NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958759562|ref|XP_038960071|]
View 

dynamin-1 isoform X4 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 3.15e-154

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


:

Pssm-ID: 197491  Cd Length: 240  Bit Score: 451.64  E-value: 3.15e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562    6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562   86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  166 KENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGK 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 9.79e-148

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


:

Pssm-ID: 460033  Cd Length: 287  Bit Score: 436.56  E-value: 9.79e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958759562 455 EMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 520-629 1.11e-83

Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle formation. It has an N-terminal GTPase domain, followed by a PH domain, a GTPase effector domain and a C-terminal proline arginine rich domain. Dynamin-like proteins, which are found in metazoa, plants and yeast have the same domain architecture as dynamin, but lack the PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269958  Cd Length: 112  Bit Score: 263.03  E-value: 1.11e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 520 VIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKD 599
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958759562 600 YRQLELACETQEEVDSWKASFLRAGVYPER 629
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
655-745 5.73e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 124.93  E-value: 5.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 655 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1958759562 735 LKEALSIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03378 super family cl33729
EBNA-3B; Provisional
 752-863 1.71e-08

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 58.54  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 752 TPMPPPvddswlqvQSVPAGRRSPTSSPTPQRRAPAVP-PARPGSRGPAPGPPPAgsalgGAPPVPSRPGASPDPFGPPP 830
Cdd:PHA03378  702 TPMRPP--------AAPPGRAQRPAAATGRARPPAAAPgRARPPAAAPGRARPPA-----AAPGRARPPAAAPGRARPPA 768

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958759562 831 QVPSRPNRAPPgvPRKGPASPTRP-AAPRPSEAP 863
Cdd:PHA03378  769 AAPGAPTPQPP--PQAPPAPQQRPrGAPTPQPPP 800
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 3.15e-154

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 451.64  E-value: 3.15e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562    6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562   86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  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 6.97e-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: 6.97e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFLHCKGKKFTDFEEVRLE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 181 LANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958759562 258 FFLSHPSYRHL-ADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:cd08771   241 FFETHPWYKLLpASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 9.79e-148

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


Pssm-ID: 460033  Cd Length: 287  Bit Score: 436.56  E-value: 9.79e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958759562 455 EMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 520-629 1.11e-83

Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle formation. It has an N-terminal GTPase domain, followed by a PH domain, a GTPase effector domain and a C-terminal proline arginine rich domain. Dynamin-like proteins, which are found in metazoa, plants and yeast have the same domain architecture as dynamin, but lack the PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269958  Cd Length: 112  Bit Score: 263.03  E-value: 1.11e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 520 VIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKD 599
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958759562 600 YRQLELACETQEEVDSWKASFLRAGVYPER 629
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 2.18e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 221.34  E-value: 2.18e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFlhckGKKFTDFEEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 106 DRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQppdiefqirDMLMQFVtKENCLILAVSPANSDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 1958759562 186 ALKIAKEVDPQGQRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 5.73e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 124.93  E-value: 5.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 655 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1958759562 735 LKEALSIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 9.16e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 107.32  E-value: 9.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  654 QLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYH 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1958759562  734 ALKEALSIIGDI 745
Cdd:smart00302  81 LLKKARQIIAAV 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 520-623 1.28e-11

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 61.81  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 520 VIRKGWLTINNIGImKGGSKEYWFVLTAENLSWYKDD---EEKEKKYMLSVDNLKLRDVEKGFMSS-KHIFALFNTEQRN 595
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1958759562 596 VykdyRQLELACETQEEVDSWKASFLRA 623
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 520-623 2.52e-11

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 61.03  E-value: 2.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  520 VIRKGWLTINNIGiMKGGSKEYWFVLTAENLSWYKDDEEKEK---KYMLSVDNLKLRDVEKGFMSS-KHIFALfnteqrn 595
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1958759562  596 VYKDYRQLELACETQEEVDSWKASFLRA 623
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PHA03378 PHA03378
EBNA-3B; Provisional
 752-863 1.71e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 58.54  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 752 TPMPPPvddswlqvQSVPAGRRSPTSSPTPQRRAPAVP-PARPGSRGPAPGPPPAgsalgGAPPVPSRPGASPDPFGPPP 830
Cdd:PHA03378  702 TPMRPP--------AAPPGRAQRPAAATGRARPPAAAPgRARPPAAAPGRARPPA-----AAPGRARPPAAAPGRARPPA 768

