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Conserved domains on  [gi|1958759570|ref|XP_038960076|]
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dynamin-1 isoform X7 [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 2.24e-154

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


:

Pssm-ID: 197491  Cd Length: 240  Bit Score: 451.64  E-value: 2.24e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570    6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570   86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  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 5.55e-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: 436.95  E-value: 5.55e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958759570 455 EMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 514-625 1.13e-85

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: 268.04  E-value: 1.13e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 514 NQVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVY 593
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958759570 594 KDYRQLELACETQEEVDSWKASFLRAGVYPER 625
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
651-741 4.70e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 125.32  E-value: 4.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 651 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 730
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1958759570 731 LKEALSIIGDI 741
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 743-860 2.78e-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: 2.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  743 TTTVSTPMPPPVDDSWLQVQSVPAG---------RRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPS 813
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958759570  814 RPGASPDPF-GPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
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 2.24e-154

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 451.64  E-value: 2.24e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570    6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570   86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  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 4.75e-149

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


Pssm-ID: 206738  Cd Length: 278  Bit Score: 439.37  E-value: 4.75e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFLHCKGKKFTDFEEVRLE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 181 LANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958759570 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 5.55e-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: 436.95  E-value: 5.55e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958759570 455 EMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 514-625 1.13e-85

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: 268.04  E-value: 1.13e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 514 NQVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVY 593
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958759570 594 KDYRQLELACETQEEVDSWKASFLRAGVYPER 625
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 1.61e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 221.72  E-value: 1.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFlhckGKKFTDFEEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 106 DRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQppdiefqirDMLMQFVtKENCLILAVSPANSDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 1958759570 186 ALKIAKEVDPQGQRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
651-741 4.70e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 125.32  E-value: 4.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 651 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 730
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1958759570 731 LKEALSIIGDI 741
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
650-741 8.20e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 107.71  E-value: 8.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  650 QLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYH 729
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1958759570  730 ALKEALSIIGDI 741
Cdd:smart00302  81 LLKKARQIIAAV 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 516-619 1.27e-11

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 61.81  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 516 VIRKGWLTINNIGImKGGSKEYWFVLTAENLSWYKDD---EEKEKKYMLSVDNLKLRDVEKGFMSS-KHIFALFNTEQRN 591
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1958759570 592 VykdyRQLELACETQEEVDSWKASFLRA 619
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 516-619 2.51e-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: 2.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  516 VIRKGWLTINNIGiMKGGSKEYWFVLTAENLSWYKDDEEKEK---KYMLSVDNLKLRDVEKGFMSS-KHIFALfnteqrn 591
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1958759570  592 VYKDYRQLELACETQEEVDSWKASFLRA 619
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PHA03247 PHA03247
large tegument protein UL36; Provisional
 743-860 2.78e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 2.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  743 TTTVSTPMPPPVDDSWLQVQSVPAG---------RRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPS 813
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958759570  814 RPGASPDPF-GPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:PHA03247  2910 QPQAPPPPQpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 742-857 4.31e-05

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 45.75  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 742 NTTTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgpppagsalGGAPPVPSRPGasPDP 821
Cdd:pfam15822  52 STAPSTVPFGPAPTGMY---PSIPLTGPSPGPPAPFPPSGPSCPPP------------------GGPYPAPTVPG--PGP 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759570 822 FGPPPQvpsrPNRAPPGVPSRKGpaSPTRPAAPRPS 857
Cdd:pfam15822 109 IGPYPT----PNMPFPELPRPYG--APTDPAAAAPS 138
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 748-856 1.55e-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: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 748 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 827
Cdd:NF040712  218 EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAP 297

                          90       100
                  ....*....|....*....|....*....
gi 1958759570 828 VPSRPnrAPPGVPSRKGPASPTRPAAPRP 856
Cdd:NF040712  298 APAAP--AAPAAPEAEEPARPEPPPAPKP 324
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 744-860 1.97e-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: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 744 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTS-SPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 822
Cdd:NF040712  200 ATVPRLAREPADARPEEVEPAPAAEGAPATdSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958759570 823 GPPPQVPSRPNRAPPGVPSRKGPASPTRPAA---PRPSEAP 860
Cdd:NF040712  280 PPAPGAAETPEAAEPPAPAPAAPAAPAAPEAeepARPEPPP 320
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 743-860 1.67e-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: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 743 TTTVSTPMPPPVDDSWlQVQSVPAGRRSPTSSPT---------PQRRAPAVPPARPGSRGPAPGpppagsalggAPPV-- 811
Cdd:COG5180   247 ATVDAQPEMRPPADAK-ERRRAAIGDTPAAEPPGlpvleagsePQSDAPEAETARPIDVKGVAS----------APPAtr 315

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759570 812 PSRP-GASPDPFGP-PPQVPSRPNRAPP------GVPSRKGPASPTRPAAPRPSEAP 860
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 ...
 758-860 6.86e-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: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 758 WLQVQSvpAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPP 837
Cdd:NF041121   10 WLAAQM--GRAAAPPSPEGPAPTAASQPATPPPPA--------------APPSPPGDPPEPPAPEPAPLPAPYPGSLAPP 73

                          90       100
                  ....*....|....*....|...
gi 1958759570 838 GVPSRKgpASPTRPAAPRPSEAP 860
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 2.24e-154

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 451.64  E-value: 2.24e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570    6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570   86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  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 4.75e-149

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


Pssm-ID: 206738  Cd Length: 278  Bit Score: 439.37  E-value: 4.75e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFLHCKGKKFTDFEEVRLE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 181 LANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958759570 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 5.55e-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: 436.95  E-value: 5.55e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958759570 455 EMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 514-625 1.13e-85

