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Conserved domains on  [gi|755497120|ref|XP_006497713|]
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dynamin-1 isoform X2 [Mus musculus]

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 3.24e-154

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: 451.64  E-value: 3.24e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120     6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120    86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120   166 KENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGK 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 9.23e-148

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: 436.56  E-value: 9.23e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 755497120  455 EMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 520-629 1.05e-83

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: 263.03  E-value: 1.05e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 520 VIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKD 599
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 755497120 600 YRQLELACETQEEVDSWKASFLRAGVYPER 629
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
655-745 5.57e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 125.32  E-value: 5.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  655 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 755497120  735 LKEALSIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 747-864 3.43e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  747 TTTVSTPMPPPVDDSWLQVQSVPAG---------RRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPS 817
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755497120  818 RPGASPDPF-GPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PHA03247 2910 QPQAPPPPQpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 3.24e-154

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: 451.64  E-value: 3.24e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120     6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120    86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120   166 KENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGK 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 7.17e-149

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: 439.37  E-value: 7.17e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFLHCKGKKFTDFEEVRLE 100
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSD 180
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 181 LANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERK 257
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755497120 258 FFLSHPSYRHL-ADRMGTPYLQKVLNQQLTNHIRDTLP 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 9.23e-148

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: 436.56  E-value: 9.23e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 755497120  455 EMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 520-629 1.05e-83

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: 263.03  E-value: 1.05e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 520 VIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKD 599
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 755497120 600 YRQLELACETQEEVDSWKASFLRAGVYPER 629
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 2.20e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 221.34  E-value: 2.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120   34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFlhckGKKFTDFEEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  106 DRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQppdiefqirDMLMQFVtKENCLILAVSPANSDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 755497120  186 ALKIAKEVDPQGQRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 5.57e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 125.32  E-value: 5.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  655 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 755497120  735 LKEALSIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 8.65e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 107.71  E-value: 8.65e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120   654 QLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYH 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 755497120   734 ALKEALSIIGDI 745
Cdd:smart00302  81 LLKKARQIIAAV 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 520-623 1.28e-11

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 61.81  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  520 VIRKGWLTINNIGImKGGSKEYWFVLTAENLSWYKDD---EEKEKKYMLSVDNLKLRDVEKGFMSS-KHIFALFNTEQRN 595
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 755497120  596 VykdyRQLELACETQEEVDSWKASFLRA 623
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 520-623 2.52e-11

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: 61.03  E-value: 2.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120   520 VIRKGWLTINNIGiMKGGSKEYWFVLTAENLSWYKDDEEKEK---KYMLSVDNLKLRDVEKGFMSS-KHIFALfnteqrn 595
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 755497120   596 VYKDYRQLELACETQEEVDSWKASFLRA 623
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-864 3.43e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  747 TTTVSTPMPPPVDDSWLQVQSVPAG---------RRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPS 817
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755497120  818 RPGASPDPF-GPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PHA03247 2910 QPQAPPPPQpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 746-861 6.71e-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: 45.36  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  746 NTTTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgpppagsalGGAPPVPSRPGasPDP 825
Cdd:pfam15822  52 STAPSTVPFGPAPTGMY---PSIPLTGPSPGPPAPFPPSGPSCPPP------------------GGPYPAPTVPG--PGP 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 755497120  826 FGPPPQvpsrPNRAPPGVPSRKGpaSPTRPAAPRPT 861
Cdd:pfam15822 109 IGPYPT----PNMPFPELPRPYG--APTDPAAAAPS 138
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 752-860 1.60e-04

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


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 44.76  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:NF040712 218 EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAP 297

                         90       100
                 ....*....|....*....|....*....
gi 755497120 832 VPSRPnrAPPGVPSRKGPASPTRPAAPRP 860
Cdd:NF040712 298 APAAP--AAPAAPEAEEPARPEPPPAPKP 324
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 748-862 2.51e-04

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


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 44.37  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 748 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTS-SPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 826
Cdd:NF040712 200 ATVPRLAREPADARPEEVEPAPAAEGAPATdSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755497120 827 GPPPQVPSRPNRAPPGVPSrkgPASPTRPAAPRPTE 862
Cdd:NF040712 280 PPAPGAAETPEAAEPPAPA---PAAPAAPAAPEAEE 312
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 762-864 3.18e-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: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 762 WLQVQSvpAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPP 841
Cdd:NF041121  10 WLAAQM--GRAAAPPSPEGPAPTAASQPATPPPPA--------------APPSPPGDPPEPPAPEPAPLPAPYPGSLAPP 73

                         90       100
                 ....*....|....*....|...
gi 755497120 842 GVPSRKgpASPTRPAAPRPTEAP 864
Cdd:NF041121  74 PPPPPG--PAGAAPGAALPVRVP 94
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 747-864 3.65e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 40.82  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 747 TTTVSTPMPPPVDDSWlQVQSVPAGRRSPTSSPT---------PQRRAPAVPPARPGSRGPAPGpppagsalggAPPV-- 815
Cdd:COG5180  247 ATVDAQPEMRPPADAK-ERRRAAIGDTPAAEPPGlpvleagsePQSDAPEAETARPIDVKGVAS----------APPAtr 315

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755497120 816 PSRP-GASPDPFGP-PPQVPSRPNRAPP------GVPSRKGPASPTRPAAPRPTEAP 864
Cdd:COG5180  316 PVRPpGGARDPGTPrPGQPTERPAGVPEaasdagQPPSAYPPAEEAVPGKPLEQGAP 372
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 3.24e-154