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958759562 831 QVPSRPNRAPPgvPRKGPASPTRP-AAPRPSEAP 863
Cdd:PHA03378  769 AAPGAPTPQPP--PQAPPAPQQRPrGAPTPQPPP 800
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 747-863 8.16e-06

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 48.06  E-value: 8.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 747 TTTVSTPMPPPVDDSWlqvqsvpagrrsPTSSPtpqRRAPAVPPArpGSRGPAPGPPPAGSALGGAPP--VPSRPGASPD 824
Cdd:pfam15822  15 TSAVSNPKPGQPPQGW------------PGSNP---WNNPSAPPA--VPSGLPPSTAPSTVPFGPAPTgmYPSIPLTGPS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958759562 825 PFGPPPQVPSRPNRAPPG-------VPRKGPASPTR------PAAPRPSEAP 863
Cdd:pfam15822  78 PGPPAPFPPSGPSCPPPGgpypaptVPGPGPIGPYPtpnmpfPELPRPYGAP 129
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 748-861 2.59e-04

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


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 43.99  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 748 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTS-SPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 826
Cdd:NF040712  200 ATVPRLAREPADARPEEVEPAPAAEGAPATdSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958759562 827 GPPPQVPSRPNRAPPGVPRkgPASPTRPAAPRPSE 861
Cdd:NF040712  280 PPAPGAAETPEAAEPPAPA--PAAPAAPAAPEAEE 312
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 752-859 1.21e-03

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: 42.06  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:NF040712  218 EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAP 297

                          90       100
                  ....*....|....*....|....*....
gi 1958759562 832 VPSRPnrAPPGVPR-KGPASPTRPAAPRP 859
Cdd:NF040712  298 APAAP--AAPAAPEaEEPARPEPPPAPKP 324
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 762-863 5.05e-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: 40.37  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 762 WLQVQSvpAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPP 841
Cdd:NF041121   10 WLAAQM--GRAAAPPSPEGPAPTAASQPATPPPPA--------------APPSPPGDPPEPPAPEPAPLPAPYPGSLAPP 73

                          90       100
                  ....*....|....*....|..
gi 1958759562 842 GVPRKGPAsPTRPAAPRPSEAP 863
Cdd:NF041121   74 PPPPPGPA-GAAPGAALPVRVP 94
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 769-863 5.86e-03

N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 39.03  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 769 PAGRRSPT--SSPTPQRRAPAVP-PARPGsrgpapgpppagsalgGAPPVPSRPGASPDPFGPppqvpsrpNRAPPGVPR 845
Cdd:cd21576   116 PARGSSPTlgSEPAPASGEDAVSgPESSF----------------GAPAIPSAPAAPGAPAVS--------GEVPGGAPG 171

                          90
                  ....*....|....*...
gi 1958759562 846 KGPASPTRPAAPRPSEAP 863
Cdd:cd21576   172 AGPAPAAGPAPRRRPVTP 189
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 3.15e-154

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 451.64  E-value: 3.15e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562    6 MEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562   86 CKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  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 6.97e-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: 6.97e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  29 LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFLHCKGKKFTDFEEVRLE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 101 IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 181 LANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958759562 258 FFLSHPSYRHL-ADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:cd08771   241 FFETHPWYKLLpASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 9.79e-148

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


Pssm-ID: 460033  Cd Length: 287  Bit Score: 436.56  E-value: 9.79e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 215 DARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 295 GLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSgDQIDTYELSGGARINRIFHERFPFEL 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 375 VKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLRE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958759562 455 EMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 520-629 1.11e-83

Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle formation. It has an N-terminal GTPase domain, followed by a PH domain, a GTPase effector domain and a C-terminal proline arginine rich domain. Dynamin-like proteins, which are found in metazoa, plants and yeast have the same domain architecture as dynamin, but lack the PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269958  Cd Length: 112  Bit Score: 263.03  E-value: 1.11e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 520 VIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKD 599
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKD 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958759562 600 YRQLELACETQEEVDSWKASFLRAGVYPER 629
Cdd:cd01256    83 YKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 2.18e-67

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 221.34  E-value: 2.18e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNS--------TTEYAEFlhckGKKFTDFEEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 106 DRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQppdiefqirDMLMQFVtKENCLILAVSPANSDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 1958759562 186 ALKIAKEVDPQGQRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
655-745 5.73e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 124.93  E-value: 5.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 655 LERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHA 734
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1958759562 735 LKEALSIIGDI 745
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
654-745 9.16e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 107.32  E-value: 9.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  654 QLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYH 733
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1958759562  734 ALKEALSIIGDI 745
Cdd:smart00302  81 LLKKARQIIAAV 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 520-623 1.28e-11

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 61.81  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 520 VIRKGWLTINNIGImKGGSKEYWFVLTAENLSWYKDD---EEKEKKYMLSVDNLKLRDVEKGFMSS-KHIFALFNTEQRN 595
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1958759562 596 VykdyRQLELACETQEEVDSWKASFLRA 623
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 520-623 2.52e-11

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 61.03  E-value: 2.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  520 VIRKGWLTINNIGiMKGGSKEYWFVLTAENLSWYKDDEEKEK---KYMLSVDNLKLRDVEKGFMSS-KHIFALfnteqrn 595
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1958759562  596 VYKDYRQLELACETQEEVDSWKASFLRA 623
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 522-616 1.10e-09

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


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 56.01  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 522 RKGWLTINNIGIMKGGsKEYWFVLTAENLSWYKDDEEKEKKYMLSVD---NLKLRDVEKGfmSSKHIFALFNTEQRNVYk 598
Cdd:cd00821     1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPKGSIPlsgILEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                          90
                  ....*....|....*...
gi 1958759562 599 dyrqleLACETQEEVDSW 616
Cdd:cd00821    77 ------LQADSEEERQEW 88
PHA03378 PHA03378
EBNA-3B; Provisional
 752-863 1.71e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 58.54  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 752 TPMPPPvddswlqvQSVPAGRRSPTSSPTPQRRAPAVP-PARPGSRGPAPGPPPAgsalgGAPPVPSRPGASPDPFGPPP 830
Cdd:PHA03378  702 TPMRPP--------AAPPGRAQRPAAATGRARPPAAAPgRARPPAAAPGRARPPA-----AAPGRARPPAAAPGRARPPA 768

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958759562 831 QVPSRPNRAPPgvPRKGPASPTRP-AAPRPSEAP 863
Cdd:PHA03378  769 AAPGAPTPQPP--PQAPPAPQQRPrGAPTPQPPP 800
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-863 3.17e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 3.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  747 TTTVSTPMPPPVDDSWLQVQSVPAG---------RRSPTSSPTPQRRAPAVPPARpGSRGPAPGPPPAGSALGGAPPVPS 817
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPPDQPERP 2908

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958759562  818 RPGASPDPFGPPPQVPSRPNRAPPGVPrkgPASPTRPAAPRPSEAP 863
Cdd:PHA03247  2909 PQPQAPPPPQPQPQPPPPPQPQPPPPP---PPRPQPPLAPTTDPAG 2951
PHA03378 PHA03378
EBNA-3B; Provisional
 763-863 8.05e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 56.23  E-value: 8.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 763 LQVQSVPAGRRSPTSSPTPQRrAPAVPPARPGSRGPAPGPPPAGSalgGAPPVPSRPGASPDPFGPPPQVPS--RPNRAP 840
Cdd:PHA03378  685 LPIQWAPGTMQPPPRAPTPMR-PPAAPPGRAQRPAAATGRARPPA---AAPGRARPPAAAPGRARPPAAAPGraRPPAAA 760