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: 268.04  E-value: 1.13e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 514 NQVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVY 593
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958759570 594 KDYRQLELACETQEEVDSWKASFLRAGVYPER 625
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 1.61e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 221.72  E-value: 1.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFlhckGKKFTDFEEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 106 DRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQppdiefqirDMLMQFVtKENCLILAVSPANSDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 1958759570 186 ALKIAKEVDPQGQRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
651-741 4.70e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 125.32  E-value: 4.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 651 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 730
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1958759570 731 LKEALSIIGDI 741
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
650-741 8.20e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 107.71  E-value: 8.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  650 QLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYH 729
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1958759570  730 ALKEALSIIGDI 741
Cdd:smart00302  81 LLKKARQIIAAV 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 516-619 1.27e-11

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 61.81  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 516 VIRKGWLTINNIGImKGGSKEYWFVLTAENLSWYKDD---EEKEKKYMLSVDNLKLRDVEKGFMSS-KHIFALFNTEQRN 591
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1958759570 592 VykdyRQLELACETQEEVDSWKASFLRA 619
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 516-619 2.51e-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: 2.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  516 VIRKGWLTINNIGiMKGGSKEYWFVLTAENLSWYKDDEEKEK---KYMLSVDNLKLRDVEKGFMSS-KHIFALfnteqrn 591
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1958759570  592 VYKDYRQLELACETQEEVDSWKASFLRA 619
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 518-612 1.09e-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: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 518 RKGWLTINNIGIMKGGsKEYWFVLTAENLSWYKDDEEKEKKYMLSVD---NLKLRDVEKGfmSSKHIFALFNTEQRNVYk 594
Cdd:cd00821     1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPKGSIPlsgILEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                          90
                  ....*....|....*...
gi 1958759570 595 dyrqleLACETQEEVDSW 612
Cdd:cd00821    77 ------LQADSEEERQEW 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 743-860 2.78e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 2.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  743 TTTVSTPMPPPVDDSWLQVQSVPAG---------RRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPS 813
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958759570  814 RPGASPDPF-GPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:PHA03247  2910 QPQAPPPPQpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
PHA03378 PHA03378
EBNA-3B; Provisional
 759-860 7.23e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 56.23  E-value: 7.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 759 LQVQSVPAGRRSPTSSPTPQrRAPAVPPARPGSRGPAPGPPPAGSalgGAPPVPSRPGASPDPFGPPPQVPSRPnRAPPG 838
Cdd:PHA03378  685 LPIQWAPGTMQPPPRAPTPM-RPPAAPPGRAQRPAAATGRARPPA---AAPGRARPPAAAPGRARPPAAAPGRA-RPPAA 759

                          90       100
                  ....*....|....*....|....
gi 1958759570 839 VPSRKGP--ASPTRPAAPRPSEAP 860
Cdd:PHA03378  760 APGRARPpaAAPGAPTPQPPPQAP 783
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-863 7.94e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 7.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  747 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSalggAPPVPSRPGASPDPFG--- 823
Cdd:PHA03247  2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS----SPPQRPRRRAARPTVGslt 2696

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958759570  824 ----PPPQVP---SRPNRAPPGVPSRKG--------PASPTRPAAPRPSEAPLLD 863
Cdd:PHA03247  2697 sladPPPPPPtpePAPHALVSATPLPPGpaaarqasPALPAAPAPPAVPAGPATP 2751
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 751-859 2.06e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.99  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 751 PPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPS 830
Cdd:PRK07764  681 PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760

                          90       100
                  ....*....|....*....|....*....
gi 1958759570 831 RPNRAPPGVPSRKGPASPTRPAAPRPSEA 859
Cdd:PRK07764  761 PPAPAPAAAPAAAPPPSPPSEEEEMAEDD 789
PHA03378 PHA03378
EBNA-3B; Provisional
 748-860 1.04e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 52.76  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 748 TPMPPPvddswlqvQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG---- 823
Cdd:PHA03378  702 TPMRPP--------AAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAapga 773

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958759570 824 ----PPPQVPSRPNRAPPGVPS-RKGPASPTRPAAPRPSEAP 860
Cdd:PHA03378  774 ptpqPPPQAPPAPQQRPRGAPTpQPPPQAGPTSMQLMPRAAP 815
PHA03247 PHA03247
large tegument protein UL36; Provisional
 724-858 1.23e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  724 MLRMYHALKEALSIIGDINTTTVSTPMPPPVDDswlqvQSVPagrrspTSSPTPQRRAPAVPpARPGSRgpapgpppags 803
Cdd:PHA03247  2533 MLTWIRGLEELASDDAGDPPPPLPPAAPPAAPD-----RSVP------PPRPAPRPSEPAVT-SRARRP----------- 2589

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958759570  804 algGAPPVPSRPGASPDPFGPPPQvPSRPNRAPPGVPSRKGPASPTRPAAPRPSE 858
Cdd:PHA03247  2590 ---DAPPQSARPRAPVDDRGDPRG-PAPPSPLPPDTHAPDPPPPSPSPAANEPDP 2640
PHA03247 PHA03247
large tegument protein UL36; Provisional
 749-861 4.19e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 4.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  749 PMPPPVDDSwlqVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPppagsalGGAPPVPSRPGASPDPFGPP-PQ 827
Cdd:PHA03247  2683 PRRRAARPT---VGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAAR-------QASPALPAAPAPPAVPAGPAtPG 2752

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958759570  828 VPSRPNR-----APPGVPSRKGPASPTRPAAPRPSEAPL 861
Cdd:PHA03247  2753 GPARPARppttaGPPAPAPPAAPAAGPPRRLTRPAVASL 2791
PHA03378 PHA03378
EBNA-3B; Provisional
 747-846 4.22e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.84  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 747 STPMPPPvddswlqvQSVPAGRRSPTSSPTPQRrAPAVPPARPGSRGPAPGPPPAGSALGGAP---------PVP-SRPG 816
Cdd:PHA03378  721 TGRARPP--------AAAPGRARPPAAAPGRAR-PPAAAPGRARPPAAAPGRARPPAAAPGAPtpqpppqapPAPqQRPR 791

