAPP---------VPFR---PGPLPPFPS-----SSDSFG------ 829
Cdd:pfam15479 361 PDSEARP-LEAYRGRQRSEKTKARAGPqAPGPGVRVSPaaffplppgVPFRalgPGPGLQFPTlnlglPSPSFGsklpfp 439
                          90       100
                  ....*....|....*....|.
gi 1622827598 830 -----------APPQVPSRPT 839
Cdd:pfam15479 440 spglrflathpVLPDVARSPS 460
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
770-836 5.17e-03

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


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 37.01  E-value: 5.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 770 PPPSPTT-QRRPTLS--APLTRPTSGRGPAPAIPSPGphSGAPPVPfrpgplppfPSSSdsFGAPPQVPS 836
Cdd:pfam16058   1 PSSSITEpPRDPSGSygEPPRAPSSSYTEPQRDPSSS--ITEPPAD---------PSSS--YTEPPRDPS 57
PH_CNK_mammalian-like cd01260
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
530-629 5.42e-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: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 530 GWLTI--SNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSfmSSKHIFALfnteQRNVYKDYR 607
Cdd:cd01260    17 GWLWKkkEAKSFFGQKWKKYWFVLKGSSLYWYSNQQDEKAEGFINLPDFKIERASEC--KKKYAFKA----CHPKIKTFY 90
                          90       100
                  ....*....|....*....|..
gi 1622827598 608 FlelACDSQEDVDSWKASLLRA 629
Cdd:cd01260    91 F---AAENLDDMNKWLSKLNMA 109
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
746-838 5.64e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 746 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSG-----RGPAPAIPSPGPHSGAPPVPfRPGPLPP 820
Cdd:PRK07764  642 APAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAapaapAGAAPAQPAPAPAATPPAGQ-ADDPAAQ 720
                          90
                  ....*....|....*...
gi 1622827598 821 FPSSSDSFGAPPQVPSRP 838
Cdd:PRK07764  721 PPQAAQGASAPSPAADDP 738
PHA03377 PHA03377
EBNA-3C; Provisional
762-838 6.44e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.42  E-value: 6.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  762 WIQHSRRSPPPSPTTQRRPTLSaPLTRPTSGrgPAPAIPSPGPHSGAPPVPFRP----GPLPPFPSSSDSFGAP------ 831
Cdd:PHA03377   813 WSQYPGHGHPQGPWAPRPPHLP-PQWDGSAG--HGQDQVSQFPHLQSETGPPRLqlsqVPQLPYSQTLVSSSAPswsspq 889

                   ....*..
gi 1622827598  832 PQVPSRP 838
Cdd:PHA03377   890 PRAPIRP 896
SSDP pfam04503
Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA ...
728-827 7.94e-03

Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA binding proteins with specificity to a pyrimidine-rich element found in the promoter region of the alpha2(I) collagen gene.


Pssm-ID: 461334 [Multi-domain]  Cd Length: 293  Bit Score: 39.17  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 728 MLRMYQALKEALGIIGdISTATVSTPAPPPvddswiqHSRRSPPPSPTTQRRPTLSAPLTRPTSGRGPAPAIPSPGPHSG 807
Cdd:pfam04503 128 MQRMNPPRGPGMGPMG-PQSYGPGMRGPPP-------NSTDGPGGMPPMNMGPGGRRPWPQPNASNPLPYSSSSPGSYGG 199
                          90       100
                  ....*....|....*....|
gi 1622827598 808 APPVPFRPGPLPPFPSSSDS 827
Cdd:pfam04503 200 PPGGGGPPGPTPIMPSPQDS 219
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
743-839 9.35e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.77  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598  743 GDISTATV-STPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLTRPTSG-----RGPAPAIPSPGPHSGAPPVPFRPG 816
Cdd:PHA03307    48 AELAAVTVvAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPAspareGSPTPPGPSSPDPPPPTPPPASPP 127
                           90       100
                   ....*....|....*....|...
gi 1622827598  817 PLPPFPSSSDSFGAPPQVPSRPT 839
Cdd:PHA03307   128 PSPAPDLSEMLRPVGSPGPPPAA 150
PHA03378 PHA03378
EBNA-3B; Provisional
746-839 9.73e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622827598 746 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRR-PTLSAPLtrptsgRGPAPAIPSPGPHSGAPPVPFRP--GPLPPFP 822
Cdd:PHA03378  581 TTSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHiPETSAPR------QWPMPLRPIPMRPLRMQPITFNVlvFPTPHQP 654
                          90       100
                  ....*....|....*....|...
gi 1622827598 823 SSSD------SFGAPPQVPSRPT 839
Cdd:PHA03378  655 PQVEitpykpTWTQIGHIPYQPS 677
 
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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