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: 451.64  E-value: 3.24e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120     6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120    86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120   166 KENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGK 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 7.17e-149

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: 439.37  E-value: 7.17e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFLHCKGKKFTDFEEVRLE 100
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSD 180
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 181 LANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERK 257
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755497120 258 FFLSHPSYRHL-ADRMGTPYLQKVLNQQLTNHIRDTLP 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 9.23e-148

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: 436.56  E-value: 9.23e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 755497120  455 EMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 520-629 1.05e-83

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: 263.03  E-value: 1.05e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 520 VIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKD 599
Cdd:cd01256    3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 755497120 600 YRQLELACETQEEVDSWKASFLRAGVYPER 629
Cdd:cd01256   83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 2.20e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 221.34  E-value: 2.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120   34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFlhckGKKFTDFEEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  106 DRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQppdiefqirDMLMQFVtKENCLILAVSPANSDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 755497120  186 ALKIAKEVDPQGQRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 5.57e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 125.32  E-value: 5.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  655 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 755497120  735 LKEALSIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 8.65e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 107.71  E-value: 8.65e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120   654 QLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYH 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 755497120   734 ALKEALSIIGDI 745
Cdd:smart00302  81 LLKKARQIIAAV 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 520-623 1.28e-11

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 61.81  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  520 VIRKGWLTINNIGImKGGSKEYWFVLTAENLSWYKDD---EEKEKKYMLSVDNLKLRDVEKGFMSS-KHIFALFNTEQRN 595
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 755497120  596 VykdyRQLELACETQEEVDSWKASFLRA 623
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 520-623 2.52e-11

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: 61.03  E-value: 2.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120   520 VIRKGWLTINNIGiMKGGSKEYWFVLTAENLSWYKDDEEKEK---KYMLSVDNLKLRDVEKGFMSS-KHIFALfnteqrn 595
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 755497120   596 VYKDYRQLELACETQEEVDSWKASFLRA 623
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 522-616 1.10e-09

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: 56.01  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 522 RKGWLTINNIGIMKGGsKEYWFVLTAENLSWYKDDEEKEKKYMLSVD---NLKLRDVEKGfmSSKHIFALFNTEQRNVYk 598
Cdd:cd00821    1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPKGSIPlsgILEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                         90
                 ....*....|....*...
gi 755497120 599 dyrqleLACETQEEVDSW 616
Cdd:cd00821   77 ------LQADSEEERQEW 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-864 3.43e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  747 TTTVSTPMPPPVDDSWLQVQSVPAG---------RRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPS 817
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755497120  818 RPGASPDPF-GPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PHA03247 2910 QPQAPPPPQpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
PHA03378 PHA03378
EBNA-3B; Provisional
 763-864 5.40e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 57.00  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 763 LQVQSVPAGRRSPTSSPTPQrRAPAVPPARPGSRGPAPGPPPAGSalgGAPPVPSRPGASPDPFGPPPQVPSRPnRAPPG 842
Cdd:PHA03378 685 LPIQWAPGTMQPPPRAPTPM-RPPAAPPGRAQRPAAATGRARPPA---AAPGRARPPAAAPGRARPPAAAPGRA-RPPAA 759

                         90       100
                 ....*....|....*....|..
gi 755497120 843 VPSRKGPASPTrPAAPRPTEAP 864
Cdd:PHA03378 760 APGRARPPAAA-PGAPTPQPPP 780
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-867 9.70e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 9.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  751 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSalggAPPVPSRPGASPDPFG--- 827
Cdd:PHA03247 2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS----SPPQRPRRRAARPTVGslt 2696

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755497120  828 ----PPPQVP---SRPNRAPPGVPSRKG--------PASPTRPAAPRPTEAPLLD 867
Cdd:PHA03247 2697 sladPPPPPPtpePAPHALVSATPLPPGpaaarqasPALPAAPAPPAVPAGPATP 2751
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 755-863 3.43e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.22  E-value: 3.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 755 PPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPS 834
Cdd:PRK07764 681 PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760

                         90       100
                 ....*....|....*....|....*....
gi 755497120 835 RPNRAPPGVPSRKGPASPTRPAAPRPTEA 863
Cdd:PRK07764 761 PPAPAPAAAPAAAPPPSPPSEEEEMAEDD 789
PHA03378 PHA03378
EBNA-3B; Provisional
 752-861 5.56e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 53.53  E-value: 5.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 752 TPMPPPvddswlqvQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG---- 827
Cdd:PHA03378 702 TPMRPP--------AAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAapga 773

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755497120 828 ----PPPQVP----SRPNRAPPGVPSRKGPASPTRPAAPRPT 861
Cdd:PHA03378 774 ptpqPPPQAPpapqQRPRGAPTPQPPPQAGPTSMQLMPRAAP 815
PHA03247 PHA03247
large tegument protein UL36; Provisional
 728-862 1.38e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  728 MLRMYHALKEALSIIGDINTTTVSTPMPPPVDDswlqvQSVPagrrspTSSPTPQRRAPAVPpARPGSRgpapgpppags 807
Cdd:PHA03247 2533 MLTWIRGLEELASDDAGDPPPPLPPAAPPAAPD-----RSVP------PPRPAPRPSEPAVT-SRARRP----------- 2589

