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Conserved domains on  [gi|1958759558|ref|XP_038960069|]
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dynamin-1 isoform X1 [Rattus norvegicus]

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 3.20e-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: 3.20e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558    6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558   86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  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 1958759558 215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958759558 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 1.21e-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: 1.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 520 VIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKD 599
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958759558 600 YRQLELACETQEEVDSWKASFLRAGVYPER 629
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
655-745 5.68e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 124.93  E-value: 5.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 655 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1958759558 735 LKEALSIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 747-864 2.87e-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: 58.03  E-value: 2.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  747 TTTVSTPMPPPVDDSWLQVQSVPAG---------RRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPS 817
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958759558  818 RPGASPDPF-GPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 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 3.20e-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: 3.20e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558    6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558   86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  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 7.64e-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: 438.99  E-value: 7.64e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFLHCKGKKFTDFEEVRLE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 181 LANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958759558 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 1958759558 215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958759558 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 1.21e-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: 1.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 520 VIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKD 599
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958759558 600 YRQLELACETQEEVDSWKASFLRAGVYPER 629
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 2.22e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 221.34  E-value: 2.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFlhckGKKFTDFEEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 106 DRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQppdiefqirDMLMQFVtKENCLILAVSPANSDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 1958759558 186 ALKIAKEVDPQGQRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 5.68e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 124.93  E-value: 5.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 655 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1958759558 735 LKEALSIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 9.17e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 107.32  E-value: 9.17e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  654 QLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYH 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1958759558  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 1958759558 520 VIRKGWLTINNIGImKGGSKEYWFVLTAENLSWYKDD---EEKEKKYMLSVDNLKLRDVEKGFMSS-KHIFALFNTEQRN 595
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1958759558 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 1958759558  520 VIRKGWLTINNIGiMKGGSKEYWFVLTAENLSWYKDDEEKEK---KYMLSVDNLKLRDVEKGFMSS-KHIFALfnteqrn 595
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1958759558  596 VYKDYRQLELACETQEEVDSWKASFLRA 623
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-864 2.87e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 2.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  747 TTTVSTPMPPPVDDSWLQVQSVPAG---------RRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPS 817
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958759558  818 RPGASPDPF-GPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:PHA03247  2910 QPQAPPPPQpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 746-861 3.52e-05

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 46.13  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 746 NTTTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgpppagsalGGAPPVPSRPGasPDP 825
Cdd:pfam15822  52 STAPSTVPFGPAPTGMY---PSIPLTGPSPGPPAPFPPSGPSCPPP------------------GGPYPAPTVPG--PGP 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759558 826 FGPPPQvpsrPNRAPPGVPSRKGpaSPTRPAAPRPS 861
Cdd:pfam15822 109 IGPYPT----PNMPFPELPRPYG--APTDPAAAAPS 138
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 752-860 1.59e-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: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:NF040712  218 EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAP 297

                          90       100
                  ....*....|....*....|....*....
gi 1958759558 832 VPSRPnrAPPGVPSRKGPASPTRPAAPRP 860
Cdd:NF040712  298 APAAP--AAPAAPEAEEPARPEPPPAPKP 324
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 748-864 2.03e-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: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 748 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTS-SPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 826
Cdd:NF040712  200 ATVPRLAREPADARPEEVEPAPAAEGAPATdSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958759558 827 GPPPQVPSRPNRAPPGVPSRKGPASPTRPAA---PRPSEAP 864
Cdd:NF040712  280 PPAPGAAETPEAAEPPAPAPAAPAAPAAPEAeepARPEPPP 320
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 747-864 1.60e-03

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 41.97  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 747 TTTVSTPMPPPVDDSWlQVQSVPAGRRSPTSSPT---------PQRRAPAVPPARPGSRGPAPGpppagsalggAPPV-- 815
Cdd:COG5180   247 ATVDAQPEMRPPADAK-ERRRAAIGDTPAAEPPGlpvleagsePQSDAPEAETARPIDVKGVAS----------APPAtr 315

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759558 816 PSRP-GASPDPFGP-PPQVPSRPNRAPP------GVPSRKGPASPTRPAAPRPSEAP 864
Cdd:COG5180   316 PVRPpGGARDPGTPrPGQPTERPAGVPEaasdagQPPSAYPPAEEAVPGKPLEQGAP 372
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 762-864 6.89e-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: 39.99  E-value: 6.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 762 WLQVQSvpAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPP 841
Cdd:NF041121   10 WLAAQM--GRAAAPPSPEGPAPTAASQPATPPPPA--------------APPSPPGDPPEPPAPEPAPLPAPYPGSLAPP 73

