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Conserved domains on  [gi|530364544|ref|XP_005245136|]
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dynamin-3 isoform X6 [Homo sapiens]

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)

CATH:  1.20.120.1240|2.30.29.30|3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  15040446
SCOP:  4004047|4002395|4004048

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 5.97e-161

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


:

Pssm-ID: 197491  Cd Length: 240  Bit Score: 468.97  E-value: 5.97e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544     6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544    86 CKGKKFTDFDEVRLEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544   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 2.16e-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: 2.16e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 530364544  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 7.84e-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: 7.84e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 526 VIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKD 605
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 530364544 606 YRFLELACDSQEDVDSWKASLLRAGVYPDK 635
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
659-749 2.48e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.09  E-value: 2.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  659 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 738
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 530364544  739 LKEALGIIGDI 749
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 758-845 1.25e-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: 56.10  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  758 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDS-- 831
Cdd:PHA03247 2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANep 2638

                          90
                  ....*....|....*..
gi 530364544  832 ---FGAPPQVPSRPTRA 845
Cdd:PHA03247 2639 dphPPPTVPPPERPRDD 2655
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 5.97e-161

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 468.97  E-value: 5.97e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544     6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544    86 CKGKKFTDFDEVRLEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544   166 RENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGK 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 29-294 3.10e-146

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: 432.44  E-value: 3.10e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRLE 100
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 530364544 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 2.16e-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: 2.16e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 530364544  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 7.84e-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: 7.84e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 526 VIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKD 605
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 530364544 606 YRFLELACDSQEDVDSWKASLLRAGVYPDK 635
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 5.50e-69

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 225.96  E-value: 5.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544   34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirEMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 530364544  186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
659-749 2.48e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.09  E-value: 2.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  659 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 738
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 530364544  739 LKEALGIIGDI 749
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
658-749 1.35e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 110.02  E-value: 1.35e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544   658 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 737
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 530364544   738 ALKEALGIIGDI 749
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 526-629 1.16e-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: 1.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544   526 VIRKGWLTISNIGiMKGGSKGYWFVLTAESLSWYKDDEEKEK---KYMLPLDNLKVRD-VEKSFMSSKHIFALFNTEQRN 601
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKT 79

                           90       100
                   ....*....|....*....|....*...
gi 530364544   602 VYkdyrfleLACDSQEDVDSWKASLLRA 629
Cdd:smart00233  80 LL-------LQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 526-629 2.35e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 64.12  E-value: 2.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  526 VIRKGWLTISNIGImKGGSKGYWFVLTAESLSWYKDD---EEKEKKYMLPLDNLKVRDVEKSFMSS-KHIFALFNTEQRN 601
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 530364544  602 VykdyRFLELACDSQEDVDSWKASLLRA 629
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 758-845 1.25e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  758 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDS-- 831
Cdd:PHA03247 2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANep 2638

                          90
                  ....*....|....*..
gi 530364544  832 ---FGAPPQVPSRPTRA 845
Cdd:PHA03247 2639 dphPPPTVPPPERPRDD 2655
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 776-845 5.21e-07

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 51.53  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  776 PSPTTQRRPTLSAPLARPTSGRGPAPAIP--SPGPHS---------GAPPVPFRP------GPLPPFPSSSDSFGAP--- 835
Cdd:pfam15822 135 AAPSGPWGSMSSGPWAPGMGGQYPAPNMPypSPGPYPavpppqspgAAPPVPWGTvppgpwGPPAPYPDPTGSYPMPgly 214

                          90
                  ....*....|....*.
gi 530364544  836 P------QVPSRPTRA 845
Cdd:pfam15822 215 PtpnnpfQVPSGPSGA 230
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 767-842 4.42e-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: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 767 IQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGA----PPQVPSRP 842
Cdd:NF041121  18 AAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPgaalPVRVPAPP 97
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 757-842 2.80e-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: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 757 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTlsaplarptsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSfgAPP 836
Cdd:NF040983  97 PPPPPPPPTPPPPPPPPPPPPPPSPPPPP-------------PPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPI--QPT 161


                 ....*.
gi 530364544 837 QVPSRP 842
Cdd:NF040983 162 QLPSIP 167
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 751-870 7.07e-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: 7.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 751 TATVSTPAPPPVDDSwiqhsrrSPPPSPTTQRRPTLSAPLARP---TSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPS 827
Cdd:cd21975   43 AKGPGPPGPAWKPDG-------ADSPGLVTAAPHLLAANVLAPlrgPSVEGSSLESGDADMGSDSDVAPASGAAASTSPE 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530364544 828 SSDSFGAPPQVPSRPTRAPPSVPSRRPPPSPTRPTIIRPLESS 870
Cdd:cd21975  116 SSSDAASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPA 158
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 752-845 2.84e-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: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 752 ATVSTPAPPPVDDSwiQHSRRSPPPSPTTQRRPTLSAPlarptsGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSSDS 831
Cdd:NF041121  20 APPSPEGPAPTAAS--QPATPPPPAAPPSPPGDPPEPP------APEPAPL-PAPYPGSLAPPPPPPPGPAGAAPGAALP 90

                         90
                 ....*....|....*...
gi 530364544 832 FGAP-PQVPSRPT---RA 845
Cdd:NF041121  91 VRVPaPPALPNPLelaRA 108
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 5.97e-161

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 468.97  E-value: 5.97e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544     6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544    86 CKGKKFTDFDEVRLEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544   166 RENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGK 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 29-294 3.10e-146

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: 432.44  E-value: 3.10e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRLE 100
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 530364544 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 2.16e-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: 2.16e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 530364544  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 7.84e-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: 7.84e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 526 VIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKD 605
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 530364544 606 YRFLELACDSQEDVDSWKASLLRAGVYPDK 635
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 5.50e-69