                          90       100
                  ....*....|....*....|...
gi 1958759562 841 PGVPRKGPASPTRPAAPRPSEAP 863
Cdd:PHA03378  761 PGRARPPAAAPGAPTPQPPPQAP 783
PHA03247 PHA03247
large tegument protein UL36; Provisional
 751-866 2.02e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  751 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAgsalGGAPPVPSRPGASPDPFG--- 827
Cdd:PHA03247  2621 THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQ----ASSPPQRPRRRAARPTVGslt 2696

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958759562  828 ----PPPQVP---SRPNRAPPGVP---------RKGPASPTRPAAPRPSEAPLLD 866
Cdd:PHA03247  2697 sladPPPPPPtpePAPHALVSATPlppgpaaarQASPALPAAPAPPAVPAGPATP 2751
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
749-863 8.71e-07

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 52.57  E-value: 8.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 749 TVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAP-AVPPARPGSRGPApgpppagsalGGAPPVPSRPGASPDPFG 827
Cdd:PRK12323  393 AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPeALAAARQASARGP----------GGAPAPAPAPAAAPAAAA 462

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759562 828 PPPQVPSRPNrAPPGVPRKGPASPTRPAAPRPSEAP 863
Cdd:PRK12323  463 RPAAAGPRPV-AAAAAAAPARAAPAAAPAPADDDPP 497
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 755-863 1.16e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 52.30  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 755 PPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPs 834
Cdd:PRK07764  681 PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP- 759

                          90       100
                  ....*....|....*....|....*....
gi 1958759562 835 rpnraPPGVPRKGPASPTRPAAPRPSEAP 863
Cdd:PRK07764  760 -----PPPAPAPAAAPAAAPPPSPPSEEE 783
PHA03247 PHA03247
large tegument protein UL36; Provisional
 753-864 1.93e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  753 PMPPPVDDSwlqVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPppagsalGGAPPVPSRPGASPDPFGP---- 828
Cdd:PHA03247  2683 PRRRAARPT---VGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAAR-------QASPALPAAPAPPAVPAGPatpg 2752

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958759562  829 ---PPQVPSRPNRAPPGVPRKGPASPTRPAAPRPSEAPL 864
Cdd:PHA03247  2753 gpaRPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 751-867 3.56e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 50.48  E-value: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 751 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPP 830
Cdd:PRK14951  379 KTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPE 458

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958759562 831 QVPSRPNRAP-PGVPRKGPASPTRPAAPRPSEAPLLDL 867
Cdd:PRK14951  459 TVAIPVRVAPePAVASAAPAPAAAPAAARLTPTEEGDV 496
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 520-616 4.58e-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: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 520 VIRKGWLTinnigiMKGGS----KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKgfMSSKHIFALFNTEQRN 595
Cdd:cd01252     3 PDREGWLL------KLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958759562 596 VYKD----------------YRqleLACETQEEVDSW 616
Cdd:cd01252    75 VIKAcktdsdgkvvegnhtvYR---ISAASEEERDEW 108
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 747-863 8.16e-06

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 48.06  E-value: 8.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 747 TTTVSTPMPPPVDDSWlqvqsvpagrrsPTSSPtpqRRAPAVPPArpGSRGPAPGPPPAGSALGGAPP--VPSRPGASPD 824
Cdd:pfam15822  15 TSAVSNPKPGQPPQGW------------PGSNP---WNNPSAPPA--VPSGLPPSTAPSTVPFGPAPTgmYPSIPLTGPS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958759562 825 PFGPPPQVPSRPNRAPPG-------VPRKGPASPTR------PAAPRPSEAP 863
Cdd:pfam15822  78 PGPPAPFPPSGPSCPPPGgpypaptVPGPGPIGPYPtpnmpfPELPRPYGAP 129
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 751-866 1.52e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.83  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 751 STPMPPPVDDSWLQvqsvPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPP 830
Cdd:PRK07764  679 AAPPPAPAPAAPAA----PAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGA 754