                          90       100
                  ....*....|....*....|...
gi 1958759558 842 GVPSRKgpASPTRPAAPRPSEAP 864
Cdd:NF041121   74 PPPPPG--PAGAAPGAALPVRVP 94
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 3.20e-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: 3.20e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558    6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558   86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  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 7.64e-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: 438.99  E-value: 7.64e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFLHCKGKKFTDFEEVRLE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 181 LANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958759558 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 1958759558 215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958759558 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 1.21e-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: 1.21e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 520 VIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKD 599
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958759558 600 YRQLELACETQEEVDSWKASFLRAGVYPER 629
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 2.22e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 221.34  E-value: 2.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFlhckGKKFTDFEEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 106 DRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQppdiefqirDMLMQFVtKENCLILAVSPANSDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 1958759558 186 ALKIAKEVDPQGQRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 5.68e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 124.93  E-value: 5.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 655 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1958759558 735 LKEALSIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 9.17e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 107.32  E-value: 9.17e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  654 QLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYH 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1958759558  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 1958759558 520 VIRKGWLTINNIGImKGGSKEYWFVLTAENLSWYKDD---EEKEKKYMLSVDNLKLRDVEKGFMSS-KHIFALFNTEQRN 595
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1958759558 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 1958759558  520 VIRKGWLTINNIGiMKGGSKEYWFVLTAENLSWYKDDEEKEK---KYMLSVDNLKLRDVEKGFMSS-KHIFALfnteqrn 595
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1958759558  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 1958759558 522 RKGWLTINNIGIMKGGsKEYWFVLTAENLSWYKDDEEKEKKYMLSVD---NLKLRDVEKGfmSSKHIFALFNTEQRNVYk 598
Cdd:cd00821     1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPKGSIPlsgILEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                          90
                  ....*....|....*...
gi 1958759558 599 dyrqleLACETQEEVDSW 616
Cdd:cd00821    77 ------LQADSEEERQEW 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-864 2.87e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 2.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  747 TTTVSTPMPPPVDDSWLQVQSVPAG---------RRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPS 817
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958759558  818 RPGASPDPF-GPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:PHA03247  2910 QPQAPPPPQpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
PHA03378 PHA03378
EBNA-3B; Provisional
 763-864 7.47e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 56.23  E-value: 7.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 763 LQVQSVPAGRRSPTSSPTPQrRAPAVPPARPGSRGPAPGPPPAGSalgGAPPVPSRPGASPDPFGPPPQVPSRPnRAPPG 842
Cdd:PHA03378  685 LPIQWAPGTMQPPPRAPTPM-RPPAAPPGRAQRPAAATGRARPPA---AAPGRARPPAAAPGRARPPAAAPGRA-RPPAA 759

                          90       100
                  ....*....|....*....|....
gi 1958759558 843 VPSRKGP--ASPTRPAAPRPSEAP 864
Cdd:PHA03378  760 APGRARPpaAAPGAPTPQPPPQAP 783
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-867 7.72e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 7.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  751 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSalggAPPVPSRPGASPDPFG--- 827
Cdd:PHA03247  2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS----SPPQRPRRRAARPTVGslt 2696

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958759558  828 ----PPPQVP---SRPNRAPPGVPSRKG--------PASPTRPAAPRPSEAPLLD 867
Cdd:PHA03247  2697 sladPPPPPPtpePAPHALVSATPLPPGpaaarqasPALPAAPAPPAVPAGPATP 2751
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 755-863 2.09e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.99  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 755 PPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPS 834
Cdd:PRK07764  681 PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760

                          90       100
                  ....*....|....*....|....*....
gi 1958759558 835 RPNRAPPGVPSRKGPASPTRPAAPRPSEA 863
Cdd:PRK07764  761 PPAPAPAAAPAAAPPPSPPSEEEEMAEDD 789
PHA03378 PHA03378
EBNA-3B; Provisional
 752-864 1.02e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 52.76  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 752 TPMPPPvddswlqvQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG---- 827
Cdd:PHA03378  702 TPMRPP--------AAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAapga 773

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958759558 828 ----PPPQVPSRPNRAPPGVPS-RKGPASPTRPAAPRPSEAP 864
Cdd:PHA03378  774 ptpqPPPQAPPAPQQRPRGAPTpQPPPQAGPTSMQLMPRAAP 815
PHA03247 PHA03247
large tegument protein UL36; Provisional
 728-862 1.21e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  728 MLRMYHALKEALSIIGDINTTTVSTPMPPPVDDswlqvQSVPagrrspTSSPTPQRRAPAVPpARPGSRgpapgpppags 807
Cdd:PHA03247  2533 MLTWIRGLEELASDDAGDPPPPLPPAAPPAAPD-----RSVP------PPRPAPRPSEPAVT-SRARRP----------- 2589

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958759558  808 algGAPPVPSRPGASPDPFGPPPQvPSRPNRAPPGVPSRKGPASPTRPAAPRPSE 862
Cdd:PHA03247  2590 ---DAPPQSARPRAPVDDRGDPRG-PAPPSPLPPDTHAPDPPPPSPSPAANEPDP 2640
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 1958759558 751 STPMPPPvddswlqvQSVPAGRRSPTSSPTPQRrAPAVPPARPGSRGPAPGPPPAGSALGGAP---------PVP-SRPG 820
Cdd:PHA03378  721 TGRARPP--------AAAPGRARPPAAAPGRAR-PPAAAPGRARPPAAAPGRARPPAAAPGAPtpqpppqapPAPqQRPR 791

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958759558 821 ASPDPFgPPPQVPSRPNR-APPGVPSRKGPA 850
Cdd:PHA03378  792 GAPTPQ-PPPQAGPTSMQlMPRAAPGQQGPT 821
PHA03247 PHA03247
large tegument protein UL36; Provisional
 753-865 4.18e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  753 PMPPPVDDSwlqVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPppagsalGGAPPVPSRPGASPDPFGPP-PQ 831
Cdd:PHA03247  2683 PRRRAARPT---VGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAAR-------QASPALPAAPAPPAVPAGPAtPG 2752