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 225.96  E-value: 5.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544   34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirEMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 530364544  186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
659-749 2.48e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.09  E-value: 2.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  659 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 738
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 530364544  739 LKEALGIIGDI 749
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
658-749 1.35e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 110.02  E-value: 1.35e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544   658 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 737
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 530364544   738 ALKEALGIIGDI 749
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 526-629 1.16e-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: 1.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544   526 VIRKGWLTISNIGiMKGGSKGYWFVLTAESLSWYKDDEEKEK---KYMLPLDNLKVRD-VEKSFMSSKHIFALFNTEQRN 601
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKT 79

                           90       100
                   ....*....|....*....|....*...
gi 530364544   602 VYkdyrfleLACDSQEDVDSWKASLLRA 629
Cdd:smart00233  80 LL-------LQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 526-629 2.35e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 64.12  E-value: 2.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  526 VIRKGWLTISNIGImKGGSKGYWFVLTAESLSWYKDD---EEKEKKYMLPLDNLKVRDVEKSFMSS-KHIFALFNTEQRN 601
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 530364544  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 7.35e-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: 7.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 528 RKGWLTISNIGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKY--MLPLDN-LKVRDVEKSfmSSKHIFALFNTEQRNVYk 604
Cdd:cd00821    1 KEGYLLKRGGGGLKSWKK-RWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                         90       100
                 ....*....|....*....|..
gi 530364544 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 1.10e-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: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 526 VIRKGWLTisnigiMKGGS----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSfmSSKHIFALFNTEQRN 601
Cdd:cd01252    3 PDREGWLL------KLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVEDK--KKPFCFELYSPSNGQ 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530364544 602 VYKD----------------YRfleLACDSQEDVDSWKASLLRA 629
Cdd:cd01252   75 VIKAcktdsdgkvvegnhtvYR---ISAASEEERDEWIKSIKAS 115
PHA03247 PHA03247
large tegument protein UL36; Provisional
 758-845 1.25e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  758 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDS-- 831
Cdd:PHA03247 2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANep 2638

                          90
                  ....*....|....*..
gi 530364544  832 ---FGAPPQVPSRPTRA 845
Cdd:PHA03247 2639 dphPPPTVPPPERPRDD 2655
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 752-844 3.22e-07

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 52.94  E-value: 3.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 752 ATVSTPAPP--------PVDDSWIQHSRR---SPPPSPTT-QRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFrP 819
Cdd:PHA02682  32 ATIPAPAAPcppdadvdPLDKYSVKEAGRyyqSRLKANSAcMQRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVTC-P 110

                         90       100
                 ....*....|....*....|....*
gi 530364544 820 GPLPPFPSSSDSFGAPPQVPSRPTR 844
Cdd:PHA02682 111 APAPACPPATAPTCPPPAVCPAPAR 135
PHA03247 PHA03247
large tegument protein UL36; Provisional
 756-845 3.60e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  756 TPaPPPVDD--SWIQHSRRSPPPSPTTQRRPTLSAPLARPTSG------RGPAPA-IPSPGPHSGAPPVPFRP-GPLPPF 825
Cdd:PHA03247  360 TP-PSSLEDlsAGRHHPKRASLPTRKRRSARHAATPFARGPGGddqtrpAAPVPAsVPTPAPTPVPASAPPPPaTPLPSA 438

                          90       100
                  ....*....|....*....|
gi 530364544  826 PSSSDSFGAPPQVPSRPTRA 845
Cdd:PHA03247  439 EPGSDDGPAPPPERQPPAPA 458
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 776-845 5.21e-07

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 51.53  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  776 PSPTTQRRPTLSAPLARPTSGRGPAPAIP--SPGPHS---------GAPPVPFRP------GPLPPFPSSSDSFGAP--- 835
Cdd:pfam15822 135 AAPSGPWGSMSSGPWAPGMGGQYPAPNMPypSPGPYPavpppqspgAAPPVPWGTvppgpwGPPAPYPDPTGSYPMPgly 214

                          90
                  ....*....|....*.
gi 530364544  836 P------QVPSRPTRA 845
Cdd:pfam15822 215 PtpnnpfQVPSGPSGA 230
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 752-845 6.59e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 53.25  E-value: 6.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  752 ATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARP------TSGRGPAPAIPSPGPHSGAPpvpfrPGPLPPF 825
Cdd:PHA03307  119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAavasdaASSRQAALPLSSPEETARAP-----SSPPAEP 193

                          90       100
                  ....*....|....*....|..
gi 530364544  826 PSSSDSFGAP--PQVPSRPTRA 845
Cdd:PHA03307  194 PPSTPPAAASprPPRRSSPISA 215
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 526-629 1.17e-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: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 526 VIRKGWLTisnigimKGGSKGY------WFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSF-MSSKHIFALFNTE 598
Cdd:cd13248    7 VVMSGWLH-------KQGGSGLknwrkrWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHAN 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 530364544 599 QRNVYkdyrfleLACDSQEDVDSWKASLLRA 629
Cdd:cd13248   80 MRTYY-------FAADTAEEMEQWMNAMSLA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-845 1.55e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  747 GDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSgrGPAPAIPSPGPHSGAPPVPFRPGPLPPFP 826
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA--GPPRRLTRPAVASLSESRESLPSPWDPAD 2806

                          90
                  ....*....|....*....
gi 530364544  827 SSSDSFGAPPQVPSRPTRA 845
Cdd:PHA03247 2807 PPAAVLAPAAALPPAASPA 2825
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
 548-629 1.98e-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: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 548 WFVLTAESLSWYKDDEEKEKKYMLPLDNL----KVRDVEKsfmssKHIFALFNTEqrnvyKDYRFlelACDSQEDVDSWk 623
Cdd:cd13298   26 WVVLRPCQLSYYKDEKEYKLRRVINLSELlavaPLKDKKR-----KNVFGIYTPS-----KNLHF---RATSEKDANEW- 91


                 ....*.
gi 530364544 624 ASLLRA 629
Cdd:cd13298   92 VEALRE 97
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-842 3.10e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  751 TATVSTPAPPPVDDSWIQHS------------------RRSPPPSPTTQRRPTLSApLARPTSGRGPAP-AIPSPGPHS- 810
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSlplggsvapggdvrrrppSRSPAAKPAAPARPPVRR-LARPAVSRSTESfALPPDQPERp 2908