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958759570 817 ASPDPFgPPPQVPSRPNR-APPGVPSRKGPA 846
Cdd:PHA03378  792 GAPTPQ-PPPQAGPTSMQlMPRAAPGQQGPT 821
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 516-612 4.52e-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: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 516 VIRKGWLTinnigiMKGGS----KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKgfMSSKHIFALFNTEQRN 591
Cdd:cd01252     3 PDREGWLL------KLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958759570 592 VYKD----------------YRqleLACETQEEVDSW 612
Cdd:cd01252    75 VIKAcktdsdgkvvegnhtvYR---ISAASEEERDEW 108
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 747-860 5.54e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 50.10  E-value: 5.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 747 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGsrgpapgpppagsalggAPPVPSRPGASPDPFGPPP 826
Cdd:PRK14951  379 KTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAP-----------------PAPVAAPAAAAPAAAPAAA 441

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958759570 827 QVPSRPNRAPPGVPSRKGPASPTR----PAAPRPSEAP 860
Cdd:PRK14951  442 PAAVALAPAPPAQAAPETVAIPVRvapePAVASAAPAP 479
PHA03378 PHA03378
EBNA-3B; Provisional
 747-860 6.62e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.07  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 747 STPMPPPvddswlqvqSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPP 826
Cdd:PHA03378  692 GTMQPPP---------RAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPG 762

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958759570 827 QVP---SRPNRAPPGVPSRKGPASPTRP-AAPRPSEAP 860
Cdd:PHA03378  763 RARppaAAPGAPTPQPPPQAPPAPQQRPrGAPTPQPPP 800
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
 514-612 8.40e-06

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


Pssm-ID: 270110  Cd Length: 106  Bit Score: 45.31  E-value: 8.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 514 NQVIRKGWLtiNNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNL----KLRDVEKgfmssKHIFALFnTEQ 589
Cdd:cd13298     4 DRVLKSGYL--LKRSRKTKNWKKRWVVLRPCQLSYYKDEKEYKLRRVINLSELlavaPLKDKKR-----KNVFGIY-TPS 75

                          90       100
                  ....*....|....*....|...
gi 1958759570 590 RNVYkdyrqleLACETQEEVDSW 612
Cdd:cd13298    76 KNLH-------FRATSEKDANEW 91
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 765-862 1.39e-05

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 48.80  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 765 PAGRRSPTSSPTPQRRaPAVPPA---RPGSRGPAPGPPPAGSALGGA---------PPVPSRPGASPDPF----GPPPQV 828
Cdd:PHA03321  434 PAPRRDNDPPPPPRAR-PGSTPAcarRARAQRARDAGPEYVDPLGALrrlpagaapPPEPAAAPSPATYYtrmgGGPPRL 512

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958759570 829 PSRpNRAPpgvPSRKGPASPTRPAAPRPSEAPLL 862
Cdd:PHA03321  513 PPR-NRAT---ETLRPDWGPPAAAPPEQMEDPYL 542
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 748-860 2.08e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 748 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 827
Cdd:PRK07764  598 EGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAA 677

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958759570 828 VPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:PRK07764  678 PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP 710
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-861 2.80e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  748 TPMPPPVDDSwlqvQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGA-PPVPSRPGASPDPFGPPP 826
Cdd:PHA03247  2738 APAPPAVPAG----PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESrESLPSPWDPADPPAAVLA 2813

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958759570  827 QVPSRPNRAPPGV----PSRKGPASPTRPAAPRPSEAPL 861
Cdd:PHA03247  2814 PAAALPPAASPAGplppPTSAQPTAPPPPPGPPPPSLPL 2852
PHA03247 PHA03247
large tegument protein UL36; Provisional
 746-857 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 1958759570  746 VSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAP-PVPSRPGASPDPFG- 823
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPaGAGEPSGAVPQPWLg 2965

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958759570  824 --PPPQVPSRPNRAPPGVPSRKGPASPTRP----AAPRPS 857
Cdd:PHA03247  2966 alVPGRVAVPRFRVPQPAPSREAPASSTPPltghSLSRVS 3005
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 742-857 4.31e-05

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 45.75  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 742 NTTTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgpppagsalGGAPPVPSRPGasPDP 821
Cdd:pfam15822  52 STAPSTVPFGPAPTGMY---PSIPLTGPSPGPPAPFPPSGPSCPPP------------------GGPYPAPTVPG--PGP 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759570 822 FGPPPQvpsrPNRAPPGVPSRKGpaSPTRPAAPRPS 857
Cdd:pfam15822 109 IGPYPT----PNMPFPELPRPYG--APTDPAAAAPS 138
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
724-860 4.49e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.18  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 724 MLRMYhalkeALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAV-PPARPGSRGPAPG----- 797
Cdd:PRK12323  357 LLRML-----AFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAaAAARAVAAAPARRspape 431

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958759570 798 -----PPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRkgPASPTRPAAPRPSEAP 860
Cdd:PRK12323  432 alaaaRQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPA--RAAPAAAPAPADDDPP 497
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
 516-618 4.76e-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: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 516 VIRKGWLTINNiGIMKGGsKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMS-SKHIFALF---NTEQRN 591
Cdd:cd13378     3 VLKAGWLKKQR-SIMKNW-QQRWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNELPPNPEEpGKHLFEILpggAGDREK 80

                          90       100
                  ....*....|....*....|....*..
gi 1958759570 592 VYKDYRQLELACETQEEVDSWKASFLR 618
Cdd:cd13378    81 VPMNHEAFLLMANSQSDMEDWVKAIRR 107
PHA03247 PHA03247
large tegument protein UL36; Provisional
 743-855 5.90e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  743 TTTVSTPMPP--PVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSAlGGAPPVPSRPGASPD 820
Cdd:PHA03247  2763 TAGPPAPAPPaaPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPPTSAQPTAPPP 2841