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958759558  832 VPSRPNR-----APPGVPSRKGPASPTRPAAPRPSEAPL 865
Cdd:PHA03247  2753 GPARPARppttaGPPAPAPPAAPAAGPPRRLTRPAVASL 2791
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 1958759558 520 VIRKGWLTinnigiMKGGS----KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKgfMSSKHIFALFNTEQRN 595
Cdd:cd01252     3 PDREGWLL------KLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958759558 596 VYKD----------------YRqleLACETQEEVDSW 616
Cdd:cd01252    75 VIKAcktdsdgkvvegnhtvYR---ISAASEEERDEW 108
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 751-864 5.48e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 50.10  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 751 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGsrgpapgpppagsalggAPPVPSRPGASPDPFGPPP 830
Cdd:PRK14951  379 KTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAP-----------------PAPVAAPAAAAPAAAPAAA 441

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958759558 831 QVPSRPNRAPPGVPSRKGPASPTR----PAAPRPSEAP 864
Cdd:PRK14951  442 PAAVALAPAPPAQAAPETVAIPVRvapePAVASAAPAP 479
PHA03378 PHA03378
EBNA-3B; Provisional
 751-864 6.50e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.07  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 751 STPMPPPvddswlqvqSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPP 830
Cdd:PHA03378  692 GTMQPPP---------RAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPG 762

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958759558 831 QVP---SRPNRAPPGVPSRKGPASPTRP-AAPRPSEAP 864
Cdd:PHA03378  763 RARppaAAPGAPTPQPPPQAPPAPQQRPrGAPTPQPPP 800
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 769-866 1.34e-05

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 48.80  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 769 PAGRRSPTSSPTPQRRaPAVPPA---RPGSRGPAPGPPPAGSALGGA---------PPVPSRPGASPDPF----GPPPQV 832
Cdd:PHA03321  434 PAPRRDNDPPPPPRAR-PGSTPAcarRARAQRARDAGPEYVDPLGALrrlpagaapPPEPAAAPSPATYYtrmgGGPPRL 512

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958759558 833 PSRpNRAPpgvPSRKGPASPTRPAAPRPSEAPLL 866
Cdd:PHA03321  513 PPR-NRAT---ETLRPDWGPPAAAPPEQMEDPYL 542
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 752-864 2.05e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:PRK07764  598 EGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAA 677

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958759558 832 VPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 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 2.63e-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: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 539 KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNL----KLRDVEKgfmssKHIFALFnTEQRNVYkdyrqleLACETQEEVD 614
Cdd:cd13298    23 KKRWVVLRPCQLSYYKDEKEYKLRRVINLSELlavaPLKDKKR-----KNVFGIY-TPSKNLH-------FRATSEKDAN 89


                  ..
gi 1958759558 615 SW 616
Cdd:cd13298    90 EW 91
PHA03247 PHA03247
large tegument protein UL36; Provisional
 752-865 2.82e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  752 TPMPPPVDDSwlqvQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGA-PPVPSRPGASPDPFGPPP 830
Cdd:PHA03247  2738 APAPPAVPAG----PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESrESLPSPWDPADPPAAVLA 2813

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958759558  831 QVPSRPNRAPPGV----PSRKGPASPTRPAAPRPSEAPL 865
Cdd:PHA03247  2814 PAAALPPAASPAGplppPTSAQPTAPPPPPGPPPPSLPL 2852
PHA03247 PHA03247
large tegument protein UL36; Provisional
 750-861 3.02e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  750 VSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAP-PVPSRPGASPDPFG- 827
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPaGAGEPSGAVPQPWLg 2965

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958759558  828 --PPPQVPSRPNRAPPGVPSRKGPASPTRP----AAPRPS 861
Cdd:PHA03247  2966 alVPGRVAVPRFRVPQPAPSREAPASSTPPltghSLSRVS 3005
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 746-861 3.52e-05

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 46.13  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 746 NTTTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgpppagsalGGAPPVPSRPGasPDP 825
Cdd:pfam15822  52 STAPSTVPFGPAPTGMY---PSIPLTGPSPGPPAPFPPSGPSCPPP------------------GGPYPAPTVPG--PGP 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759558 826 FGPPPQvpsrPNRAPPGVPSRKGpaSPTRPAAPRPS 861
Cdd:pfam15822 109 IGPYPT----PNMPFPELPRPYG--APTDPAAAAPS 138
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
728-864 4.52e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.18  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 728 MLRMYhalkeALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAV-PPARPGSRGPAPG----- 801
Cdd:PRK12323  357 LLRML-----AFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAaAAARAVAAAPARRspape 431

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958759558 802 -----PPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRkgPASPTRPAAPRPSEAP 864
Cdd:PRK12323  432 alaaaRQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPA--RAAPAAAPAPADDDPP 497
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 1958759558 520 VIRKGWLTINNiGIMKGGsKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMS-SKHIFALF---NTEQRN 595
Cdd:cd13378     3 VLKAGWLKKQR-SIMKNW-QQRWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNELPPNPEEpGKHLFEILpggAGDREK 80

                          90       100
                  ....*....|....*....|....*..
gi 1958759558 596 VYKDYRQLELACETQEEVDSWKASFLR 622
Cdd:cd13378    81 VPMNHEAFLLMANSQSDMEDWVKAIRR 107
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-865 5.78e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  747 TTTVSTPMPP--PVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSAlGGAPPVPSRPGASPD 824
Cdd:PHA03247  2763 TAGPPAPAPPaaPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPPTSAQPTAPPP 2841