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755497120  808 algGAPPVPSRPGASPDPFGPPPQvPSRPNRAPPGVPSRKGPASPTRPAAPRPTE 862
Cdd:PHA03247 2590 ---DAPPQSARPRAPVDDRGDPRG-PAPPSPLPPDTHAPDPPPPSPSPAANEPDP 2640
PHA03378 PHA03378
EBNA-3B; Provisional
 751-864 2.90e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 51.22  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 751 STPMPPPvddswlqvqSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPP 830
Cdd:PHA03378 692 GTMQPPP---------RAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPG 762

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755497120 831 QVP---SRPNRAPPGVPSRKGPASPTRP-AAPRPTEAP 864
Cdd:PHA03378 763 RARppaAAPGAPTPQPPPQAPPAPQQRPrGAPTPQPPP 800
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 751-868 3.48e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 50.87  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 751 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPP 830
Cdd:PRK14951 379 KTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPE 458

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755497120 831 QVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAPLLDL 868
Cdd:PRK14951 459 TVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGDV 496
PHA03378 PHA03378
EBNA-3B; Provisional
 751-850 4.14e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.84  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 751 STPMPPPvddswlqvQSVPAGRRSPTSSPTPQRrAPAVPPARPGSRGPAPGPPPAGSALGGAP---------PVP-SRPG 820
Cdd:PHA03378 721 TGRARPP--------AAAPGRARPPAAAPGRAR-PPAAAPGRARPPAAAPGRARPPAAAPGAPtpqpppqapPAPqQRPR 791

                         90       100       110
                 ....*....|....*....|....*....|.
gi 755497120 821 ASPDPFgPPPQVPSRPNR-APPGVPSRKGPA 850
Cdd:PHA03378 792 GAPTPQ-PPPQAGPTSMQlMPRAAPGQQGPT 821
PHA03247 PHA03247
large tegument protein UL36; Provisional
 765-863 4.21e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  765 VQSVPAGRRSPTSSPTPQRRAPAVPPARP--GSRGPAPGPPPAGSALGGAPPVPSRPG----ASPDPFGPPP--QVPSRP 836
Cdd:PHA03247  365 LEDLSAGRHHPKRASLPTRKRRSARHAATpfARGPGGDDQTRPAAPVPASVPTPAPTPvpasAPPPPATPLPsaEPGSDD 444

                          90       100
                  ....*....|....*....|....*..
gi 755497120  837 NRAPPgvPSRKGPASPTRPAAPRPTEA 863
Cdd:PHA03247  445 GPAPP--PERQPPAPATEPAPDDPDDA 469
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 520-616 4.54e-06

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: 46.54  E-value: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 520 VIRKGWLTinnigiMKGGS----KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKgfMSSKHIFALFNTEQRN 595
Cdd:cd01252    3 PDREGWLL------KLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755497120 596 VYKD----------------YRqleLACETQEEVDSW 616
Cdd:cd01252   75 VIKAcktdsdgkvvegnhtvYR---ISAASEEERDEW 108
PHA03247 PHA03247
large tegument protein UL36; Provisional
 753-865 5.34e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  753 PMPPPVDDSwlqVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPppagsalGGAPPVPSRPGASPDPFGPP-PQ 831
Cdd:PHA03247 2683 PRRRAARPT---VGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAAR-------QASPALPAAPAPPAVPAGPAtPG 2752

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 755497120  832 VPSRPNR-----APPGVPSRKGPASPTRPAAPRPTEAPL 865
Cdd:PHA03247 2753 GPARPARppttaGPPAPAPPAAPAAGPPRRLTRPAVASL 2791
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 769-866 1.36e-05

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 48.80  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 769 PAGRRSPTSSPTPQRRaPAVPPA---RPGSRGPAPGPPPAGSALGGA---------PPVPSRPGASPDPF----GPPPQV 832
Cdd:PHA03321 434 PAPRRDNDPPPPPRAR-PGSTPAcarRARAQRARDAGPEYVDPLGALrrlpagaapPPEPAAAPSPATYYtrmgGGPPRL 512

                         90       100       110
                 ....*....|....*....|....*....|....
gi 755497120 833 PSRpNRAPpgvPSRKGPASPTRPAAPRPTEAPLL 866
Cdd:PHA03321 513 PPR-NRAT---ETLRPDWGPPAAAPPEQMEDPYL 542
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 752-864 1.38e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.83  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:PRK07764 598 EGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAA 677

                         90       100       110
                 ....*....|....*....|....*....|...
gi 755497120 832 VPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PRK07764 678 PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP 710
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
 539-616 2.58e-05

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: 43.77  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 539 KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNL----KLRDVEKgfmssKHIFALFnTEQRNVYkdyrqleLACETQEEVD 614
Cdd:cd13298   23 KKRWVVLRPCQLSYYKDEKEYKLRRVINLSELlavaPLKDKKR-----KNVFGIY-TPSKNLH-------FRATSEKDAN 89


                 ..
gi 755497120 615 SW 616
Cdd:cd13298   90 EW 91
PHA03247 PHA03247
large tegument protein UL36; Provisional
 750-855 3.43e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  750 VSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAP-PVPSRPGASPDPFG- 827
Cdd:PHA03247 2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPaGAGEPSGAVPQPWLg 2965

                          90       100       110
                  ....*....|....*....|....*....|
gi 755497120  828 --PPPQVPSRPNRAPPGVPSRKGPASPTRP 855
Cdd:PHA03247 2966 alVPGRVAVPRFRVPQPAPSREAPASSTPP 2995
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
 520-622 4.78e-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: 43.40  E-value: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 520 VIRKGWLTINNiGIMKGGsKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMS-SKHIFALF---NTEQRN 595
Cdd:cd13378    3 VLKAGWLKKQR-SIMKNW-QQRWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNELPPNPEEpGKHLFEILpggAGDREK 80