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1958759570  821 PFGP-PPQVPSRPNRAPPGVPSRKGP--ASPTRPAAPR 855
Cdd:PHA03247  2842 PPGPpPPSLPLGGSVAPGGDVRRRPPsrSPAAKPAAPA 2879
PHA03247 PHA03247
large tegument protein UL36; Provisional
 761-859 6.98e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  761 VQSVPAGRRSPTSSPTPQR-----RAPAVPPARPGSRGPAPGPPPA---GSALGGAPPVPSrpGASPDPFGPPP--QVPS 830
Cdd:PHA03247   365 LEDLSAGRHHPKRASLPTRkrrsaRHAATPFARGPGGDDQTRPAAPvpaSVPTPAPTPVPA--SAPPPPATPLPsaEPGS 442

                           90       100
                   ....*....|....*....|....*....
gi 1958759570  831 RPNRAPPgvPSRKGPASPTRPAAPRPSEA 859
Cdd:PHA03247   443 DDGPAPP--PERQPPAPATEPAPDDPDDA 469
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-860 8.70e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 8.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  748 TPMPPPvdDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPFGP-PP 826
Cdd:PHA03247  2707 TPEPAP--HALVSATPLPPGPAAARQASPALPAAPAPPAV------------PAGPATPGGPARPARPPTTAGPPAPaPP 2772

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958759570  827 QVPSR--PNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:PHA03247  2773 AAPAAgpPRRLTRPAVASLSESRESLPSPWDPADPP 2808
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 748-857 9.38e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 9.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 748 TPMPPPVDDswlQVQSVPAGRRSPTSSPTPqrrAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPdpfgPPPQ 827
Cdd:PRK07764  407 AAAPAPAAA---APAAAAAPAPAAAPQPAP---APAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAA----APEP 476

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958759570 828 VPSRPNRAPPGVPSRKGPASPTRPAAPRPS 857
Cdd:PRK07764  477 TAAPAPAPPAAPAPAAAPAAPAAPAAPAGA 506
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 749-860 1.09e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  749 PMPPPVDD---SWLQVQSVPAGRRSPTSSP--TPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 823
Cdd:PHA03307   258 PRPAPITLptrIWEASGWNGPSSRPGPASSssSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958759570  824 PPPqVPSRPNRAPPGVPSRKGPASPT--RPAAPRPSEAP 860
Cdd:PHA03307   338 GAA-VSPGPSPSRSPSPSRPPPPADPssPRKRPRPSRAP 375
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 747-860 1.11e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.93  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  747 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAV---PPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 823
Cdd:PHA03307   805 SGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAarpPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPG 884

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958759570  824 PPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:PHA03307   885 AAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPMPPGGP 921
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 748-856 1.55e-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: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 748 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 827
Cdd:NF040712  218 EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAP 297

                          90       100
                  ....*....|....*....|....*....
gi 1958759570 828 VPSRPnrAPPGVPSRKGPASPTRPAAPRP 856
Cdd:NF040712  298 APAAP--AAPAAPEAEEPARPEPPPAPKP 324
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 744-860 1.97e-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: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 744 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTS-SPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 822
Cdd:NF040712  200 ATVPRLAREPADARPEEVEPAPAAEGAPATdSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958759570 823 GPPPQVPSRPNRAPPGVPSRKGPASPTRPAA---PRPSEAP 860
Cdd:NF040712  280 PPAPGAAETPEAAEPPAPAPAAPAAPAAPEAeepARPEPPP 320
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 516-612 2.25e-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: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 516 VIRKGWLTinnigiMKGGS-----KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGF-MSSKHIFALFNTEQ 589
Cdd:cd13248     7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                          90       100
                  ....*....|....*....|...
gi 1958759570 590 RNVYkdyrqleLACETQEEVDSW 612
Cdd:cd13248    81 RTYY-------FAADTAEEMEQW 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
 762-860 2.50e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  762 QSVPAGRRSPTSSPTPQRRAPAV----------PPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPqvPSR 831
Cdd:PHA03247  2670 LGRAAQASSPPQRPRRRAARPTVgsltsladppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV--PAG 2747

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958759570  832 PnrAPPGVPSRKG-PASPTRPAAPRPSEAP 860
Cdd:PHA03247  2748 P--ATPGGPARPArPPTTAGPPAPAPPAAP 2775
PHA03247 PHA03247
large tegument protein UL36; Provisional
 744-862 2.59e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  744 TTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQrrAPAVP--PARPgsrgpapgpppagsalgGAPPVPS---RPGAS 818
Cdd:PHA03247  2715 LVSATPLPPGPAAAR---QASPALPAAPAPPAVPA--GPATPggPARP-----------------ARPPTTAgppAPAPP 2772

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958759570  819 PDPFGPPPQVPSRPNRAP--PGVPSRKGPASPTRPAAPRPSEAPLL 862
Cdd:PHA03247  2773 AAPAAGPPRRLTRPAVASlsESRESLPSPWDPADPPAAVLAPAAAL 2818
PHA03247 PHA03247
large tegument protein UL36; Provisional
 749-860 3.60e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  749 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPQrrAPAVPPARPGSRGPAPGPPPAGSALGGAPP---VPSRPGASPDP---- 821
Cdd:PHA03247  2808 PAAVLAPAAALPPAASPAGPLPPPTSAQPT--APPPPPGPPPPSLPLGGSVAPGGDVRRRPPsrsPAAKPAAPARPpvrr 2885