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958759558  825 PFGPPPQ--------VPSRP--NRAPPGVPSRKgPASPTRPAAPRPSEAPL 865
Cdd:PHA03247  2842 PPGPPPPslplggsvAPGGDvrRRPPSRSPAAK-PAAPARPPVRRLARPAV 2891
PHA03247 PHA03247
large tegument protein UL36; Provisional
 765-863 6.79e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  765 VQSVPAGRRSPTSSPTPQR-----RAPAVPPARPGSRGPAPGPPPA---GSALGGAPPVPSrpGASPDPFGPPP--QVPS 834
Cdd:PHA03247   365 LEDLSAGRHHPKRASLPTRkrrsaRHAATPFARGPGGDDQTRPAAPvpaSVPTPAPTPVPA--SAPPPPATPLPsaEPGS 442

                           90       100
                   ....*....|....*....|....*....
gi 1958759558  835 RPNRAPPgvPSRKGPASPTRPAAPRPSEA 863
Cdd:PHA03247   443 DDGPAPP--PERQPPAPATEPAPDDPDDA 469
PHA03247 PHA03247
large tegument protein UL36; Provisional
 752-864 8.60e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 8.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  752 TPMPPPvdDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPFGP-PP 830
Cdd:PHA03247  2707 TPEPAP--HALVSATPLPPGPAAARQASPALPAAPAPPAV------------PAGPATPGGPARPARPPTTAGPPAPaPP 2772

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958759558  831 QVPSR--PNRAPPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:PHA03247  2773 AAPAAgpPRRLTRPAVASLSESRESLPSPWDPADPP 2808
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 752-861 9.35e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 9.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 752 TPMPPPVDDswlQVQSVPAGRRSPTSSPTPqrrAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPdpfgPPPQ 831
Cdd:PRK07764  407 AAAPAPAAA---APAAAAAPAPAAAPQPAP---APAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAA----APEP 476

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958759558 832 VPSRPNRAPPGVPSRKGPASPTRPAAPRPS 861
Cdd:PRK07764  477 TAAPAPAPPAAPAPAAAPAAPAAPAAPAGA 506
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 753-864 1.02e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  753 PMPPPVDD---SWLQVQSVPAGRRSPTSSP--TPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 827
Cdd:PHA03307   258 PRPAPITLptrIWEASGWNGPSSRPGPASSssSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958759558  828 PPPqVPSRPNRAPPGVPSRKGPASPT--RPAAPRPSEAP 864
Cdd:PHA03307   338 GAA-VSPGPSPSRSPSPSRPPPPADPssPRKRPRPSRAP 375
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 751-864 1.07e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  751 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAV---PPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 827
Cdd:PHA03307   805 SGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAarpPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPG 884

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958759558  828 PPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:PHA03307   885 AAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPMPPGGP 921
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 752-860 1.59e-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: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:NF040712  218 EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAP 297

                          90       100
                  ....*....|....*....|....*....
gi 1958759558 832 VPSRPnrAPPGVPSRKGPASPTRPAAPRP 860
Cdd:NF040712  298 APAAP--AAPAAPEAEEPARPEPPPAPKP 324
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 748-864 2.03e-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: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 748 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTS-SPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 826
Cdd:NF040712  200 ATVPRLAREPADARPEEVEPAPAAEGAPATdSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958759558 827 GPPPQVPSRPNRAPPGVPSRKGPASPTRPAA---PRPSEAP 864
Cdd:NF040712  280 PPAPGAAETPEAAEPPAPAPAAPAAPAAPEAeepARPEPPP 320
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 1958759558 520 VIRKGWLTinnigiMKGGS-----KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGF-MSSKHIFALFNTEQ 593
Cdd:cd13248     7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                          90       100
                  ....*....|....*....|...
gi 1958759558 594 RNVYkdyrqleLACETQEEVDSW 616
Cdd:cd13248    81 RTYY-------FAADTAEEMEQW 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
 766-864 2.47e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  766 QSVPAGRRSPTSSPTPQRRAPAV----------PPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPqvPSR 835
Cdd:PHA03247  2670 LGRAAQASSPPQRPRRRAARPTVgsltsladppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV--PAG 2747

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958759558  836 PnrAPPGVPSRKG-PASPTRPAAPRPSEAP 864
Cdd:PHA03247  2748 P--ATPGGPARPArPPTTAGPPAPAPPAAP 2775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-866 2.49e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  748 TTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQrrAPAVP--PARPgsrgpapgpppagsalgGAPPVPS---RPGAS 822
Cdd:PHA03247  2715 LVSATPLPPGPAAAR---QASPALPAAPAPPAVPA--GPATPggPARP-----------------ARPPTTAgppAPAPP 2772

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958759558  823 PDPFGPPPQVPSRPNRAP--PGVPSRKGPASPTRPAAPRPSEAPLL 866
Cdd:PHA03247  2773 AAPAAGPPRRLTRPAVASlsESRESLPSPWDPADPPAAVLAPAAAL 2818
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 715-867 3.32e-04

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: 43.76  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 715 MEESAEQAQRRdemlrmyHALKEALSIIGDINTTTVSTPMPppvddSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPArpg 794
Cdd:pfam07174   1 MDQVDPNSTRR-------KGLWATLAIAAVAGASAVAVALP-----AVAHADPEPAPPPPSTATAPPAPPPPPPAPA--- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958759558 795 srGPAPGPPPAGSALGGAPPVPSRPGASP----DPFGPPPQvPSRPNRAPPG-VPSRKGPASPTRPAAPRPSEAPLLD 867
Cdd:pfam07174  66 --APAPPPPPAAPNAPNAPPPPADPNAPPpppaDPNAPPPP-AVDPNAPEPGrIDNAVGGFSYVVPAGWVESDATHLD 140
PHA03247 PHA03247
large tegument protein UL36; Provisional
 753-864 3.59e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  753 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPQrrAPAVPPARPGSRGPAPGPPPAGSALGGAPP---VPSRPGASPDP---- 825
Cdd:PHA03247  2808 PAAVLAPAAALPPAASPAGPLPPPTSAQPT--APPPPPGPPPPSLPLGGSVAPGGDVRRRPPsrsPAAKPAAPARPpvrr 2885