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759562 831 QVPSRPNRAPPgvPRKGPASPTRPAAPRPSEAPLLD 866
Cdd:PRK07764  755 PAQPPPPPAPA--PAAAPAAAPPPSPPSEEEEMAED 788
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 746-860 1.69e-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: 47.29  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 746 NTTTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgpppagsalGGAPPVPSRPGasPDP 825
Cdd:pfam15822  52 STAPSTVPFGPAPTGMY---PSIPLTGPSPGPPAPFPPSGPSCPPP------------------GGPYPAPTVPG--PGP 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958759562 826 FGPPPQvpsrPNRAPPGVPRKGPAsPTRPAAPRPS 860
Cdd:pfam15822 109 IGPYPT----PNMPFPELPRPYGA-PTDPAAAAPS 138
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 769-865 1.72e-05

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 48.42  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 769 PAGRRSPTSSPTPQRRaPAVPPA---RPGSRGPAPGPPPAGSALGGA---------PPVPSRPGASPDPF----GPPPQV 832
Cdd:PHA03321  434 PAPRRDNDPPPPPRAR-PGSTPAcarRARAQRARDAGPEYVDPLGALrrlpagaapPPEPAAAPSPATYYtrmgGGPPRL 512

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958759562 833 PSRpNRAPPgvPRKGPASPTRPAAPRPSEAPLL 865
Cdd:PHA03321  513 PPR-NRATE--TLRPDWGPPAAAPPEQMEDPYL 542
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 752-863 1.82e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 752 TPMPPPVDDswlQVQSVPAGRRSPTSSPTPqrrAPAVPPARPGSRGPAPGpppagsalgGAPPVPSRPGASPDPFGPPPQ 831
Cdd:PRK07764  407 AAAPAPAAA---APAAAAAPAPAAAPQPAP---APAPAPAPPSPAGNAPA---------GGAPSPPPAAAPSAQPAPAPA 471

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958759562 832 VPSRPNRAPPGVPRKGPASPTRPAAPRPSEAP 863
Cdd:PRK07764  472 AAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAP 503
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
 539-616 2.61e-05

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


Pssm-ID: 270110  Cd Length: 106  Bit Score: 43.77  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 539 KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNL----KLRDVEKgfmssKHIFALFnTEQRNVYkdyrqleLACETQEEVD 614
Cdd:cd13298    23 KKRWVVLRPCQLSYYKDEKEYKLRRVINLSELlavaPLKDKKR-----KNVFGIY-TPSKNLH-------FRATSEKDAN 89


                  ..
gi 1958759562 615 SW 616
Cdd:cd13298    90 EW 91
PHA03247 PHA03247
large tegument protein UL36; Provisional
 728-860 4.05e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  728 MLRMYHALKEALSIIGDINTTTVSTPMPPPVDDswlqvQSVPAGRRSP-TSSPTPQRRA--PAVPPARPGSRGPAPGPPP 804
Cdd:PHA03247  2533 MLTWIRGLEELASDDAGDPPPPLPPAAPPAAPD-----RSVPPPRPAPrPSEPAVTSRArrPDAPPQSARPRAPVDDRGD 2607

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  805 AGsalGGAPPVPSRPGAS-PDPfgPPPQVPSRPNRAPPGVPRKGPASP---TRPAAPRPS 860
Cdd:PHA03247  2608 PR---GPAPPSPLPPDTHaPDP--PPPSPSPAANEPDPHPPPTVPPPErprDDPAPGRVS 2662
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
 520-622 4.77e-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: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 520 VIRKGWLTINNiGIMKGGsKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMS-SKHIFALF---NTEQRN 595
Cdd:cd13378     3 VLKAGWLKKQR-SIMKNW-QQRWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNELPPNPEEpGKHLFEILpggAGDREK 80

                          90       100
                  ....*....|....*....|....*..
gi 1958759562 596 VYKDYRQLELACETQEEVDSWKASFLR 622
Cdd:cd13378    81 VPMNHEAFLLMANSQSDMEDWVKAIRR 107
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 752-863 4.85e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGA-PPVPSRPGASPDPFGPPP 830
Cdd:PRK07764  598 EGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAvPDASDGGDGWPAKAGGAA 677