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958759570  822 -FGPPPQVPSRPNRAPPGVPSR-KGPASPTRPAAPRPSEAP 860
Cdd:PHA03247  2886 lARPAVSRSTESFALPPDQPERpPQPQAPPPPQPQPQPPPP 2926
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 711-863 3.80e-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: 43.38  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 711 MEESAEQAQRRdemlrmyHALKEALSIIGDINTTTVSTPMPppvddSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPArpg 790
Cdd:pfam07174   1 MDQVDPNSTRR-------KGLWATLAIAAVAGASAVAVALP-----AVAHADPEPAPPPPSTATAPPAPPPPPPAPA--- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958759570 791 srGPAPGPPPAGSALGGAPPVPSRPGASP----DPFGPPPQvPSRPNRAPPG-VPSRKGPASPTRPAAPRPSEAPLLD 863
Cdd:pfam07174  66 --APAPPPPPAAPNAPNAPPPPADPNAPPpppaDPNAPPPP-AVDPNAPEPGrIDNAVGGFSYVVPAGWVESDATHLD 140
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 765-854 3.89e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.30  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 765 PAGRRSPTSSPTPQRraPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPFGP-PPQVPSRPNRaPPGVPSRK 843
Cdd:PTZ00449  591 PEEPKKPKRPRSAQR--PTRPKS------------PKLPELLDIPKSPKRPESPKSPKRPpPPQRPSSPER-PEGPKIIK 655

                          90
                  ....*....|.
gi 1958759570 844 GPASPTRPAAP 854
Cdd:PTZ00449  656 SPKPPKSPKPP 666
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 706-856 4.34e-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: 43.99  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 706 DQNTLMEESAEQA--QRRDEMLRMYHALKEALSIiGDINTTTVSTPMPPPvddswlQVQSVPAgRRSPTSSPTPQRRAPA 783
Cdd:pfam03154 153 DNESDSDSSAQQQilQTQPPVLQAQSGAASPPSP-PPPGTTQAATAGPTP------SAPSVPP-QGSPATSQPPNQTQST 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 784 VPPARPGSRGPAPGPPPAgsalggapPVPSRPGASPDPFGPPPQVPSRPNRAPP--------GVPSRKGPASPTRPAAPR 855
Cdd:pfam03154 225 AAPHTLIQQTPTLHPQRL--------PSPHPPLQPMTQPPPPSQVSPQPLPQPSlhgqmppmPHSLQTGPSHMQHPVPPQ 296


                  .
gi 1958759570 856 P 856
Cdd:pfam03154 297 P 297
PHA03247 PHA03247
large tegument protein UL36; Provisional
 753-864 4.37e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  753 PVDDSwlqvqsvPAGRRSPTSSPTPQRRAPAVPPArpgsrgpaPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVpSRP 832
Cdd:PHA03247  2601 PVDDR-------GDPRGPAPPSPLPPDTHAPDPPP--------PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRV-SRP 2664

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958759570  833 NRA-PPGVPSRKG--PASPTRPAAPrPSEAPLLDL 864
Cdd:PHA03247  2665 RRArRLGRAAQASspPQRPRRRAAR-PTVGSLTSL 2698
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
770-860 4.89e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 770 SPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPT 849
Cdd:PRK07003  405 AAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDA 484

                          90
                  ....*....|.
gi 1958759570 850 RPAAPRPSEAP 860
Cdd:PRK07003  485 PPDAAFEPAPR 495
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
746-860 5.53e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 746 VSTPMPPPVDDSWLQVQsvPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPppagsaLGGAPPVPSRPGASPDPFGPP 825
Cdd:PRK12323  451 APAPAAAPAAAARPAAA--GPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEE------LPPEFASPAPAQPDAAPAGWV 522

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958759570 826 PQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:PRK12323  523 AESIPDPATADPDDAFETLAPAPAAAPAPRAAAAT 557
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 749-863 6.58e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.16  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 749 PMPPPVDDSWLQVQSVPAGRRSPTSSPtpqrrAPAVPPARPGSRGPAPgpppagsalgGAPPVPSRPGASPDPFGPPPQV 828
Cdd:PRK14951  391 AAPVAQAAAAPAPAAAPAAAASAPAAP-----PAAAPPAPVAAPAAAA----------PAAAPAAAPAAVALAPAPPAQA 455

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958759570 829 PSRPNRAPPGVPSRKGPASPTRPAAPRPSEAPLLD 863
Cdd:PRK14951  456 APETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
Gag_MA pfam01140
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
 769-845 6.62e-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: 40.44  E-value: 6.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759570 769 RSPTSSPTPQRRAPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPfgPPPQVPSRPNRAPPGvPSRKGP 845
Cdd:pfam01140  64 KTRVFAPGPHGHPDQVPYI------------VTWEALAADPPPWVRPFLTPKP--PPPQPPAAPGLRPPL-PPASAP 125
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
 516-558 8.33e-04

Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called Differentially expressed in FDCP 6/DEF-6 or IRF4-binding protein) functions in cellular signal transduction pathways (in conjunction with Rac), regulates cell motility through actin rearrangement, and contributes to the transformation and invasion activity of mouse embryo fibroblasts. Metazoan SWAP-70 is found in B lymphocytes, mast cells, and in a variety of organs. Metazoan SWAP-70 contains an N-terminal EF-hand motif, a centrally located PH domain, and a C-terminal coiled-coil domain. The PH domain of Metazoan SWAP-70 contains a phosphoinositide-binding site and a nuclear localization signal (NLS), which localize SWAP-70 to the plasma membrane and nucleus, respectively. The NLS is a sequence of four Lys residues located at the N-terminus of the C-terminal a-helix; this is a unique characteristic of the Metazoan SWAP-70 PH domain. The SWAP-70 PH domain binds PtdIns(3,4,5)P3 and PtdIns(4,5)P2 embedded in lipid bilayer vesicles. There are additional plant SWAP70 proteins, but these are not included in this hierarchy. Rice SWAP70 (OsSWAP70) exhibits GEF activity toward the its Rho GTPase, OsRac1, and regulates chitin-induced production of reactive oxygen species and defense gene expression in rice. Arabidopsis SWAP70 (AtSWAP70) plays a role in both PAMP- and effector-triggered immunity. Plant SWAP70 contains both DH and PH domains, but their arrangement is the reverse of that in typical DH-PH-type Rho GEFs, wherein the DH domain is flanked by a C-terminal PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270092  Cd Length: 110  Bit Score: 39.59  E-value: 8.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958759570 516 VIRKGWLtinnigiMKGGSK-----EYWFVLTAENLSWYKDDEEKEKK 558
Cdd:cd13273     8 VIKKGYL-------WKKGHLlptwtERWFVLKPNSLSYYKSEDLKEKK 48
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 729-860 8.35e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 8.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  729 HALKEALSIIGDINTTTVSTPMPPPVDDSWLqvqsVPAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalGGA 808
Cdd:PHA03307    48 AELAAVTVVAGAAACDRFEPPTGPPPGPGTE----APANESRSTPTWSLSTLAPASPAREGSPT-------------PPG 110