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958759558  826 -FGPPPQVPSRPNRAPPGVPSR-KGPASPTRPAAPRPSEAP 864
Cdd:PHA03247  2886 lARPAVSRSTESFALPPDQPERpPQPQAPPPPQPQPQPPPP 2926
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 769-858 3.78e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.30  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 769 PAGRRSPTSSPTPQRraPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPFGP-PPQVPSRPNRaPPGVPSRK 847
Cdd:PTZ00449  591 PEEPKKPKRPRSAQR--PTRPKS------------PKLPELLDIPKSPKRPESPKSPKRPpPPQRPSSPER-PEGPKIIK 655

                          90
                  ....*....|.
gi 1958759558 848 GPASPTRPAAP 858
Cdd:PTZ00449  656 SPKPPKSPKPP 666
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 710-860 3.98e-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: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 710 DQNTLMEESAEQA--QRRDEMLRMYHALKEALSIiGDINTTTVSTPMPPPvddswlQVQSVPAgRRSPTSSPTPQRRAPA 787
Cdd:pfam03154 153 DNESDSDSSAQQQilQTQPPVLQAQSGAASPPSP-PPPGTTQAATAGPTP------SAPSVPP-QGSPATSQPPNQTQST 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 788 VPPARPGSRGPAPGPPPAgsalggapPVPSRPGASPDPFGPPPQVPSRPNRAPP--------GVPSRKGPASPTRPAAPR 859
Cdd:pfam03154 225 AAPHTLIQQTPTLHPQRL--------PSPHPPLQPMTQPPPPSQVSPQPLPQPSlhgqmppmPHSLQTGPSHMQHPVPPQ 296


                  .
gi 1958759558 860 P 860
Cdd:pfam03154 297 P 297
PHA03247 PHA03247
large tegument protein UL36; Provisional
 757-868 4.25e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  757 PVDDSwlqvqsvPAGRRSPTSSPTPQRRAPAVPPArpgsrgpaPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVpSRP 836
Cdd:PHA03247  2601 PVDDR-------GDPRGPAPPSPLPPDTHAPDPPP--------PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRV-SRP 2664

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958759558  837 NRA-PPGVPSRKG--PASPTRPAAPrPSEAPLLDL 868
Cdd:PHA03247  2665 RRArRLGRAAQASspPQRPRRRAAR-PTVGSLTSL 2698
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
774-864 5.01e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 774 SPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPT 853
Cdd:PRK07003  405 AAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDA 484

                          90
                  ....*....|.
gi 1958759558 854 RPAAPRPSEAP 864
Cdd:PRK07003  485 PPDAAFEPAPR 495
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
750-864 5.42e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 750 VSTPMPPPVDDSWLQVQsvPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPppagsaLGGAPPVPSRPGASPDPFGPP 829
Cdd:PRK12323  451 APAPAAAPAAAARPAAA--GPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEE------LPPEFASPAPAQPDAAPAGWV 522

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958759558 830 PQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:PRK12323  523 AESIPDPATADPDDAFETLAPAPAAAPAPRAAAAT 557
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 1958759558 773 RSPTSSPTPQRRAPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPfgPPPQVPSRPNRAPPGvPSRKGP 849
Cdd:pfam01140  64 KTRVFAPGPHGHPDQVPYI------------VTWEALAADPPPWVRPFLTPKP--PPPQPPAAPGLRPPL-PPASAP 125
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 753-867 6.56e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.16  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 753 PMPPPVDDSWLQVQSVPAGRRSPTSSPtpqrrAPAVPPARPGSRGPAPgpppagsalgGAPPVPSRPGASPDPFGPPPQV 832
Cdd:PRK14951  391 AAPVAQAAAAPAPAAAPAAAASAPAAP-----PAAAPPAPVAAPAAAA----------PAAAPAAAPAAVALAPAPPAQA 455

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958759558 833 PSRPNRAPPGVPSRKGPASPTRPAAPRPSEAPLLD 867
Cdd:PRK14951  456 APETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 733-864 7.84e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 7.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  733 HALKEALSIIGDINTTTVSTPMPPPVDDSWLqvqsVPAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalGGA 812
Cdd:PHA03307    48 AELAAVTVVAGAAACDRFEPPTGPPPGPGTE----APANESRSTPTWSLSTLAPASPAREGSPT-------------PPG 110

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958759558  813 PPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:PHA03307   111 PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAV 162
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 775-859 8.11e-04

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 41.90  E-value: 8.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 775 PTSSPTPQrraPAVPPARPGsrgpapgpppagsalGGAPPVP---------SRPGASPDPFG--PPPQV-PSRPNraPPG 842
Cdd:pfam15822 163 PYPSPGPY---PAVPPPQSP---------------GAAPPVPwgtvppgpwGPPAPYPDPTGsyPMPGLyPTPNN--PFQ 222