                         90       100
                 ....*....|....*....|....*..
gi 755497120 596 VYKDYRQLELACETQEEVDSWKASFLR 622
Cdd:cd13378   81 VPMNHEAFLLMANSQSDMEDWVKAIRR 107
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
728-864 5.18e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.79  E-value: 5.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 728 MLRMYhalkeALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAV-PPARPGSRGPAPG----- 801
Cdd:PRK12323 357 LLRML-----AFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAaAAARAVAAAPARRspape 431

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755497120 802 -----PPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRkgPASPTRPAAPRPTEAP 864
Cdd:PRK12323 432 alaaaRQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPA--RAAPAAAPAPADDDPP 497
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 746-861 6.71e-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: 45.36  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  746 NTTTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgpppagsalGGAPPVPSRPGasPDP 825
Cdd:pfam15822  52 STAPSTVPFGPAPTGMY---PSIPLTGPSPGPPAPFPPSGPSCPPP------------------GGPYPAPTVPG--PGP 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 755497120  826 FGPPPQvpsrPNRAPPGVPSRKGpaSPTRPAAPRPT 861
Cdd:pfam15822 109 IGPYPT----PNMPFPELPRPYG--APTDPAAAAPS 138
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 753-864 1.14e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.93  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  753 PMPPPVDD---SWLQVQSVPAGRRSPTSSP--TPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAP---PVPSRPGASPD 824
Cdd:PHA03307  258 PRPAPITLptrIWEASGWNGPSSRPGPASSssSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSREsssSSTSSSSESSR 337

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 755497120  825 PFG-PPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PHA03307  338 GAAvSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSP 378
PHA03247 PHA03247
large tegument protein UL36; Provisional
 752-865 1.48e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  752 TPMPPPVDDSwlqvQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrGPAPGPPPAGSALGGAPPVPSRPGA-SPDPFGPPP 830
Cdd:PHA03247 2738 APAPPAVPAG----PATPGGPARPARPPTTAGPPAPAPPA-----APAAGPPRRLTRPAVASLSESRESLpSPWDPADPP 2808

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 755497120  831 QVPSRPNRAPPGVPSRKGPASPT---RPAAPRPTEAPL 865
Cdd:PHA03247 2809 AAVLAPAAALPPAASPAGPLPPPtsaQPTAPPPPPGPP 2846
PHA03247 PHA03247
large tegument protein UL36; Provisional
 752-864 1.58e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  752 TPMPPPvdDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPFGP-PP 830
Cdd:PHA03247 2707 TPEPAP--HALVSATPLPPGPAAARQASPALPAAPAPPAV------------PAGPATPGGPARPARPPTTAGPPAPaPP 2772

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 755497120  831 QVPSR--PNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PHA03247 2773 AAPAAgpPRRLTRPAVASLSESRESLPSPWDPADPP 2808
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 752-860 1.60e-04

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


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 44.76  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:NF040712 218 EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAP 297

                         90       100
                 ....*....|....*....|....*....
gi 755497120 832 VPSRPnrAPPGVPSRKGPASPTRPAAPRP 860
Cdd:NF040712 298 APAAP--AAPAAPEAEEPARPEPPPAPKP 324
PHA03247 PHA03247
large tegument protein UL36; Provisional
 757-868 1.86e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  757 PVDDSwlqvqsvPAGRRSPTSSPTPQRRAPAVPPArpgsrgpaPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVpSRP 836
Cdd:PHA03247 2601 PVDDR-------GDPRGPAPPSPLPPDTHAPDPPP--------PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRV-SRP 2664

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755497120  837 NRA-PPGVPSRKG--PASPTRPAAPrPTEAPLLDL 868
Cdd:PHA03247 2665 RRArRLGRAAQASspPQRPRRRAAR-PTVGSLTSL 2698
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 520-616 2.26e-04

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: 41.10  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 520 VIRKGWLTinnigiMKGGS-----KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGF-MSSKHIFALFNTEQ 593
Cdd:cd13248    7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                         90       100
                 ....*....|....*....|...
gi 755497120 594 RNVYkdyrqleLACETQEEVDSW 616
Cdd:cd13248   81 RTYY-------FAADTAEEMEQW 96
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 751-864 2.28e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  751 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAV---PPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 827
Cdd:PHA03307  805 SGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAarpPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPG 884

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 755497120  828 PPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PHA03307  885 AAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPMPPGGP 921
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 748-862 2.51e-04

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


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 44.37  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 748 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTS-SPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 826
Cdd:NF040712 200 ATVPRLAREPADARPEEVEPAPAAEGAPATdSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755497120 827 GPPPQVPSRPNRAPPGVPSrkgPASPTRPAAPRPTE 862
Cdd:NF040712 280 PPAPGAAETPEAAEPPAPA---PAAPAAPAAPEAEE 312
PHA03247 PHA03247
large tegument protein UL36; Provisional
 766-864 2.88e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  766 QSVPAGRRSPTSSPTPQRRAPAV----------PPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPqvPSR 835
Cdd:PHA03247 2670 LGRAAQASSPPQRPRRRAARPTVgsltsladppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV--PAG 2747