                          90       100       110
                  ....*....|....*....|....*....|..
gi 530364544  811 GAPPVPFRPGPLPPFPSSSDSFGAPPQvPSRP 842
Cdd:PHA03247 2909 PQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRP 2939
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 767-842 4.42e-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: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 767 IQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGA----PPQVPSRP 842
Cdd:NF041121  18 AAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPgaalPVRVPAPP 97
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 719-842 2.32e-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: 47.23  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  719 MEESAEQAQRRDemlRMYQALkeALGIIGDISTATVSTPApppvddswIQHSRRSP-PPSPTTQRRPTLSAPLARPTSGR 797
Cdd:pfam07174   1 MDQVDPNSTRRK---GLWATL--AIAAVAGASAVAVALPA--------VAHADPEPaPPPPSTATAPPAPPPPPPAPAAP 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 530364544  798 GPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRP 842
Cdd:pfam07174  68 APPPP-PAAPNAPNAPPPPADPNAPPPPPADPNAPPPPAVDPNAP 111
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 757-842 2.80e-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: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 757 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTlsaplarptsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSfgAPP 836
Cdd:NF040983  97 PPPPPPPPTPPPPPPPPPPPPPPSPPPPP-------------PPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPI--QPT 161


                 ....*.
gi 530364544 837 QVPSRP 842
Cdd:NF040983 162 QLPSIP 167
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 751-842 3.26e-05

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: 46.13  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  751 TATVSTPAPPPVDDSWIQHSRRSPPPSPTTQrrPTLSAPLARPTS-GRGPAPAipspGPHSGAPPVPFRPGPLPPFPSSS 829
Cdd:pfam15822  15 TSAVSNPKPGQPPQGWPGSNPWNNPSAPPAV--PSGLPPSTAPSTvPFGPAPT----GMYPSIPLTGPSPGPPAPFPPSG 88

                          90
                  ....*....|...
gi 530364544  830 DSfgAPPqvPSRP 842
Cdd:pfam15822  89 PS--CPP--PGGP 97
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
 526-628 3.96e-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: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 526 VIRKGWLTiSNIGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMS-SKHIFALF---NTEQRN 601
Cdd:cd13378    3 VLKAGWLK-KQRSIMKNWQQ-RWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNELPPNPEEpGKHLFEILpggAGDREK 80

                         90       100
                 ....*....|....*....|....*..
gi 530364544 602 VYKDYRFLELACDSQEDVDSWKASLLR 628
Cdd:cd13378   81 VPMNHEAFLLMANSQSDMEDWVKAIRR 107
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 755-842 4.19e-05

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 46.92  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 755 STP-APPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPF--PSSSDS 831
Cdd:PHA03264 261 SKGyEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDAdrPEGWPS 340

                         90
                 ....*....|....
gi 530364544 832 FGA---PPQVPSRP 842
Cdd:PHA03264 341 LEAitfPPPTPATP 354
PHA03247 PHA03247
large tegument protein UL36; Provisional
 758-845 4.48e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  758 APPPVDDswIQHSRRSPPPSPTTQRRPT-----LSAPLArPTSGRG---PAPAIPSPGPHSGAPPVPF--RPGPLPPFPS 827
Cdd:PHA03247 2688 ARPTVGS--LTSLADPPPPPPTPEPAPHalvsaTPLPPG-PAAARQaspALPAAPAPPAVPAGPATPGgpARPARPPTTA 2764

                          90
                  ....*....|....*...
gi 530364544  828 SSDSFGAPPQVPSRPTRA 845
Cdd:PHA03247 2765 GPPAPAPPAAPAAGPPRR 2782
PHA03247 PHA03247
large tegument protein UL36; Provisional
 749-842 6.67e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  749 ISTATVSTPAPPPVDDswiqHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSP---------------------G 807
Cdd:PHA03247 2791 LSESRESLPSPWDPAD----PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGppppslplggsvapggdvrrrP 2866

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 530364544  808 PHSGAPPVPFRPG-------PLPPFPSSSDSFGAPPQVPSRP 842
Cdd:PHA03247 2867 PSRSPAAKPAAPArppvrrlARPAVSRSTESFALPPDQPERP 2908
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
 717-839 7.44e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 46.37  E-value: 7.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 717 TLMEESAEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPvddswiqhsrrsPPPSPTTQRRPTLSAPLAR-PTS 795
Cdd:PRK14963 313 TALDEQMERFARRSDALSLELALLHALLALGGAPSEGVAAVAPPA------------PAPADLTQRLNRLEKEVRSlRSA 380

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530364544 796 GRGPAPAIPSPGPHSGapPVPFR-PGPLPPFPSSSDSFGAPPQVP 839
Cdd:PRK14963 381 PTAAATAAGAPLPDFD--PRPRGpPAPEPARSAEAPPLVAPAAAP 423
PHA03247 PHA03247
large tegument protein UL36; Provisional
 757-845 9.12e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 9.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  757 PAPPPVDDSwiQHSRRSPPPSPTtqrrPTLSAPlARPTSGRGPAPAIPSPGPHSGAPPVPFRPGP----LPPFPSSSDSF 832
Cdd:PHA03247 2905 PERPPQPQA--PPPPQPQPQPPP----PPQPQP-PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPwlgaLVPGRVAVPRF 2977

                          90
                  ....*....|...
gi 530364544  833 GAPPQVPSRPTRA 845
Cdd:PHA03247 2978 RVPQPAPSREAPA 2990
PH2_PH_fungal cd13299
Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal ...
 545-626 9.80e-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: 9.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 545 KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLkVRDVEKSFMSSKHIFAL-FNTEQrnvyKDYRFlelACDSQEDVDSWK 623
Cdd:cd13299   24 KKYWLVLRNRSLSFYKDQSEYSPVKIIPIDDI-IDVVELDPLSKSKKWCLqIITPE----KRIRF---CADDEESLIKWL 95