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958759562 831 QVPSRPNRAPPGVPRKGPASPTRPAAPRPSEAP 863
Cdd:PRK07764  678 PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP 710
PHA03378 PHA03378
EBNA-3B; Provisional
 751-849 5.53e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.98  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 751 STPMPPPvddswlqvQSVPAGRRSPTSSPTPQRrAPAVPPARPGSRGPAPGPPPAGSALGGAP---------PVP-SRPG 820
Cdd:PHA03378  721 TGRARPP--------AAAPGRARPPAAAPGRAR-PPAAAPGRARPPAAAPGRARPPAAAPGAPtpqpppqapPAPqQRPR 791

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958759562 821 ASPDPFgPPPQVPSRP----NRAPPGvpRKGPA 849
Cdd:PHA03378  792 GAPTPQ-PPPQAGPTSmqlmPRAAPG--QQGPT 821
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 751-863 7.17e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 7.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  751 STPMPPPVDDSWLQVQSVPAGRRSPTSSPtpqRRAPAVPPARpgsrgpapgpppagsaLGGAPPVPSRPGASPDPfgPPP 830
Cdd:PHA03307   307 PAPSSPRASSSSSSSRESSSSSTSSSSES---SRGAAVSPGP----------------SPSRSPSPSRPPPPADP--SSP 365

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958759562  831 QVPSRPNRAPPGvPRKGPASPTRPAApRPSEAP 863
Cdd:PHA03307   366 RKRPRPSRAPSS-PAASAGRPTRRRA-RAAVAG 396
PHA03247 PHA03247
large tegument protein UL36; Provisional
 752-864 7.38e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 7.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  752 TPMPPPVDDSwlqvQSVPAGRRSPTSSPTPQR-------RAPAVPPARPGSRGpapgpppagsalGGAPPVPSRPGA--S 822
Cdd:PHA03247  2738 APAPPAVPAG----PATPGGPARPARPPTTAGppapappAAPAAGPPRRLTRP------------AVASLSESRESLpsP 2801

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958759562  823 PDPFGPPPQVPSR----PNRAPPGVPRKGPASPTrPAAPRPSEAPL 864
Cdd:PHA03247  2802 WDPADPPAAVLAPaaalPPAASPAGPLPPPTSAQ-PTAPPPPPGPP 2846
PHA03247 PHA03247
large tegument protein UL36; Provisional
 752-862 9.83e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 9.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  752 TPMPPPvdDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPagsalgGAPPVPSRPGASPDPFGPppq 831
Cdd:PHA03247  2707 TPEPAP--HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARP------ARPPTTAGPPAPAPPAAP--- 2775

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958759562  832 vPSRPNRAPPgVPRKGPASPTRPAAPRPSEA 862
Cdd:PHA03247  2776 -AAGPPRRLT-RPAVASLSESRESLPSPWDP 2804
Gag_MA pfam01140
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
 773-848 1.24e-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: 42.75  E-value: 1.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958759562 773 RSPTSSPTPQRRAPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPfgPPPQVPSRPNRAPPGVPRKGP 848
Cdd:pfam01140  64 KTRVFAPGPHGHPDQVPYI------------VTWEALAADPPPWVRPFLTPKP--PPPQPPAAPGLRPPLPPASAP 125
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 768-863 1.82e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 768 VPAGRRSPTSSPTPQR---RAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVP 844
Cdd:PRK07764  387 VAGGAGAPAAAAPSAAaaaPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQP 466

                          90
                  ....*....|....*....
gi 1958759562 845 RKGPASPTRPAAPRPSEAP 863
Cdd:PRK07764  467 APAPAAAPEPTAAPAPAPP 485
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 753-863 2.18e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  753 PMPPPVDD---SWLQVQSVPAGRRSPTSSP--TPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAP-------PVPSRPG 820
Cdd:PHA03307   258 PRPAPITLptrIWEASGWNGPSSRPGPASSssSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSREssssstsSSSESSR 337

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958759562  821 ASPDPFGPPPQVPSRPNRAPPgvPRKGPASPTRPAAPRPSEAP 863
Cdd:PHA03307   338 GAAVSPGPSPSRSPSPSRPPP--PADPSSPRKRPRPSRAPSSP 378
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 520-616 2.26e-04