                          90
                  ....*....|....*...
gi 1958759558 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 1958759558 516 DEIL--VIRKGWLtinnigiMKGGSK-----EYWFVLTAENLSWYKDDEEKEKK 562
Cdd:cd13273     2 DELIldVIKKGYL-------WKKGHLlptwtERWFVLKPNSLSYYKSEDLKEKK 48
PHA03247 PHA03247
large tegument protein UL36; Provisional
 779-864 8.93e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 8.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  779 PTPQRRAPAVPPARPGSRGPAPGPPPAGSalGGAPPVPSRpGASPDPFGPPPQVPSRPNRAPPGV--PSRKGpASPTRPA 856
Cdd:PHA03247   236 PFVERRVVISHPLRGDIAAPAPPPVVGEG--ADRAPETAR-GATGPPPPPEAAAPNGAAAPPDGVwgAALAG-APLALPA 311


                   ....*...
gi 1958759558  857 APRPSEAP 864
Cdd:PHA03247   312 PPDPPPPA 319
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 753-863 9.78e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 9.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  753 PMPPPVDDSWLQVQSVPA-GRRSPTSSPTP--QRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPP 829
Cdd:PHA03307   126 PPPSPAPDLSEMLRPVGSpGPPPAASPPAAgaSPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPR 205

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958759558  830 PQVPSRPNRAPPGVPsrkGPASPTRPAAPRPSEA 863
Cdd:PHA03307   206 PPRRSSPISASASSP---APAPGRSAADDAGASS 236
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 769-864 1.01e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.75  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 769 PAGRRSPTSSPTPQRRAPAVPPARpgsrgpapgpppagsalggaPPVPSRPGASPDPFGPP-PQVPSRPNRAPPgvPSRk 847
Cdd:PTZ00449  585 PKHPKDPEEPKKPKRPRSAQRPTR--------------------PKSPKLPELLDIPKSPKrPESPKSPKRPPP--PQR- 641

                          90
                  ....*....|....*..
gi 1958759558 848 gPASPTRPAAPRPSEAP 864
Cdd:PTZ00449  642 -PSSPERPEGPKIIKSP 657
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 747-868 1.12e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 747 TTTVSTPMPPPVDDSWLQVqSVPAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalggAPPVPSRPGASPDPF 826
Cdd:PRK14951  397 AAAAPAPAAAPAAAASAPA-APPAAAPPAPVAAPAAAAPAAAPAAAPAAV---------------ALAPAPPAQAAPETV 460

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958759558 827 GPPPQVPSRPNRAPPgvpsrkGPASPTRPAAPRPSEAPLLDL 868
Cdd:PRK14951  461 AIPVRVAPEPAVASA------APAPAAAPAAARLTPTEEGDV 496
PHA03247 PHA03247
large tegument protein UL36; Provisional
 771-864 1.39e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  771 GRRSPTSSPTPQRRAPA----------VPPaRPGSRGPAPGPPPAGSALGGAPPV-PSRPGASPDPFGPPPQ-------- 831
Cdd:PHA03247  2502 GPPDPDAPPAPSRLAPAilpdepvgepVHP-RMLTWIRGLEELASDDAGDPPPPLpPAAPPAAPDRSVPPPRpaprpsep 2580

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958759558  832 ----------VPSRPNR-----APPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:PHA03247  2581 avtsrarrpdAPPQSARprapvDDRGDPRGPAPPSPLPPDTHAPDPPP 2628
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 752-865 1.47e-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: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 752 TPMPPPVddswlqvqsvPAGRRSPTSSPTPQRRAPaVPParpgsrgpapgpppAGSALGGAPPVPSRPGAsPDPFGPPP- 830
Cdd:pfam03154 250 QPMTQPP----------PPSQVSPQPLPQPSLHGQ-MPP--------------MPHSLQTGPSHMQHPVP-PQPFPLTPq 303

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958759558 831 ----QVPSRPNRAPPGVPSRKGPASPTRPAAPR---PSEAPL 865
Cdd:pfam03154 304 ssqsQVPPGPSPAAPGQSQQRIHTPPSQSQLQSqqpPREQPL 345
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 766-864 1.59e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 766 QSVPAGRRSPTSSPTPQRRAPAVPPARPGsrgpapgpppagsalGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPS 845
Cdd:PRK07764  383 RRLGVAGGAGAPAAAAPSAAAAAPAAAPA---------------PAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGN 447

                          90
                  ....*....|....*....
gi 1958759558 846 RKGPASPTRPAAPRPSEAP 864
Cdd:PRK07764  448 APAGGAPSPPPAAAPSAQP 466
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 747-864 1.60e-03

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 41.97  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 747 TTTVSTPMPPPVDDSWlQVQSVPAGRRSPTSSPT---------PQRRAPAVPPARPGSRGPAPGpppagsalggAPPV-- 815
Cdd:COG5180   247 ATVDAQPEMRPPADAK-ERRRAAIGDTPAAEPPGlpvleagsePQSDAPEAETARPIDVKGVAS----------APPAtr 315

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759558 816 PSRP-GASPDPFGP-PPQVPSRPNRAPP------GVPSRKGPASPTRPAAPRPSEAP 864
Cdd:COG5180   316 PVRPpGGARDPGTPrPGQPTERPAGVPEaasdagQPPSAYPPAEEAVPGKPLEQGAP 372
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 766-864 1.91e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 766 QSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPpagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPS 845
Cdd:PRK07764  395 AAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPA-------PAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPA 467

                          90
                  ....*....|....*....
gi 1958759558 846 RKGPASPTRPAAPRPSEAP 864
Cdd:PRK07764  468 PAPAAAPEPTAAPAPAPPA 486
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 756-864 1.92e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 756 PPVddswLQVQSVPAGRRSP-------TSSPTPQRRAPAVPPArpgsrgpapgpppagsalgGAPPVPSRPGASPDPFGP 828
Cdd:pfam03154 171 PPV----LQAQSGAASPPSPpppgttqAATAGPTPSAPSVPPQ-------------------GSPATSQPPNQTQSTAAP 227