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958759570  809 PPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:PHA03307   111 PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAV 162
PHA03247 PHA03247
large tegument protein UL36; Provisional
 775-860 8.73e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 8.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  775 PTPQRRAPAVPPARPGSRGPAPGPPPAGSalGGAPPVPSRpGASPDPFGPPPQVPSRPNRAPPGV--PSRKGpASPTRPA 852
Cdd:PHA03247   236 PFVERRVVISHPLRGDIAAPAPPPVVGEG--ADRAPETAR-GATGPPPPPEAAAPNGAAAPPDGVwgAALAG-APLALPA 311


                   ....*...
gi 1958759570  853 APRPSEAP 860
Cdd:PHA03247   312 PPDPPPPA 319
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 771-855 9.58e-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: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 771 PTSSPTPQrraPAVPPARPGsrgpapgpppagsalGGAPPVP---------SRPGASPDPFG--PPPQV-PSRPNraPPG 838
Cdd:pfam15822 163 PYPSPGPY---PAVPPPQSP---------------GAAPPVPwgtvppgpwGPPAPYPDPTGsyPMPGLyPTPNN--PFQ 222

                          90
                  ....*....|....*...
gi 1958759570 839 VPSrkGPA-SPTRPAAPR 855
Cdd:pfam15822 223 VPS--GPSgAPPMPGGPH 238
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 749-859 9.89e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 9.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  749 PMPPPVDDSWLQVQSVPA-GRRSPTSSPTP--QRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPP 825
Cdd:PHA03307   126 PPPSPAPDLSEMLRPVGSpGPPPAASPPAAgaSPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPR 205

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958759570  826 PQVPSRPNRAPPGVPsrkGPASPTRPAAPRPSEA 859
Cdd:PHA03307   206 PPRRSSPISASASSP---APAPGRSAADDAGASS 236
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 765-860 1.03e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.75  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 765 PAGRRSPTSSPTPQRRAPAVPPARpgsrgpapgpppagsalggaPPVPSRPGASPDPFGPP-PQVPSRPNRAPPgvPSRk 843
Cdd:PTZ00449  585 PKHPKDPEEPKKPKRPRSAQRPTR--------------------PKSPKLPELLDIPKSPKrPESPKSPKRPPP--PQR- 641

                          90
                  ....*....|....*..
gi 1958759570 844 gPASPTRPAAPRPSEAP 860
Cdd:PTZ00449  642 -PSSPERPEGPKIIKSP 657
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 743-864 1.13e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 743 TTTVSTPMPPPVDDSWLQVqSVPAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalggAPPVPSRPGASPDPF 822
Cdd:PRK14951  397 AAAAPAPAAAPAAAASAPA-APPAAAPPAPVAAPAAAAPAAAPAAAPAAV---------------ALAPAPPAQAAPETV 460

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958759570 823 GPPPQVPSRPNRAPPgvpsrkGPASPTRPAAPRPSEAPLLDL 864
Cdd:PRK14951  461 AIPVRVAPEPAVASA------APAPAAAPAAARLTPTEEGDV 496
PHA03247 PHA03247
large tegument protein UL36; Provisional
 767-860 1.45e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  767 GRRSPTSSPTPQRRAPA----------VPPaRPGSRGPAPGPPPAGSALGGAPPVP-SRPGASPDPFGPPPQ-------- 827
Cdd:PHA03247  2502 GPPDPDAPPAPSRLAPAilpdepvgepVHP-RMLTWIRGLEELASDDAGDPPPPLPpAAPPAAPDRSVPPPRpaprpsep 2580

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958759570  828 ----------VPSRPNR-----APPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:PHA03247  2581 avtsrarrpdAPPQSARprapvDDRGDPRGPAPPSPLPPDTHAPDPPP 2628
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 762-860 1.57e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 762 QSVPAGRRSPTSSPTPQRRAPAVPPARPGsrgpapgpppagsalGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPS 841
Cdd:PRK07764  383 RRLGVAGGAGAPAAAAPSAAAAAPAAAPA---------------PAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGN 447

                          90
                  ....*....|....*....
gi 1958759570 842 RKGPASPTRPAAPRPSEAP 860
Cdd:PRK07764  448 APAGGAPSPPPAAAPSAQP 466
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 748-861 1.58e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 748 TPMPPPVddswlqvqsvPAGRRSPTSSPTPQRRAPaVPParpgsrgpapgpppAGSALGGAPPVPSRPGAsPDPFGPPP- 826
Cdd:pfam03154 250 QPMTQPP----------PPSQVSPQPLPQPSLHGQ-MPP--------------MPHSLQTGPSHMQHPVP-PQPFPLTPq 303

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958759570 827 ----QVPSRPNRAPPGVPSRKGPASPTRPAAPR---PSEAPL 861
Cdd:pfam03154 304 ssqsQVPPGPSPAAPGQSQQRIHTPPSQSQLQSqqpPREQPL 345
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 743-860 1.67e-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: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 743 TTTVSTPMPPPVDDSWlQVQSVPAGRRSPTSSPT---------PQRRAPAVPPARPGSRGPAPGpppagsalggAPPV-- 811
Cdd:COG5180   247 ATVDAQPEMRPPADAK-ERRRAAIGDTPAAEPPGlpvleagsePQSDAPEAETARPIDVKGVAS----------APPAtr 315