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270068  Cd Length: 104  Bit Score: 41.10  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 520 VIRKGWLTinnigiMKGGS-----KEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGF-MSSKHIFALFNTEQ 593
Cdd:cd13248     7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                          90       100
                  ....*....|....*....|...
gi 1958759562 594 RNVYkdyrqleLACETQEEVDSW 616
Cdd:cd13248    81 RTYY-------FAADTAEEMEQW 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
 769-864 2.56e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  769 PAGRRSPTSSPTPQRRAPAV-----------------PPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:PHA03247  2769 PAPPAAPAAGPPRRLTRPAVaslsesreslpspwdpaDPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958759562  832 --------VPSRP--NRAPPGVPRKGPASPTRPAAPRPSEAPL 864
Cdd:PHA03247  2849 slplggsvAPGGDvrRRPPSRSPAAKPAAPARPPVRRLARPAV 2891
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 748-861 2.59e-04

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


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 43.99  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 748 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTS-SPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 826
Cdd:NF040712  200 ATVPRLAREPADARPEEVEPAPAAEGAPATdSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958759562 827 GPPPQVPSRPNRAPPGVPRkgPASPTRPAAPRPSE 861
Cdd:NF040712  280 PPAPGAAETPEAAEPPAPA--PAAPAAPAAPEAEE 312
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 752-867 2.73e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGsrgpapgpppagsalGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:PRK07764  708 TPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPD---------------PAGAPAQPPPPPAPAPAAAPAA 772

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759562 832 VPSRPNRAPPGVPRKGPASPTRPAAPRPSEAPLLDL 867
Cdd:PRK07764  773 APPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMEL 808
PHA03247 PHA03247
large tegument protein UL36; Provisional
 757-867 3.10e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  757 PVDDSwlqvqsvPAGRRSPTSSPTPQRRAPAVPPArpgsrgpaPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVpSRP 836
Cdd:PHA03247  2601 PVDDR-------GDPRGPAPPSPLPPDTHAPDPPP--------PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRV-SRP 2664

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958759562  837 NRAPPGVPRKGPASPT---RPAAPRPSEAPLLDL 867
Cdd:PHA03247  2665 RRARRLGRAAQASSPPqrpRRRAARPTVGSLTSL 2698
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 755-862 4.33e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 755 PPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPV-PSRPGASPDPFGPPPQVP 833
Cdd:PRK07764  619 AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAaPPPAPAPAAPAAPAGAAP 698

                          90       100
                  ....*....|....*....|....*....
gi 1958759562 834 SRPNRAPPGVPRKGPASPTRPAAPRPSEA 862
Cdd:PRK07764  699 AQPAPAPAATPPAGQADDPAAQPPQAAQG 727
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 733-863 6.56e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 6.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  733 HALKEALSIIGDINTTTVSTPMPPPVDDSWLqvqsVPAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalGGA 812
Cdd:PHA03307    48 AELAAVTVVAGAAACDRFEPPTGPPPGPGTE----APANESRSTPTWSLSTLAPASPAREGSPT-------------PPG 110

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958759562  813 PPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPRKGPASPTRPAAPRPSEAP 863
Cdd:PHA03307   111 PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAA 161
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 769-863 7.72e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.14  E-value: 7.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 769 PAGRRSPTSSPTPQRRaPAVP-----PARPGSRGPAPgpppagsalggAPPVPSRPGASPDPFGPP----PQVPSRPNra 839
Cdd:PTZ00449  563 PAKEHKPSKIPTLSKK-PEFPkdpkhPKDPEEPKKPK-----------RPRSAQRPTRPKSPKLPElldiPKSPKRPE-- 628

                          90       100
                  ....*....|....*....|....
gi 1958759562 840 PPGVPRKgPASPTRPAAPRPSEAP 863
Cdd:PTZ00449  629 SPKSPKR-PPPPQRPSSPERPEGP 651
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
 516-562 8.12e-04