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759558 829 PPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:pfam03154 228 HTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP 263
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 749-858 2.29e-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: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 749 TVSTPMPPPVddswlqvqsvPAGRRSPTSSPTPQrrAPAVPPARPGSRGPapgpppagsalgGAPPVPSRPGASPDPfGP 828
Cdd:pfam06346  42 SAAIPPPPPL----------PGGTSIPPPPPLPG--AASIPPPPPLPGST------------GIPPPPPLPGGAGIP-PP 96

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958759558 829 PPQVPSRPNRAPPGVPSRKGPASPTRPAAP 858
Cdd:pfam06346  97 PPPLPGGAGVPPPPPPLPGGPGIPPPPPFP 126
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 747-862 2.46e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  747 TTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 826
Cdd:PHA03307    89 TWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAAS 168

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958759558  827 GPPP----QVPSRPNRAPPGVPSRKGPASPTRPAAPRPSE 862
Cdd:PHA03307   169 SRQAalplSSPEETARAPSSPPAEPPPSTPPAAASPRPPR 208
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 725-863 2.77e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  725 RDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSwlqvqSVPAGRRSPTSSPTPqrRAPAVPPARPGSRGPAPGPPP 804
Cdd:PHA03307   252 ENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSS-----SSPRERSPSPSPSSP--GSGPAPSSPRASSSSSSSRES 324

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958759558  805 AGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEA 863
Cdd:PHA03307   325 SSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAG 383
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 1958759558 753 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARpgsrgpapgpppagsalgGAPPVPSRPGASpdpfgPPPQV 832
Cdd:PHA02030  254 IIKPKSKAAGSNLPAVPNVAADAGSAAAPAVPAAAAAVAQ------------------AAPSVPQVPNVA-----VLPDV 310

                          90       100
                  ....*....|....*....|....*.
gi 1958759558 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 1958759558 747 TTTVSTPMPPPVDDSWLQVQSVPAG--RRSPTSSPTPQRRAPAVP--PARPGSRGPAPGPPPAGSALGGAP------PVP 816
Cdd:pfam16072 158 TTVINAGGQQPAAPAAPAYPVAPAAypAQAPAAAPAPAPGAPQTPlaPLNPVAAAPAAAAGAAAAPVVAAAapaaaaPPP 237

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759558 817 SRPGAsPDPFGPPPQ------VPSRPNRAPPGVPSR 846
Cdd:pfam16072 238 PAPAA-PPADAAPPApggiicVPVRVPEPDPKDATK 272
Aim21 pfam11489
Altered inheritance of mitochondria protein 21; This is a family of proteins conserved in ...
 748-867 3.04e-03

Altered inheritance of mitochondria protein 21; This is a family of proteins conserved in yeasts. Saccharomyces cerevisiae Aim21 may be involved in mitochondrial migration along actin filament. It may also interact with ribosomes.


Pssm-ID: 371558 [Multi-domain]  Cd Length: 677  Bit Score: 41.11  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 748 TTVSTP----MPPPVDDSWLQVQSVPAGRRSPtsSPTPQRRAPAVP-------PARPGSRGPAPGPPPAGSAlggaPPVP 816
Cdd:pfam11489 502 TTVETPdevkSTSPGVPTKPAIPARPKSGKPT--SPTEKRKPPPVPkkpkpqiPARPAKAQPQQAGEEFKPK----PRVP 575

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958759558 817 SRPGASP-------------DPFGPPPQVPSRPNRAPpgvPSRKGPASPTRPAAPRPSEAPLLD 867
Cdd:pfam11489 576 ARPGGSKisalragfasdlnGRLQLGPQAPKKVVEED---KEPSEEKGDKEEEEDTKEKAPLSD 636
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 766-864 3.90e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 766 QSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPagsalGGAPPVPSRPGAspdpfGPPPQVPSRPNRAPPGvps 845
Cdd:PRK07764  420 AAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPP-----AAAPSAQPAPAP-----AAAPEPTAAPAPAPPA--- 486

                          90
                  ....*....|....*....
gi 1958759558 846 rkGPASPTRPAAPRPSEAP 864
Cdd:PRK07764  487 --APAPAAAPAAPAAPAAP 503
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 743-865 4.06e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  743 GDINTTTVSTPMPPPVDDSwlqvqsvpAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGAS 822
Cdd:PHA03307   107 TPPGPSSPDPPPPTPPPAS--------PPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSS 178

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958759558  823 PD---PFGPPPQVPSRPNRAPPGVPSR-KGPASPTRPAAPRPSEAPL 865
Cdd:PHA03307   179 PEetaRAPSSPPAEPPPSTPPAAASPRpPRRSSPISASASSPAPAPG 225
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
751-864 4.13e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.99  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 751 STPMPPPVDDSWLQVQSV---PAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 827
Cdd:PRK07003  421 TRAEAPPAAPAPPATADRgddAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPS 500

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958759558 828 PPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:PRK07003  501 AATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTP 537
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 541-616 4.37e-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: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 541 YWFVLTAENLS-W-YKDDEEKeKKYMLSVD-----NLKLRDVEKGFMSSKHIFAL-FNTEQRNVYKDYRQLE----LACE 608
Cdd:cd01263    23 RWCVLRGGYLSfWkYPDDEEK-KKPIGSIDltkciTEKVEPAPRELCARPNTFLLeTLRPAEDDDRDDTNEKirvlLSAD 101