                          90       100       110
                  ....*....|....*....|....*....|
gi 755497120  836 PnrAPPGVPSRKG-PASPTRPAAPRPTEAP 864
Cdd:PHA03247 2748 P--ATPGGPARPArPPTTAGPPAPAPPAAP 2775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-866 3.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  748 TTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQrrAPAVP--PARPgsrgpapgpppagsalgGAPPVPS---RPGAS 822
Cdd:PHA03247 2715 LVSATPLPPGPAAAR---QASPALPAAPAPPAVPA--GPATPggPARP-----------------ARPPTTAgppAPAPP 2772

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 755497120  823 PDPFGPPPQVPSRPNRAP--PGVPSRKGPASPTRPAAPRPTEAPLL 866
Cdd:PHA03247 2773 AAPAAGPPRRLTRPAVASlsESRESLPSPWDPADPPAAVLAPAAAL 2818
PHA03247 PHA03247
large tegument protein UL36; Provisional
 753-864 3.47e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  753 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPQrrAPAVPPArpgsrgpapgPPPAGSALGGA-------------------P 813
Cdd:PHA03247 2808 PAAVLAPAAALPPAASPAGPLPPPTSAQPT--APPPPPG----------PPPPSLPLGGSvapggdvrrrppsrspaakP 2875

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755497120  814 PVPSRPGA----------SPDPFGPPPQVPSRPnrAPPGVPSRKGPaSPTRPAAPRPTEAP 864
Cdd:PHA03247 2876 AAPARPPVrrlarpavsrSTESFALPPDQPERP--PQPQAPPPPQP-QPQPPPPPQPQPPP 2933
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 710-860 3.81e-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: 44.37  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  710 DQNTLMEESAEQA--QRRDEMLRMYHALKEALSIiGDINTTTVSTPMPPPvddswlQVQSVPAgRRSPTSSPTPQRRAPA 787
Cdd:pfam03154 153 DNESDSDSSAQQQilQTQPPVLQAQSGAASPPSP-PPPGTTQAATAGPTP------SAPSVPP-QGSPATSQPPNQTQST 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  788 VPPARPGSRGPAPGPPPAgsalggapPVPSRPGASPDPFGPPPQVPSRPNRAPP--------GVPSRKGPASPTRPAAPR 859
Cdd:pfam03154 225 AAPHTLIQQTPTLHPQRL--------PSPHPPLQPMTQPPPPSQVSPQPLPQPSlhgqmppmPHSLQTGPSHMQHPVPPQ 296


                  .
gi 755497120  860 P 860
Cdd:pfam03154 297 P 297
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 769-858 3.82e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.30  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 769 PAGRRSPTSSPTPQRraPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPFGP-PPQVPSRPNRaPPGVPSRK 847
Cdd:PTZ00449 591 PEEPKKPKRPRSAQR--PTRPKS------------PKLPELLDIPKSPKRPESPKSPKRPpPPQRPSSPER-PEGPKIIK 655

                         90
                 ....*....|.
gi 755497120 848 GPASPTRPAAP 858
Cdd:PTZ00449 656 SPKPPKSPKPP 666
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
750-864 4.49e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.10  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 750 VSTPMPPPVDDSWLQVQsvPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPppagsaLGGAPPVPSRPGASPDPFGPP 829
Cdd:PRK12323 451 APAPAAAPAAAARPAAA--GPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEE------LPPEFASPAPAQPDAAPAGWV 522

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755497120 830 PQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PRK12323 523 AESIPDPATADPDDAFETLAPAPAAAPAPRAAAAT 557
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 752-866 4.52e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 4.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGsrgpapgpppagsalGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:PRK07764 708 TPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPD---------------PAGAPAQPPPPPAPAPAAAPAA 772

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755497120 832 VPSRPNRAPPGVPsrkgPASPTRPAAPRPTEAPLL 866
Cdd:PRK07764 773 APPPSPPSEEEEM----AEDDAPSMDDEDRRDAEE 803
Gag_MA pfam01140
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
 773-849 5.87e-04

Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity.


Pssm-ID: 426076 [Multi-domain]  Cd Length: 126  Bit Score: 40.83  E-value: 5.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755497120  773 RSPTSSPTPQRRAPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPfgPPPQVPSRPNRAPPGvPSRKGP 849
Cdd:pfam01140  64 KTRVFAPGPHGHPDQVPYI------------VTWEALAADPPPWVRPFLTPKP--PPPQPPAAPGLRPPL-PPASAP 125
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-859 5.91e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 5.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  747 TTTVSTPMPP--PVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSalGGAPPVPSRPGASPD 824
Cdd:PHA03247 2763 TAGPPAPAPPaaPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA--GPLPPPTSAQPTAPP 2840

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 755497120  825 PFGPPPQVPSRP--NRAPPGVPSRKGP--ASPTRPAAPR 859
Cdd:PHA03247 2841 PPPGPPPPSLPLggSVAPGGDVRRRPPsrSPAAKPAAPA 2879
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 775-859 7.96e-04

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 41.90  E-value: 7.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  775 PTSSPTPQrraPAVPPARPGsrgpapgpppagsalGGAPPVP---------SRPGASPDPFG--PPPQV-PSRPNraPPG 842
Cdd:pfam15822 163 PYPSPGPY---PAVPPPQSP---------------GAAPPVPwgtvppgpwGPPAPYPDPTGsyPMPGLyPTPNN--PFQ 222