                 ...
gi 530364544 624 ASL 626
Cdd:cd13299   96 GAL 98
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 746-845 1.02e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  746 IGDISTATVSTPAPPPVDDSwiqhsRRSPPPSP--------TTQRRPT----------LSAPLARPTSGRGPAPAI---P 804
Cdd:PHA03307  273 SGWNGPSSRPGPASSSSSPR-----ERSPSPSPsspgsgpaPSSPRASssssssressSSSTSSSSESSRGAAVSPgpsP 347

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 530364544  805 SPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRA 845
Cdd:PHA03307  348 SRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRR 388
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 750-845 1.22e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 750 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPtlsAPLARPTSGRGPAPAIPSPGP-HSGAPPVPFRPGPLPPFPSS 828
Cdd:PRK07764 401 AAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAP---APAPAPPSPAGNAPAGGAPSPpPAAAPSAQPAPAPAAAPEPT 477

                         90
                 ....*....|....*..
gi 530364544 829 SDSFGAPPQVPSRPTRA 845
Cdd:PRK07764 478 AAPAPAPPAAPAPAAAP 494
PHA03377 PHA03377
EBNA-3C; Provisional
 753-842 1.29e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 45.81  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  753 TVSTPAPP---PVDD---SWIQHSRRSPPP-SPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPV-------PFR 818
Cdd:PHA03377  525 SVTQPAKPhrkVQDGfqrSGRRQKRATPPKvSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPStgprqqaKCK 604

                          90       100
                  ....*....|....*....|....
gi 530364544  819 PGPlppfPSSSDSFGAPPQvpSRP 842
Cdd:PHA03377  605 DGP----PASGPHEKQPPS--SAP 622
PHA03247 PHA03247
large tegument protein UL36; Provisional
 750-842 1.43e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  750 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTS-GRGPAPAIPSPGPHSGA-----PPVPFRPGPLP 823
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSeSRESLPSPWDPADPPAAvlapaAALPPAASPAG 2826

                          90
                  ....*....|....*....
gi 530364544  824 PFPSSSDSFGAPPQVPSRP 842
Cdd:PHA03247 2827 PLPPPTSAQPTAPPPPPGP 2845
PHA03247 PHA03247
large tegument protein UL36; Provisional
 759-842 1.46e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  759 PPPVDDSWIQHSRRSPPPSPTTQRRPTL-SAPLARPTSGRGPAPAI--------PSPGPHSGAPPVPFRPG-PLPPFPSS 828
Cdd:PHA03247 2648 PPERPRDDPAPGRVSRPRRARRLGRAAQaSSPPQRPRRRAARPTVGsltsladpPPPPPTPEPAPHALVSAtPLPPGPAA 2727

                          90
                  ....*....|....*
gi 530364544  829 S-DSFGAPPQVPSRP 842
Cdd:PHA03247 2728 ArQASPALPAAPAPP 2742
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 711-845 1.50e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  711 SSEDQNTLMEESAEQAQRRDEMLrmyqALKEALGII-----GDISTATVSTPAPPPVDDSwiQHSRRSPPPSPTTQRRPT 785
Cdd:pfam03154 150 SPQDNESDSDSSAQQQILQTQPP----VLQAQSGAAsppspPPPGTTQAATAGPTPSAPS--VPPQGSPATSQPPNQTQS 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  786 LSAPLARPTSG------RGPAP-------------------AIPSPGPHSGAPPVPFR--------PGPLPPFPSSSDSF 832
Cdd:pfam03154 224 TAAPHTLIQQTptlhpqRLPSPhpplqpmtqppppsqvspqPLPQPSLHGQMPPMPHSlqtgpshmQHPVPPQPFPLTPQ 303

                         170
                  ....*....|...
gi 530364544  833 GAPPQVPSRPTRA 845
Cdd:pfam03154 304 SSQSQVPPGPSPA 316
PHA03378 PHA03378
EBNA-3B; Provisional
 752-842 1.59e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 752 ATVSTPAPPPvddswiqhSRRSPPPSPTTQRRPTLSA------PLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLP-P 824
Cdd:PHA03378 692 GTMQPPPRAP--------TPMRPPAAPPGRAQRPAAAtgrarpPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPgR 763

                         90       100
                 ....*....|....*....|...
gi 530364544 825 FPSSSDSFGAP-----PQVPSRP 842
Cdd:PHA03378 764 ARPPAAAPGAPtpqppPQAPPAP 786
PHA03247 PHA03247
large tegument protein UL36; Provisional
 750-845 1.63e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  750 STATVSTPAPPPVDDSWIQhsRRSPPP-----SPTTQRRPTLSAPLARPTSGRGPAPAIP-SPGPHSGAPP----VPFRP 819
Cdd:PHA03247 2762 TTAGPPAPAPPAAPAAGPP--RRLTRPavaslSESRESLPSPWDPADPPAAVLAPAAALPpAASPAGPLPPptsaQPTAP 2839

                          90       100       110
                  ....*....|....*....|....*....|....
gi 530364544  820 GPLPPFPSSSDSFG---AP-----PQVPSRPTRA 845
Cdd:PHA03247 2840 PPPPGPPPPSLPLGgsvAPggdvrRRPPSRSPAA 2873
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 744-843 1.89e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 744 GIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTlSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLP 823
Cdd:PRK07764 661 DASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA-PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPV 739

                         90       100
                 ....*....|....*....|
gi 530364544 824 PFPSSSDSFGAPPQVPSRPT 843
Cdd:PRK07764 740 PLPPEPDDPPDPAGAPAQPP 759
PH_Boi cd13316
Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally ...
 529-629 1.96e-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: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 529 KGWLTisnigiMKGGSKGYW----FVLTAESLSWYKDDEEKEKKYMLPLDNLKV-RDVEKSFMSSKHIFALFNTEQRNVY 603
Cdd:cd13316    3 SGWMK------KRGERYGTWktryFVLKGTRLYYLKSENDDKEKGLIDLTGHRVvPDDSNSPFRGSYGFKLVPPAVPKVH 76