                  ....*...
gi 1958759558 609 TQEEVDSW 616
Cdd:cd01263   102 TKEERIEW 109
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 1958759558 753 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPqrrAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSR-PGASPDPfGPPPQ 831
Cdd:PHA02682   84 PSPACAAPAPACPACAPAAPAPAVTCPAP---APACPPATAPTCPPPAVCPAPARPAPACPPSTRQcPPAPPLP-TPKPA 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958759558 832 VPSRP-----NRAPPGVPSRKGPASPTRPAAprpseAPLLD 867
Cdd:PHA02682  160 PAAKPiflhnQLPPPDYPAASCPTIETAPAA-----SPVLE 195
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 769-865 5.65e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558  769 PAGRRSPTSSPTPQrrAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPN--RAPPGVPSR 846
Cdd:PHA03307   846 PPARSSESSKSKPA--AAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKlgPMPPGGPDP 923

                           90       100
                   ....*....|....*....|....
gi 1958759558  847 KG-----PASPTRPaaPRPSEAPL 865
Cdd:PHA03307   924 RGgfrrvPPGDLHT--PAPSAAAL 945
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
752-864 5.67e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQrRAPAVPPArpgsrgpaPGPPPAGSALGGAPPVPSRPGA--SPDPFGPP 829
Cdd:PRK12323  427 SPAPEALAAARQASARGPGGAPAPAPAPAAA-PAAAARPA--------AAGPRPVAAAAAAAPARAAPAAapAPADDDPP 497

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759558 830 PQVPSRPNRAPPGV-PSRKGPASPTRPAAPRPSEAP 864
Cdd:PRK12323  498 PWEELPPEFASPAPaQPDAAPAGWVAESIPDPATAD 533
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 769-866 5.86e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.46  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 769 PAGRRSPTSSPTPQRRAPAVPPARPGSRGPApgpppagsalggapPVPSRPGASPdPFGPPPQVPSRPNRAPPGVP--SR 846
Cdd:PHA02682   81 PLAPSPACAAPAPACPACAPAAPAPAVTCPA--------------PAPACPPATA-PTCPPPAVCPAPARPAPACPpsTR 145

                          90       100
                  ....*....|....*....|.
gi 1958759558 847 KGPASPTRPAA-PRPSEAPLL 866
Cdd:PHA02682  146 QCPPAPPLPTPkPAPAAKPIF 166
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
 772-865 6.04e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 39.88  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 772 RRSPTSSPTPQRRAPavPPARPGSRGPAPGPPPagsalggAPPVPSRPGASPDP--FGPPPQVPSRPNRAPPGVPSrkGP 849
Cdd:PHA03201    2 KRARSRSPSPPRRPS--PPRPTPPRSPDASPEE-------TPPSPPGPGAEPPPgrAAGPAAPRRRPRGCPAGVTF--SS 70

                          90       100
                  ....*....|....*....|.
gi 1958759558 850 ASPTRPA-----APRPSEAPL 865
Cdd:PHA03201   71 SAPPRPPlglddAPAATPPPL 91
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 811-864 6.23e-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: 6.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958759558 811 GAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:pfam15240  71 GGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGP 124
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
748-864 6.38e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 748 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 827
Cdd:PRK07003  405 AAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDA 484

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958759558 828 PP-------PQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 864
Cdd:PRK07003  485 PPdaafepaPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPP 528
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 753-864 6.41e-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: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 753 PMPPPVDDSWlqvQSVPAGRRSPTSSPTPQRrAPAVPPARPGSRgpapgpPPAGSALGGAPPVPSRPGASPDPFGPPPQV 832
Cdd:pfam15240  65 PGPPPPGGPQ---QPPPQGGKQKPQGPPPQG-GPRPPPGKPQGP------PPQGGNQQQGPPPPGKPQGPPPQGGGPPPQ 134

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958759558 833 PSRPNRAPPGVPSR-KGPasPTRPAAP-RPSEAP 864
Cdd:pfam15240 135 GGNQQGPPPPPPGNpQGP--PQRPPQPgNPQGPP 166
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 762-864 6.89e-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: 39.99  E-value: 6.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 762 WLQVQSvpAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPP 841
Cdd:NF041121   10 WLAAQM--GRAAAPPSPEGPAPTAASQPATPPPPA--------------APPSPPGDPPEPPAPEPAPLPAPYPGSLAPP 73

                          90       100
                  ....*....|....*....|...
gi 1958759558 842 GVPSRKgpASPTRPAAPRPSEAP 864
Cdd:NF041121   74 PPPPPG--PAGAAPGAALPVRVP 94
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 768-864 7.25e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 768 VPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPagsalggAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRK 847
Cdd:PRK07764  387 VAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAP-------APAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPA 459

                          90
                  ....*....|....*..
gi 1958759558 848 GPASPTRPAAPRPSEAP 864
Cdd:PRK07764  460 AAPSAQPAPAPAAAPEP 476
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 749-865 7.71e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.07  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759558 749 TVSTPMPPPVDDSWLQVQSVP-AGR----RSPTSSPTPQRR------APAVPPARPGSRGPAPgpppagsalggAPP--V 815
Cdd:PHA02682   36 APAAPCPPDADVDPLDKYSVKeAGRyyqsRLKANSACMQRPsgqsplAPSPACAAPAPACPAC-----------APAapA 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958759558 816 PSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASP--TR---PAAPRPSEAPL 865
Cdd:PHA02682  105 PAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPpsTRqcpPAPPLPTPKPA 159
 
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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