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759570 812 PSRP-GASPDPFGP-PPQVPSRPNRAPP------GVPSRKGPASPTRPAAPRPSEAP 860
Cdd:COG5180   316 PVRPpGGARDPGTPrPGQPTERPAGVPEaasdagQPPSAYPPAEEAVPGKPLEQGAP 372
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 762-860 1.88e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 762 QSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPpagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPS 841
Cdd:PRK07764  395 AAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPA-------PAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPA 467

                          90
                  ....*....|....*....
gi 1958759570 842 RKGPASPTRPAAPRPSEAP 860
Cdd:PRK07764  468 PAPAAAPEPTAAPAPAPPA 486
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 752-860 2.02e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 752 PPVddswLQVQSVPAGRRSP-------TSSPTPQRRAPAVPPArpgsrgpapgpppagsalgGAPPVPSRPGASPDPFGP 824
Cdd:pfam03154 171 PPV----LQAQSGAASPPSPpppgttqAATAGPTPSAPSVPPQ-------------------GSPATSQPPNQTQSTAAP 227

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759570 825 PPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:pfam03154 228 HTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP 263
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 743-858 2.37e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  743 TTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 822
Cdd:PHA03307    89 TWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAAS 168

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958759570  823 GPPP----QVPSRPNRAPPGVPSRKGPASPTRPAAPRPSE 858
Cdd:PHA03307   169 SRQAalplSSPEETARAPSSPPAEPPPSTPPAAASPRPPR 208
DUF4813 pfam16072
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ...
 743-842 2.79e-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: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 743 TTTVSTPMPPPVDDSWLQVQSVPAG--RRSPTSSPTPQRRAPAVP--PARPGSRGPAPGPPPAGSALGGAP------PVP 812
Cdd:pfam16072 158 TTVINAGGQQPAAPAAPAYPVAPAAypAQAPAAAPAPAPGAPQTPlaPLNPVAAAPAAAAGAAAAPVVAAAapaaaaPPP 237

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759570 813 SRPGAsPDPFGPPPQ------VPSRPNRAPPGVPSR 842
Cdd:pfam16072 238 PAPAA-PPADAAPPApggiicVPVRVPEPDPKDATK 272
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 745-854 2.80e-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: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 745 TVSTPMPPPVddswlqvqsvPAGRRSPTSSPTPQrrAPAVPPARPGSRGPapgpppagsalgGAPPVPSRPGASPDPfGP 824
Cdd:pfam06346  42 SAAIPPPPPL----------PGGTSIPPPPPLPG--AASIPPPPPLPGST------------GIPPPPPLPGGAGIP-PP 96

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958759570 825 PPQVPSRPNRAPPGVPSRKGPASPTRPAAP 854
Cdd:pfam06346  97 PPPLPGGAGVPPPPPPLPGGPGIPPPPPFP 126
PHA02030 PHA02030
hypothetical protein
 749-854 2.84e-03

hypothetical protein


Pssm-ID: 222843 [Multi-domain]  Cd Length: 336  Bit Score: 40.73  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 749 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARpgsrgpapgpppagsalgGAPPVPSRPGASpdpfgPPPQV 828
Cdd:PHA02030  254 IIKPKSKAAGSNLPAVPNVAADAGSAAAPAVPAAAAAVAQ------------------AAPSVPQVPNVA-----VLPDV 310

                          90       100
                  ....*....|....*....|....*.
gi 1958759570 829 PSRPNRAPPGVPsrKGPASPTRPAAP 854
Cdd:PHA02030  311 PQVAPVAAPAAP--EVPAVPVVPAAP 334
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 721-859 3.03e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  721 RDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSwlqvqSVPAGRRSPTSSPTPqrRAPAVPPARPGSRGPAPGPPP 800
Cdd:PHA03307   252 ENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSS-----SSPRERSPSPSPSSP--GSGPAPSSPRASSSSSSSRES 324

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958759570  801 AGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEA 859
Cdd:PHA03307   325 SSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAG 383
Aim21 pfam11489
Altered inheritance of mitochondria protein 21; This is a family of proteins conserved in ...
 744-863 3.05e-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: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 744 TTVSTP----MPPPVDDSWLQVQSVPAGRRSPtsSPTPQRRAPAVP-------PARPGSRGPAPGPPPAGSAlggaPPVP 812
Cdd:pfam11489 502 TTVETPdevkSTSPGVPTKPAIPARPKSGKPT--SPTEKRKPPPVPkkpkpqiPARPAKAQPQQAGEEFKPK----PRVP 575

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958759570 813 SRPGASP-------------DPFGPPPQVPSRPNRAPpgvPSRKGPASPTRPAAPRPSEAPLLD 863
Cdd:pfam11489 576 ARPGGSKisalragfasdlnGRLQLGPQAPKKVVEED---KEPSEEKGDKEEEEDTKEKAPLSD 636
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 762-860 3.94e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 762 QSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPagsalGGAPPVPSRPGAspdpfGPPPQVPSRPNRAPPGvps 841
Cdd:PRK07764  420 AAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPP-----AAAPSAQPAPAP-----AAAPEPTAAPAPAPPA--- 486

                          90
                  ....*....|....*....
gi 1958759570 842 rkGPASPTRPAAPRPSEAP 860
Cdd:PRK07764  487 --APAPAAAPAAPAAPAAP 503
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 739-861 4.11e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  739 GDINTTTVSTPMPPPVDDSwlqvqsvpAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGAS 818
Cdd:PHA03307   107 TPPGPSSPDPPPPTPPPAS--------PPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSS 178

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958759570  819 PD---PFGPPPQVPSRPNRAPPGVPSR-KGPASPTRPAAPRPSEAPL 861
Cdd:PHA03307   179 PEetaRAPSSPPAEPPPSTPPAAASPRpPRRSSPISASASSPAPAPG 225
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 537-612 4.18e-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: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 537 YWFVLTAENLS-W-YKDDEEKeKKYMLSVD-----NLKLRDVEKGFMSSKHIFAL-FNTEQRNVYKDYRQLE----LACE 604
Cdd:cd01263    23 RWCVLRGGYLSfWkYPDDEEK-KKPIGSIDltkciTEKVEPAPRELCARPNTFLLeTLRPAEDDDRDDTNEKirvlLSAD 101