                         90       100
                 ....*....|....*....|....*.
gi 530364544 604 kdYrfleLACDSQEDVDSWKASLLRA 629
Cdd:cd13316   77 --Y----FAVDEKEELREWMKALMKA 96
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 749-844 2.49e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 44.95  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 749 ISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAI-------PSPGPHSGAP-------P 814
Cdd:PHA03321 404 LATELFRTGVPSEHYEASLRLLSSRQPPGAPAPRRDNDPPPPPRARPGSTPACARraraqraRDAGPEYVDPlgalrrlP 483

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530364544 815 VPFRPGPLPPFPSSSDSF-----GAPPQVPSRPTR 844
Cdd:PHA03321 484 AGAAPPPEPAAAPSPATYytrmgGGPPRLPPRNRA 518
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
 771-841 2.57e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 44.73  E-value: 2.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530364544 771 RRSPPPSPTTQRRPTlSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSF-GAPPQVPSR 841
Cdd:PRK14965 379 RGAPAPPSAAWGAPT-PAAPAAPPPAAAPPVPPAAPARPAAARPAPAPAPPAAAAPPARSADpAAAASAGDR 449
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 773-843 2.75e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 43.70  E-value: 2.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530364544 773 SPP-PSPTTQRrPTLSAPLARP-TSGRGPAPAIPsPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRPT 843
Cdd:PHA02682  85 SPAcAAPAPAC-PACAPAAPAPaVTCPAPAPACP-PATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLPT 155
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 749-845 3.38e-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: 44.52  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  749 ISTATVSTPAPPPVDDSwiqHSRRSPPPSP----TTQRRPTLSAP---LARPT-SGRGPAPAIPSPGPHSGAP------- 813
Cdd:pfam05109 468 VSTADVTSPTPAGTTSG---ASPVTPSPSPrdngTESKAPDMTSPtsaVTTPTpNATSPTPAVTTPTPNATSPtlgktsp 544

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530364544  814 ------PVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRA 845
Cdd:pfam05109 545 tsavttPTPNATSPTPAVTTPTPNATIPTLGKTSPTSA 582
PHA03378 PHA03378
EBNA-3B; Provisional
 752-842 3.50e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 752 ATVSTPAPPPV-DDSWIQHSRRSPPPSPTTQRRPT-LSAPLARPTSGRGP--APAIPSPGPHSGAPPVPF---RPGPLPP 824
Cdd:PHA03378 718 AAATGRARPPAaAPGRARPPAAAPGRARPPAAAPGrARPPAAAPGRARPPaaAPGAPTPQPPPQAPPAPQqrpRGAPTPQ 797

                         90
                 ....*....|....*...
gi 530364544 825 fpsssdsfgAPPQVPSRP 842
Cdd:PHA03378 798 ---------PPPQAGPTS 806
PHA03247 PHA03247
large tegument protein UL36; Provisional
 757-845 3.77e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  757 PAPP-PVDdswiqhsrrspPPSPTTQRrptlSAPLARPTSgRGPAPAIPSPGPHSGAPPVPFRP-----------GPLPP 824
Cdd:PHA03247 2551 PPPPlPPA-----------APPAAPDR----SVPPPRPAP-RPSEPAVTSRARRPDAPPQSARPrapvddrgdprGPAPP 2614

                          90       100
                  ....*....|....*....|.
gi 530364544  825 FPSSSDSFGAPPQVPSRPTRA 845
Cdd:PHA03247 2615 SPLPPDTHAPDPPPPSPSPAA 2635
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 733-843 3.85e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 44.03  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 733 LRMYQALKEALgiigdISTATVSTPAPPpvddswiqhsrRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGA 812
Cdd:PRK14950 349 LPLELAVIEAL-----LVPVPAPQPAKP-----------TAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPV 412

                         90       100       110
                 ....*....|....*....|....*....|.
gi 530364544 813 PPVPFRPGPLPPFPSSSDSFGAPPQVPSRPT 843
Cdd:PRK14950 413 PPRPVAPPVPHTPESAPKLTRAAIPVDEKPK 443
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
 526-576 3.86e-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: 3.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530364544 526 VIRKGWLTISNIGIMKGGS---KGYWFVLTAESLSWYKD-DEEKEKKYMLPLDNL 576
Cdd:cd13297   13 VIERGWLYKEGGKGGARGNltkKKRWFVLTGNSLDYYKSsEKNSLKLGTLVLNSL 67
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 751-842 4.20e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.93  E-value: 4.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 751 TATVSTPAPPPVddswiQHSRRSPPPSPTTQRRPTlSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSD 830
Cdd:PRK14951 385 EAAAPAAAPVAQ-----AAAAPAPAAAPAAAASAP-AAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPE 458

                         90
                 ....*....|..
gi 530364544 831 SFGAPPQVPSRP 842
Cdd:PRK14951 459 TVAIPVRVAPEP 470
PHA03378 PHA03378
EBNA-3B; Provisional
 711-844 4.40e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 4.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 711 SSEDQNTLMEESAEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPL 790
Cdd:PHA03378 605 TPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTM 684

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530364544 791 ARPTSGRG---PAPAIPSPGPHSGAPPVPFRP-----GPLPPfPSSSDSFGAPPQVPSRPTR 844
Cdd:PHA03378 685 LPIQWAPGtmqPPPRAPTPMRPPAAPPGRAQRpaaatGRARP-PAAAPGRARPPAAAPGRAR 745
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
 519-626 4.71e-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: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 519 LPPSRQIVIRKGWLTisnigiMKGGSKG----YWFVLTAESLSWYKDDEEkekKYmLPLDNLKVRDV-----EKSFMSSK 589
Cdd:cd13215   14 LPKRSGAVIKSGYLS------KRSKRTLrytrYWFVLKGDTLSWYNSSTD---LY-FPAGTIDLRYAtsielSKSNGEAT 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530364544 590 HIFALFNTEQRnvykdYRFLelaCDSQEDVDSWKASL 626
Cdd:cd13215   84 TSFKIVTNSRT-----YKFK---ADSETSADEWVKAL 112
DUF4813 pfam16072
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ...
 755-841 5.54e-04