                          90
                  ....*....|....*...
gi 755497120  843 VPSrkGPA-SPTRPAAPR 859
Cdd:pfam15822 223 VPS--GPSgAPPMPGGPH 238
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
 516-562 8.13e-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: 39.97  E-value: 8.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755497120 516 DEIL--VIRKGWLtinnigiMKGGSK-----EYWFVLTAENLSWYKDDEEKEKK 562
Cdd:cd13273    2 DELIldVIKKGYL-------WKKGHLlptwtERWFVLKPNSLSYYKSEDLKEKK 48
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 769-864 8.34e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.14  E-value: 8.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 769 PAGRRSPTSSPTPQRRAPAVPPARpgsrgpapgpppagsalggaPPVPSRPGASPDPFGPP-PQVPSRPNRAPPgvPSRk 847
Cdd:PTZ00449 585 PKHPKDPEEPKKPKRPRSAQRPTR--------------------PKSPKLPELLDIPKSPKrPESPKSPKRPPP--PQR- 641

                         90
                 ....*....|....*..
gi 755497120 848 gPASPTRPAAPRPTEAP 864
Cdd:PTZ00449 642 -PSSPERPEGPKIIKSP 657
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
774-864 9.98e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.91  E-value: 9.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 774 SPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPT 853
Cdd:PRK07003 405 AAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDA 484

                         90
                 ....*....|.
gi 755497120 854 RPAAPRPTEAP 864
Cdd:PRK07003 485 PPDAAFEPAPR 495
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-865 1.07e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  748 TTVSTPMPPPvddswlqvqSVPAGRRSPTSSPTPQRRAPAV-------PPARPGSRGPAPGPPpagsalggAPPVPSRPG 820
Cdd:PHA03247 2696 TSLADPPPPP---------PTPEPAPHALVSATPLPPGPAAarqaspaLPAAPAPPAVPAGPA--------TPGGPARPA 2758

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755497120  821 ASPDPFGPPpqvPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAPL 865
Cdd:PHA03247 2759 RPPTTAGPP---APAPPAAPAAGPPRRLTRPAVASLSESRESLPS 2800
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 715-867 1.29e-03

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: 41.84  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  715 MEESAEQAQRRdemlrmyHALKEALSIIGDINTTTVSTPMPppvddSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPArpg 794
Cdd:pfam07174   1 MDQVDPNSTRR-------KGLWATLAIAAVAGASAVAVALP-----AVAHADPEPAPPPPSTATAPPAPPPPPPAPA--- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755497120  795 srGPAPGPPPAGSALGGAPPVPSRPGASP----DPFGPPPQvPSRPNRAPPG-VPSRKGPASPTRPAAPRPTEAPLLD 867
Cdd:pfam07174  66 --APAPPPPPAAPNAPNAPPPPADPNAPPpppaDPNAPPPP-AVDPNAPEPGrIDNAVGGFSYVVPAGWVESDATHLD 140
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 752-865 1.58e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  752 TPMPPPVddswlqvqsvPAGRRSPTSSPTPQRRAPaVPParpgsrgpapgpppAGSALGGAPPVPSRPGAsPDPFGPPP- 830
Cdd:pfam03154 250 QPMTQPP----------PPSQVSPQPLPQPSLHGQ-MPP--------------MPHSLQTGPSHMQHPVP-PQPFPLTPq 303

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755497120  831 ----QVPSRPNRAPPGVPSRKGPASPTRPAAPR---PTEAPL 865
Cdd:pfam03154 304 ssqsQVPPGPSPAAPGQSQQRIHTPPSQSQLQSqqpPREQPL 345
PHA03247 PHA03247
large tegument protein UL36; Provisional
 771-864 1.68e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  771 GRRSPTSSPTPQRRAPA----------VPPaRPGSRGPAPGPPPAGSALGGAPPV-PSRPGASPDPFGPPPQ-------- 831
Cdd:PHA03247 2502 GPPDPDAPPAPSRLAPAilpdepvgepVHP-RMLTWIRGLEELASDDAGDPPPPLpPAAPPAAPDRSVPPPRpaprpsep 2580

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755497120  832 ----------VPSRPNR-----APPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PHA03247 2581 avtsrarrpdAPPQSARprapvDDRGDPRGPAPPSPLPPDTHAPDPPP 2628
PHA03247 PHA03247
large tegument protein UL36; Provisional
 779-864 1.68e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  779 PTPQRRAPAVPPARPGSRGPAPGPPPAGSalGGAPPVPSRpGASPDPFGPPPQVPSRPNRAPPGV--PSRKGpASPTRPA 856
Cdd:PHA03247  236 PFVERRVVISHPLRGDIAAPAPPPVVGEG--ADRAPETAR-GATGPPPPPEAAAPNGAAAPPDGVwgAALAG-APLALPA 311


                  ....*...
gi 755497120  857 APRPTEAP 864
Cdd:PHA03247  312 PPDPPPPA 319
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 756-864 2.09e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  756 PPVddswLQVQSVPAGRRSP-------TSSPTPQRRAPAVPPArpgsrgpapgpppagsalgGAPPVPSRPGASPDPFGP 828
Cdd:pfam03154 171 PPV----LQAQSGAASPPSPpppgttqAATAGPTPSAPSVPPQ-------------------GSPATSQPPNQTQSTAAP 227

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 755497120  829 PPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:pfam03154 228 HTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP 263
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
 772-865 2.17e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 41.03  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 772 RRSPTSSPTPQRRAPavPPARPGSRGPAPGPPPagsalggAPPVPSRPGASPDP--FGPPPQVPSRPNRAPPGVPSrkGP 849
Cdd:PHA03201   2 KRARSRSPSPPRRPS--PPRPTPPRSPDASPEE-------TPPSPPGPGAEPPPgrAAGPAAPRRRPRGCPAGVTF--SS 70