                  ....*...
gi 1958759570 605 TQEEVDSW 612
Cdd:cd01263   102 TKEERIEW 109
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
747-860 4.44e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.60  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 747 STPMPPPVDDSWLQVQSV---PAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 823
Cdd:PRK07003  421 TRAEAPPAAPAPPATADRgddAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPS 500

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958759570 824 PPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:PRK07003  501 AATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTP 537
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 749-863 5.15e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.84  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 749 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPqrrAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSR-PGASPDPfGPPPQ 827
Cdd:PHA02682   84 PSPACAAPAPACPACAPAAPAPAVTCPAP---APACPPATAPTCPPPAVCPAPARPAPACPPSTRQcPPAPPLP-TPKPA 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958759570 828 VPSRP-----NRAPPGVPSRKGPASPTRPAAprpseAPLLD 863
Cdd:PHA02682  160 PAAKPiflhnQLPPPDYPAASCPTIETAPAA-----SPVLE 195
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
748-860 5.68e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 748 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQrRAPAVPPArpgsrgpaPGPPPAGSALGGAPPVPSRPGA--SPDPFGPP 825
Cdd:PRK12323  427 SPAPEALAAARQASARGPGGAPAPAPAPAAA-PAAAARPA--------AAGPRPVAAAAAAAPARAAPAAapAPADDDPP 497

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759570 826 PQVPSRPNRAPPGV-PSRKGPASPTRPAAPRPSEAP 860
Cdd:PRK12323  498 PWEELPPEFASPAPaQPDAAPAGWVAESIPDPATAD 533
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 765-862 5.88e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.46  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 765 PAGRRSPTSSPTPQRRAPAVPPARPGSRGPApgpppagsalggapPVPSRPGASPdPFGPPPQVPSRPNRAPPGVP--SR 842
Cdd:PHA02682   81 PLAPSPACAAPAPACPACAPAAPAPAVTCPA--------------PAPACPPATA-PTCPPPAVCPAPARPAPACPpsTR 145

                          90       100
                  ....*....|....*....|.
gi 1958759570 843 KGPASPTRPAA-PRPSEAPLL 862
Cdd:PHA02682  146 QCPPAPPLPTPkPAPAAKPIF 166
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 765-861 5.96e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570  765 PAGRRSPTSSPTPQrrAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPN--RAPPGVPSR 842
Cdd:PHA03307   846 PPARSSESSKSKPA--AAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKlgPMPPGGPDP 923

                           90       100
                   ....*....|....*....|....
gi 1958759570  843 KG-----PASPTRPaaPRPSEAPL 861
Cdd:PHA03307   924 RGgfrrvPPGDLHT--PAPSAAAL 945
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
 768-861 6.61e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 39.49  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 768 RRSPTSSPTPQRRAPavPPARPGSRGPAPGPPPagsalggAPPVPSRPGASPDP--FGPPPQVPSRPNRAPPGVPSrkGP 845
Cdd:PHA03201    2 KRARSRSPSPPRRPS--PPRPTPPRSPDASPEE-------TPPSPPGPGAEPPPgrAAGPAAPRRRPRGCPAGVTF--SS 70

                          90       100
                  ....*....|....*....|.
gi 1958759570 846 ASPTRPA-----APRPSEAPL 861
Cdd:PHA03201   71 SAPPRPPlglddAPAATPPPL 91
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
744-860 6.74e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 6.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 744 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 823
Cdd:PRK07003  405 AAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDA 484

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958759570 824 PP-------PQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:PRK07003  485 PPdaafepaPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPP 528
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 807-860 6.74e-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: 6.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958759570 807 GAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASPTRPAAPRPSEAP 860
Cdd:pfam15240  71 GGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGP 124
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 758-860 6.86e-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: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 758 WLQVQSvpAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPP 837
Cdd:NF041121   10 WLAAQM--GRAAAPPSPEGPAPTAASQPATPPPPA--------------APPSPPGDPPEPPAPEPAPLPAPYPGSLAPP 73

                          90       100
                  ....*....|....*....|...
gi 1958759570 838 GVPSRKgpASPTRPAAPRPSEAP 860
Cdd:NF041121   74 PPPPPG--PAGAAPGAALPVRVP 94
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 749-860 7.07e-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: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 749 PMPPPVDDSWlqvQSVPAGRRSPTSSPTPQRrAPAVPPARPGSRgpapgpPPAGSALGGAPPVPSRPGASPDPFGPPPQV 828
Cdd:pfam15240  65 PGPPPPGGPQ---QPPPQGGKQKPQGPPPQG-GPRPPPGKPQGP------PPQGGNQQQGPPPPGKPQGPPPQGGGPPPQ 134

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958759570 829 PSRPNRAPPGVPSR-KGPasPTRPAAP-RPSEAP 860
Cdd:pfam15240 135 GGNQQGPPPPPPGNpQGP--PQRPPQPgNPQGPP 166
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 764-860 7.15e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 764 VPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPagsalggAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRK 843
Cdd:PRK07764  387 VAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAP-------APAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPA 459

                          90
                  ....*....|....*..
gi 1958759570 844 GPASPTRPAAPRPSEAP 860
Cdd:PRK07764  460 AAPSAQPAPAPAAAPEP 476
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 745-861 7.67e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.07  E-value: 7.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759570 745 TVSTPMPPPVDDSWLQVQSVP-AGR----RSPTSSPTPQRR------APAVPPARPGSRGPAPgpppagsalggAPP--V 811
Cdd:PHA02682   36 APAAPCPPDADVDPLDKYSVKeAGRyyqsRLKANSACMQRPsgqsplAPSPACAAPAPACPAC-----------APAapA 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958759570 812 PSRPGASPDPFGPPPQVPSRPNRAPPGVPSRKGPASP--TR---PAAPRPSEAPL 861
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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