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


Pssm-ID: 435117 [Multi-domain]  Cd Length: 288  Bit Score: 42.82  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  755 STPAPP--PVDDSWIQHSRRSPPPSPTTQRRPTLSAPLArPTSGRGPAPAIPSPGPHSGApPVPFRPGPLPPFPSSSDSF 832
Cdd:pfam16072 169 AAPAAPayPVAPAAYPAQAPAAAPAPAPGAPQTPLAPLN-PVAAAPAAAAGAAAAPVVAA-AAPAAAAPPPPAPAAPPAD 246

                          90
                  ....*....|....*
gi 530364544  833 GAPPQ------VPSR 841
Cdd:pfam16072 247 AAPPApggiicVPVR 261
PHA03247 PHA03247
large tegument protein UL36; Provisional
 750-866 6.81e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  750 STATVSTPAPPPVDDSWIQHSRRSPPPSPTT------------QRRPTLSAPLARP-TSGRGPAPAIPSPGPHSGAPPVP 816
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvapggdvRRRPPSRSPAAKPaAPARPPVRRLARPAVSRSTESFA 2899

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530364544  817 FRPGPLPPFPsssdsfgaPPQVPSRPTraPPSVPSRRPPPSPTRPTIIRP 866
Cdd:PHA03247 2900 LPPDQPERPP--------QPQAPPPPQ--PQPQPPPPPQPQPPPPPPPRP 2939
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 751-870 7.07e-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: 7.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 751 TATVSTPAPPPVDDSwiqhsrrSPPPSPTTQRRPTLSAPLARP---TSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPS 827
Cdd:cd21975   43 AKGPGPPGPAWKPDG-------ADSPGLVTAAPHLLAANVLAPlrgPSVEGSSLESGDADMGSDSDVAPASGAAASTSPE 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530364544 828 SSDSFGAPPQVPSRPTRAPPSVPSRRPPPSPTRPTIIRPLESS 870
Cdd:cd21975  116 SSSDAASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPA 158
PHA03247 PHA03247
large tegument protein UL36; Provisional
 752-848 7.35e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 7.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  752 ATVSTPAPPPVddswiqhsRR--SPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSP---GPHSGAPPVPFRPGPLPPFP 826
Cdd:PHA03247 2873 AKPAAPARPPV--------RRlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPqppPPPQPQPPPPPPPRPQPPLA 2944

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530364544  827 SSSDSFGAPPQVPSRP----------------TRAPPS 848
Cdd:PHA03247 2945 PTTDPAGAGEPSGAVPqpwlgalvpgrvavprFRVPQP 2982
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
 526-574 8.67e-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: 8.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530364544 526 VIRKGWLtisnigiMKGGSK-----GYWFVLTAESLSWYKDDEEKEKKYMLPLD 574
Cdd:cd13273    8 VIKKGYL-------WKKGHLlptwtERWFVLKPNSLSYYKSEDLKEKKGEIALD 54
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
737-831 9.40e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 43.03  E-value: 9.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 737 QALKEALG-------IIGDISTATVSTPAPPPVDDSwIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPH 809
Cdd:PRK14948 496 QAFAKVLGrsiklnlESQSGSASNTAKTPPPPQKSP-PPPAPTPPLPQPTATAPPPTPPPPPPTATQASSNAPAQIPADS 574

                         90       100
                 ....*....|....*....|..
gi 530364544 810 SGAPPVPFRPGPLPPFPSSSDS 831
Cdd:PRK14948 575 SPPPPIPEEPTPSPTKDSSPEE 596
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 757-839 9.70e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  757 PAPPPVDDSWIQHSRRSPPPSPTTQrrptlsapLARPTSGRGPAPAiPSPGPHSGAPPvpfRPGPLPPFPSSSDSFGAPP 836
Cdd:pfam03154 292 PVPPQPFPLTPQSSQSQVPPGPSPA--------APGQSQQRIHTPP-SQSQLQSQQPP---REQPLPPAPLSMPHIKPPP 359


                  ...
gi 530364544  837 QVP 839
Cdd:pfam03154 360 TTP 362
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 726-845 9.72e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 9.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 726 AQRRDEMLRmyQALKEALGIigdisTATVS-TPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLS-APLARPTSGRGPAPAI 803
Cdd:PRK07764 563 SPGNAEVLV--TALAEELGG-----DWQVEaVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPaAPAAPAAPAPAGAAAA 635

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530364544 804 PSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRA 845
Cdd:PRK07764 636 PAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAA 677
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 752-824 9.76e-04

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


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 39.68  E-value: 9.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530364544  752 ATVSTPAPPPVDdswiqhsrrSPPPSPTTQRRPTLSAPlARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPP 824
Cdd:pfam12526  41 PPVGDPRPPVVD---------TPPPVSAVWVLPPPSEP-AAPEPDLVPPVTGPAGPPSPLAPPAPAQKPPLPP 103
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
 548-628 1.32e-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: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 548 WFVLTAESLSWYKDDEEKEKKY--MLPLDnlKVRDVEK----SFMSSKHIFALfnteqrnVYKDYrFLELACDSQEDVDS 621
Cdd:cd01238   24 WFVLTKSSLSYYEGDGEKRGKEkgSIDLS--KVRCVEEvkdeAFFERKYPFQV-------VYDDY-TLYVFAPSEEDRDE 93


                 ....*..
gi 530364544 622 WKASLLR 628
Cdd:cd01238   94 WIAALRK 100
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-845 1.33e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  751 TATVSTPAPPPVDDSWIQHS-----RRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVpfrpgpLPPF 825
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASpalpaAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR------LTRP 2786