                         90       100
                 ....*....|....*....|.
gi 755497120 850 ASPTRPA-----APRPTEAPL 865
Cdd:PHA03201  71 SAPPRPPlglddAPAATPPPL 91
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 749-865 2.26e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 41.00  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 749 TVSTPMPPPVDDSWLQVQSVP-AGR----RSPTSSPTPQRR------APAVPPARPGSRGPAPgpppagsalggAPP--V 815
Cdd:PHA02682  36 APAAPCPPDADVDPLDKYSVKeAGRyyqsRLKANSACMQRPsgqsplAPSPACAAPAPACPAC-----------APAapA 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755497120 816 PSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASP--TR---PAAPRPTEAPL 865
Cdd:PHA02682 105 PAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPpsTRqcpPAPPLPTPKPA 159
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 733-864 2.30e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  733 HALKEALSIIGDINTTTVSTPMPPPVDDSWLqvqsVPAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalGGA 812
Cdd:PHA03307   48 AELAAVTVVAGAAACDRFEPPTGPPPGPGTE----APANESRSTPTWSLSTLAPASPAREGSPT-------------PPG 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755497120  813 PPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PHA03307  111 PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAV 162
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 749-858 2.31e-03

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


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 39.47  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  749 TVSTPMPPPVddswlqvqsvPAGRRSPTSSPTPQrrAPAVPPARPGSRGPapgpppagsalgGAPPVPSRPGASPDPfGP 828
Cdd:pfam06346  42 SAAIPPPPPL----------PGGTSIPPPPPLPG--AASIPPPPPLPGST------------GIPPPPPLPGGAGIP-PP 96

                          90       100       110
                  ....*....|....*....|....*....|
gi 755497120  829 PPQVPSRPNRAPPGVPSRKGPASPTRPAAP 858
Cdd:pfam06346  97 PPPLPGGAGVPPPPPPLPGGPGIPPPPPFP 126
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 753-863 2.48e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  753 PMPPPVDDSWLQVQSVPA-GRRSPTSSPTP--QRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPP 829
Cdd:PHA03307  126 PPPSPAPDLSEMLRPVGSpGPPPAASPPAAgaSPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPR 205

                          90       100       110
                  ....*....|....*....|....*....|....
gi 755497120  830 PQVPSRPNRAPPGVPsrkGPASPTRPAAPRPTEA 863
Cdd:PHA03307  206 PPRRSSPISASASSP---APAPGRSAADDAGASS 236
PHA02030 PHA02030
hypothetical protein
 753-858 2.78e-03

hypothetical protein


Pssm-ID: 222843 [Multi-domain]  Cd Length: 336  Bit Score: 40.73  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 753 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARpgsrgpapgpppagsalgGAPPVPSRPGASpdpfgPPPQV 832
Cdd:PHA02030 254 IIKPKSKAAGSNLPAVPNVAADAGSAAAPAVPAAAAAVAQ------------------AAPSVPQVPNVA-----VLPDV 310

                         90       100
                 ....*....|....*....|....*.
gi 755497120 833 PSRPNRAPPGVPsrKGPASPTRPAAP 858
Cdd:PHA02030 311 PQVAPVAAPAAP--EVPAVPVVPAAP 334
DUF4813 pfam16072
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ...
 747-846 2.80e-03

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: 40.51  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  747 TTTVSTPMPPPVDDSWLQVQSVPAG--RRSPTSSPTPQRRAPAVP--PARPGSRGPAPGPPPAGSALGGAP------PVP 816
Cdd:pfam16072 158 TTVINAGGQQPAAPAAPAYPVAPAAypAQAPAAAPAPAPGAPQTPlaPLNPVAAAPAAAAGAAAAPVVAAAapaaaaPPP 237

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 755497120  817 SRPGAsPDPFGPPPQ------VPSRPNRAPPGVPSR 846
Cdd:pfam16072 238 PAPAA-PPADAAPPApggiicVPVRVPEPDPKDATK 272
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 762-864 3.18e-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: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 762 WLQVQSvpAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPP 841
Cdd:NF041121  10 WLAAQM--GRAAAPPSPEGPAPTAASQPATPPPPA--------------APPSPPGDPPEPPAPEPAPLPAPYPGSLAPP 73

                         90       100
                 ....*....|....*....|...
gi 755497120 842 GVPSRKgpASPTRPAAPRPTEAP 864
Cdd:NF041121  74 PPPPPG--PAGAAPGAALPVRVP 94
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 747-864 3.65e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 40.82  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 747 TTTVSTPMPPPVDDSWlQVQSVPAGRRSPTSSPT---------PQRRAPAVPPARPGSRGPAPGpppagsalggAPPV-- 815
Cdd:COG5180  247 ATVDAQPEMRPPADAK-ERRRAAIGDTPAAEPPGlpvleagsePQSDAPEAETARPIDVKGVAS----------APPAtr 315