                          90       100
                  ....*....|....*....|....
gi 530364544  826 PSSSDSFGAP----PQVPSRPTRA 845
Cdd:PHA03247 2787 AVASLSESREslpsPWDPADPPAA 2810
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
750-841 1.38e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 750 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRptlSAPLARPTSGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSS 829
Cdd:PRK12323 404 AAPAAAPAAAAAARAVAAAPARRSPAPEALAAAR---QASARGPGGAPAPAPA-PAAAPAAAARPAAAGPRPVAAAAAAA 479

                         90
                 ....*....|..
gi 530364544 830 DSFGAPPQVPSR 841
Cdd:PRK12323 480 PARAAPAAAPAP 491
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
 524-629 1.78e-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: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 524 QIVIRKGWLTISNiGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVE-KSFMSSKHIFALF----NTE 598
Cdd:cd13263    1 ERPIKSGWLKKQG-SIVKNWQQ-RWFVLRGDQLYYYKDEDDTKPQGTIPLPGNKVKEVPfNPEEPGKFLFEIIpgggGDR 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 530364544 599 QRNVYKDYRfleLACDSQEDVDSWKASLLRA 629
Cdd:cd13263   79 MTSNHDSYL---LMANSQAEMEEWVKVIRRV 106
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 755-845 2.08e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  755 STPAPPPVDDSWIQHSRRSPPPspTTQRRPTLSAPLARPTSGRGPAPAIPSPGPhsgAPPVPFRPGPLPPFPSSSDSFGA 834
Cdd:PHA03307   67 PPTGPPPGPGTEAPANESRSTP--TWSLSTLAPASPAREGSPTPPGPSSPDPPP---PTPPPASPPPSPAPDLSEMLRPV 141

                          90
                  ....*....|.
gi 530364544  835 PPQVPSRPTRA 845
Cdd:PHA03307  142 GSPGPPPAASP 152
PH2_TAPP1_2 cd13271
Tandem PH-domain-containing proteins 1 and 2 Pleckstrin homology (PH) domain, C-terminal ...
 520-622 2.31e-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: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 520 PPSRQIVIRKGWLTISNIgIMKGGSKGYwFVLTAESLSWYKDDEEKEKKYMLPL-DNLKVRDVE-KSFMSSKHIFALFnT 597
Cdd:cd13271    2 QRAGRNVIKSGYCVKQGA-VRKNWKRRF-FILDDNTISYYKSETDKEPLRTIPLrEVLKVHECLvKSLLMRDNLFEII-T 78

                         90       100
                 ....*....|....*....|....*
gi 530364544 598 EQRNVYkdyrfleLACDSQEDVDSW 622
Cdd:cd13271   79 TSRTFY-------IQADSPEEMHSW 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
 757-844 2.38e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  757 PAPPPVDDSW-IQHSRRSPPPSPTTQ--RRPTLSAPLARPTS-GRGPAP-AIPSPGPHSGAPPVPFRPGP------LPPF 825
Cdd:PHA03247 2656 PAPGRVSRPRrARRLGRAAQASSPPQrpRRRAARPTVGSLTSlADPPPPpPTPEPAPHALVSATPLPPGPaaarqaSPAL 2735

                          90       100
                  ....*....|....*....|.
gi 530364544  826 PSSSDSFGAP--PQVPSRPTR 844
Cdd:PHA03247 2736 PAAPAPPAVPagPATPGGPAR 2756
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 752-845 2.84e-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: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 752 ATVSTPAPPPVDDSwiQHSRRSPPPSPTTQRRPTLSAPlarptsGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSSDS 831
Cdd:NF041121  20 APPSPEGPAPTAAS--QPATPPPPAAPPSPPGDPPEPP------APEPAPL-PAPYPGSLAPPPPPPPGPAGAAPGAALP 90

                         90
                 ....*....|....*...
gi 530364544 832 FGAP-PQVPSRPT---RA 845
Cdd:NF041121  91 VRVPaPPALPNPLelaRA 108
PHA03379 PHA03379
EBNA-3A; Provisional
 750-839 2.89e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.58  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 750 STATVSTPAPPPVDDSWIQ--HSRRSPPPSPTTQRRPTLSAPLAR-------PTSGRG---PAPAI---------PSPGP 808
Cdd:PHA03379 436 SHGSAQVPEPPPVHDLEPGplHDQHSMAPCPVAQLPPGPLQDLEPgdqlpgvVQDGRPacaPVPAPagpivrpweASLSQ 515

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530364544 809 HSGAPPVPFRPGPLP----PFPSSSDSFGAPPQVP 839
Cdd:PHA03379 516 VPGVAFAPVMPQPMPvepvPVPTVALERPVCPAPP 550
SSDP pfam04503
Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA ...
 732-831 3.07e-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: 40.71  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  732 MLRMYQALKEALGIIGdISTATVSTPAPPPvddswiqHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSG 811
Cdd:pfam04503 128 MQRMNPPRGPGMGPMG-PQSYGPGMRGPPP-------NSTDGPGGMPPMNMGPGGRRPWPQPNASNPLPYSSSSPGSYGG 199

                          90       100
                  ....*....|....*....|
gi 530364544  812 APPVPFRPGPLPPFPSSSDS 831
Cdd:pfam04503 200 PPGGGGPPGPTPIMPSPQDS 219
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 751-843 3.09e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 751 TATVSTPAPPPVDDswiQHSRRSPPPSPTTQRRPtlSAPLARPTSGRGPAPAiPSPGPHSGAPPVPF-RPGPLPPFPSSS 829
Cdd:PRK07764 417 PAAAAAPAPAAAPQ---PAPAPAPAPAPPSPAGN--APAGGAPSPPPAAAPS-AQPAPAPAAAPEPTaAPAPAPPAAPAP 490

                         90
                 ....*....|....
gi 530364544 830 DsfgAPPQVPSRPT 843
Cdd:PRK07764 491 A---AAPAAPAAPA 501
DUF4639 pfam15479
Domain of unknown function (DUF4639); This family of proteins is found in eukaryotes. Proteins ...
 778-843 3.27e-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: 40.95  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  778 PTTQRRPtLSAPLARPTSGRGPAPAIP-SPGPHSGAPP---------VPFR---PGPLPPFPS-----SSDSFG------ 833
Cdd:pfam15479 361 PDSEARP-LEAYRGRQRSEKTKARAGPqAPGPGVRVSPaaffplppgVPFRalgPGPGLQFPTlnlglPSPSFGsklpfp 439

                          90       100
                  ....*....|....*....|.
gi 530364544  834 -----------APPQVPSRPT 843
Cdd:pfam15479 440 spglrflathpVLPDVARSPS 460
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 750-842 4.35e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 750 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSG-----RGPAPAIPSPGPHSGAPPVPfRPGPLPP 824
Cdd:PRK07764 642 APAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAapaapAGAAPAQPAPAPAATPPAGQ-ADDPAAQ 720

                         90
                 ....*....|....*...
gi 530364544 825 FPSSSDSFGAPPQVPSRP 842
Cdd:PRK07764 721 PPQAAQGASAPSPAADDP 738
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
 526-629 4.39e-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: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 526 VIRKGWLtisnigiMKGGS-----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQr 600
Cdd:cd13301    3 IIKEGYL-------VKKGHvvnnwKARWFVLKEDGLEYYKKKTDSSPKGMIPLKGCTITSPCLEYGKRPLVFKLTTAKG- 74

                         90       100
                 ....*....|....*....|....*....
gi 530364544 601 nvyKDYrFLElACdSQEDVDSWKASLLRA 629
Cdd:cd13301   75 ---QEH-FFQ-AC-SREERDAWAKDITKA 97
PHA03377 PHA03377
EBNA-3C; Provisional
 766-844 4.41e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.81  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  766 WIQHSRRSPPPSPTTQRRPTLS---APLARP--TSGRGPAPAIPSPGP----HSGAPPVPFrpgPLPPFPSSSDSFGAP- 835
Cdd:PHA03377  813 WSQYPGHGHPQGPWAPRPPHLPpqwDGSAGHgqDQVSQFPHLQSETGPprlqLSQVPQLPY---SQTLVSSSAPSWSSPq 889

                          90
                  ....*....|.
gi 530364544  836 PQVPSRP--TR 844
Cdd:PHA03377  890 PRAPIRPipTR 900
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
 528-566 4.99e-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: 4.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530364544 528 RKGWLtisnigiMKGGSKG-----YWFVLTAESLSWYKD--DEEKE 566
Cdd:cd13275    1 KKGWL-------MKQGSRQgewskHWFVLRGAALKYYRDpsAEEAG 39
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 774-840 5.42e-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: 5.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  774 PPPSPTT-QRRPTLS--APLARPTSGRGPAPAIPSPGphSGAPPVPfrpgplppfPSSSdsFGAPPQVPS 840
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 5.53e-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: 5.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 530 GWLTI--SNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSfmSSKHIFALfnteQRNVYKDYR 607
Cdd:cd01260   17 GWLWKkkEAKSFFGQKWKKYWFVLKGSSLYWYSNQQDEKAEGFINLPDFKIERASEC--KKKYAFKA----CHPKIKTFY 90

                         90       100
                 ....*....|....*....|..
gi 530364544 608 FlelACDSQEDVDSWKASLLRA 629
Cdd:cd01260   91 F---AAENLDDMNKWLSKLNMA 109
TYA pfam01021
Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a ...
 755-840 6.10e-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: 39.94  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544  755 STPAPPPVDDSwiqHSRRSPPP--SPTTQRRP----TLSAPLARPTSGRgPAPAIPS--PGPHSGAPPVPFRPGPLPPFP 826
Cdd:pfam01021  40 TTPGSSAVPEN---HHHASPQPasVPPPQNGPysqqCMMTPNQANPSGW-PFYGHPSmmPYTPYQMSPMYFPPGPQSQFP 115

                          90
                  ....*....|....
gi 530364544  827 SSSDSFGAPPQVPS 840
Cdd:pfam01021 116 QYPSSVGTPLSTPS 129
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 750-845 7.56e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 750 STATVSTPAPPPVDDSWIQHSRRSPPPSP----TTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPF 825
Cdd:PRK07764 608 PPEEAARPAAPAAPAAPAAPAPAGAAAAPaeasAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAP 687

                         90       100
                 ....*....|....*....|..
gi 530364544 826 PSSSDSFGAPP--QVPSRPTRA 845
Cdd:PRK07764 688 AAPAAPAGAAPaqPAPAPAATP 709
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 774-840 8.15e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 39.66  E-value: 8.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530364544 774 PPP--------SPTTQRRPTLSAPlARPTSGRGPAPAIpspgPHSGAPPVPFRPG----PLPPFPSSSDSFGAPPQVPS 840
Cdd:PRK14959 398 PTPgtqgpqgtAPAAGMTPSSAAP-ATPAPSAAPSPRV----PWDDAPPAPPRSGipprPAPRMPEASPVPGAPDSVAS 471
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
723-840 8.45e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 8.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 723 AEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPVDdswiqhsrRSPPPSPTTQRRP-TLSAPLARPTSGRGPAP 801
Cdd:PRK12323 420 AAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAA--------AARPAAAGPRPVAaAAAAAPARAAPAAAPAP 491

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530364544 802 AIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPS 840
Cdd:PRK12323 492 ADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPA 530
PHA03369 PHA03369
capsid maturational protease; Provisional
 703-843 9.79e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 39.60  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364544 703 SELLAQLYSSEDQnTLMEESAEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPvddswIQHSRRSPPPSPTTQR 782
Cdd:PHA03369 309 YKLLRTIYKHKDE-TVIEQYLIEGRKLFSTINGLKAHNEILKTASLTAPSRVLAAAAKV-----AVIAAPQTHTGPADRQ 382

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530364544 783 RPtlSAPLARPTSgrgpapaIPSPGPHSGAPPVPF---RPGPLPPFPSSSDSFGAPPQ----VPSRPT 843
Cdd:PHA03369 383 RP--QRPDGIPYS-------VPARSPMTAYPPVPQfcgDPGLVSPYNPQSPGTSYGPEpvgpVPPQPT 441
 
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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