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755497120 816 PSRP-GASPDPFGP-PPQVPSRPNRAPP------GVPSRKGPASPTRPAAPRPTEAP 864
Cdd:COG5180  316 PVRPpGGARDPGTPrPGQPTERPAGVPEaasdagQPPSAYPPAEEAVPGKPLEQGAP 372
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 743-865 3.83e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  743 GDINTTTVSTPMPPPVDDSwlqvqsvpAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGAS 822
Cdd:PHA03307  107 TPPGPSSPDPPPPTPPPAS--------PPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSS 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 755497120  823 PD---PFGPPPQVPSRPNRAPPGVPSR-KGPASPTRPAAPRPTEAPL 865
Cdd:PHA03307  179 PEetaRAPSSPPAEPPPSTPPAAASPRpPRRSSPISASASSPAPAPG 225
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 747-860 3.93e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  747 TTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 826
Cdd:PHA03307   89 TWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAAS 168

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 755497120  827 GPPP----QVPSRPNRAPPGVPSRKGPASPTRPAAPRP 860
Cdd:PHA03307  169 SRQAalplSSPEETARAPSSPPAEPPPSTPPAAASPRP 206
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 766-864 3.93e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 766 QSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPpagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPS 845
Cdd:PRK07764 395 AAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPA-------PAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPA 467

                         90
                 ....*....|....*....
gi 755497120 846 RKGPASPTRPAAPRPTEAP 864
Cdd:PRK07764 468 PAPAAAPEPTAAPAPAPPA 486
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 725-863 4.03e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120  725 RDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSwlqvqSVPAGRRSPTSSPTPqrRAPAVPPARPGSRGPAPGPPP 804
Cdd:PHA03307  252 ENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSS-----SSPRERSPSPSPSSP--GSGPAPSSPRASSSSSSSRES 324

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755497120  805 AGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEA 863
Cdd:PHA03307  325 SSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAG 383
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 541-616 4.41e-03

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. 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: 269964  Cd Length: 121  Bit Score: 38.03  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 541 YWFVLTAENLS-W-YKDDEEKeKKYMLSVD-----NLKLRDVEKGFMSSKHIFAL-FNTEQRNVYKDYRQLE----LACE 608
Cdd:cd01263   23 RWCVLRGGYLSfWkYPDDEEK-KKPIGSIDltkciTEKVEPAPRELCARPNTFLLeTLRPAEDDDRDDTNEKirvlLSAD 101


                 ....*...
gi 755497120 609 TQEEVDSW 616
Cdd:cd01263  102 TKEERIEW 109
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 755-863 4.73e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 40.37  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 755 PPPVDDSwlqVQSVPAGRRSPTSSPTPQRRAPAvPPARPGsrgpapgpppagsalGGAPPVP---SRPGASPDPFGPPPQ 831
Cdd:PHA03264 266 PPPAPSG---GSPAPPGDDRPEAKPEPGPVEDG-APGRET---------------GGEGEGPepaGRDGAAGGEPKPGPP 326

                         90       100       110
                 ....*....|....*....|....*....|...
gi 755497120 832 VPSRPNRAPPGVPSRKG-PASPTRPAAPRPTEA 863
Cdd:PHA03264 327 RPAPDADRPEGWPSLEAiTFPPPTPATPAVPRA 359
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 766-864 4.82e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 766 QSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAgsalGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPS 845
Cdd:PRK07764 420 AAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPA----AAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA 495

                         90
                 ....*....|....*....
gi 755497120 846 RkgPASPTRPAAPRPTEAP 864
Cdd:PRK07764 496 A--PAAPAAPAGADDAATL 512
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 768-864 4.95e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 768 VPAGRRSPTSSPTPQR---RAPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVP 844
Cdd:PRK07764 387 VAGGAGAPAAAAPSAAaaaPAAAPAPA------------AAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAP 454

                         90       100
                 ....*....|....*....|
gi 755497120 845 SRKGPASPTRPAAPRPTEAP 864
Cdd:PRK07764 455 SPPPAAAPSAQPAPAPAAAP 474
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 753-867 5.46e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.84  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 753 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPqrrAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSR-PGASPDPfGPPPQ 831
Cdd:PHA02682  84 PSPACAAPAPACPACAPAAPAPAVTCPAP---APACPPATAPTCPPPAVCPAPARPAPACPPSTRQcPPAPPLP-TPKPA 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755497120 832 VPSRP-----NRAPPGVPSRKGPASPTRPAAprpteAPLLD 867
Cdd:PHA02682 160 PAAKPiflhnQLPPPDYPAASCPTIETAPAA-----SPVLE 195
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 811-864 6.65e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 38.48  E-value: 6.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755497120  811 GAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:pfam15240  71 GGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGP 124
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
748-864 7.76e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 7.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 748 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 827
Cdd:PRK07003 405 AAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDA 484

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755497120 828 PP-------PQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PRK07003 485 PPdaafepaPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPP 528
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
751-864 9.44e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 9.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 751 STPMPPPVDDSWLQVQSV---PAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 827
Cdd:PRK07003 421 TRAEAPPAAPAPPATADRgddAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPS 500

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755497120 828 PPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPTEAP 864
Cdd:PRK07003 501 AATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTP 537
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
752-864 9.53e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.47  E-value: 9.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497120 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRrAPAVPPArpgsrgpaPGPPPAGSALGGAPPVPSRPGA--SPDPFGPP 829
Cdd:PRK12323 427 SPAPEALAAARQASARGPGGAPAPAPAPAAAP-AAAARPA--------AAGPRPVAAAAAAAPARAAPAAapAPADDDPP 497

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755497120 830 PQVPSRPNRAPPGV-PSRKGPASPTRPAAPRPTEAP 864
Cdd:PRK12323 498 PWEELPPEFASPAPaQPDAAPAGWVAESIPDPATAD 533
 
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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