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


Pssm-ID: 270092  Cd Length: 110  Bit Score: 39.97  E-value: 8.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958759562 516 DEIL--VIRKGWLtinnigiMKGGSK-----EYWFVLTAENLSWYKDDEEKEKK 562
Cdd:cd13273     2 DELIldVIKKGYL-------WKKGHLlptwtERWFVLKPNSLSYYKSEDLKEKK 48
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 701-867 8.76e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.87  E-value: 8.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 701 LLANLYSCGDQNTLMEESAEQAQR---RDEMLRMYHALKEALSIIGDINTTTVST-PMPPPVDDSWLQVQSVPAGRRSPT 776
Cdd:PRK14950  294 MLLNSGADRSLLDLTADEKAALQKvsqIANLEALTKWVKAFSQLDFQLRTTSYGQlPLELAVIEALLVPVPAPQPAKPTA 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 777 SSPTPQR--RAPAVPParPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPRKGPASPTRP 854
Cdd:PRK14950  374 AAPSPVRptPAPSTRP--KAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPPK 451

                         170
                  ....*....|...
gi 1958759562 855 AAPRPSEAPLLDL 867
Cdd:PRK14950  452 EEEKALIADGDVL 464
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 769-863 9.15e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.14  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 769 PAGRRSPTSSPTPQRraPAVPPArpgsrgpapgppPAGSALGGAPPVPSRPGASPDPFGP-PPQVPSRPNRaPPGVprKG 847
Cdd:PTZ00449  591 PEEPKKPKRPRSAQR--PTRPKS------------PKLPELLDIPKSPKRPESPKSPKRPpPPQRPSSPER-PEGP--KI 653

                          90
                  ....*....|....*.
gi 1958759562 848 PASPTRPAAPRPSEAP 863
Cdd:PTZ00449  654 IKSPKPPKSPKPPFDP 669
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 755-864 1.05e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 42.96  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  755 PPPVDDSW------LQVQSVPAGRRSPTSSPTPQRRAPAVPPARpgsrgpapgpppagsalGGAPPVPSRPGASPDPFGP 828
Cdd:PRK12270    22 PNSVDPSWreffadYGPGSTAAPTAAAAAAAAAASAPAAAPAAK-----------------APAAPAPAPPAAAAPAAPP 84

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958759562  829 PPQVPSRPNRAPPGVPRKGPASPTRPAAPRPSEAPL 864
Cdd:PRK12270    85 KPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPL 120
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
750-863 1.05e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 750 VSTPMPPPVDDSWLQVQsvPAGRRSPTSSPTPQRRAPAVPPARPgsrgpaPGPPPAGSALGGAPPVPSRPGASPDPFGPP 829
Cdd:PRK12323  451 APAPAAAPAAAARPAAA--GPRPVAAAAAAAPARAAPAAAPAPA------DDDPPPWEELPPEFASPAPAQPDAAPAGWV 522

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958759562 830 PQVPSRPNRAPPGVPRKGPA-SPTRPAAPRPSEAP 863
Cdd:PRK12323  523 AESIPDPATADPDDAFETLApAPAAAPAPRAAAAT 557
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 752-859 1.21e-03

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: 42.06  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQ 831
Cdd:NF040712  218 EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAP 297

                          90       100
                  ....*....|....*....|....*....
gi 1958759562 832 VPSRPnrAPPGVPR-KGPASPTRPAAPRP 859
Cdd:NF040712  298 APAAP--AAPAAPEaEEPARPEPPPAPKP 324
PHA03247 PHA03247
large tegument protein UL36; Provisional
 753-864 1.23e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  753 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPQrrAPAVPPArpgsrgpapgPPPAGSALGG--AP--PVPSRPGASPDPfgP 828
Cdd:PHA03247  2808 PAAVLAPAAALPPAASPAGPLPPPTSAQPT--APPPPPG----------PPPPSLPLGGsvAPggDVRRRPPSRSPA--A 2873

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958759562  829 PPQVPSRP---NRAPPGVPRKG------PASPTRPAAPRPSEAPL 864
Cdd:PHA03247  2874 KPAAPARPpvrRLARPAVSRSTesfalpPDQPERPPQPQAPPPPQ 2918
DUF4813 pfam16072
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ...
 747-857 1.27e-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: 41.67  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 747 TTTVSTPMPPPVDDSWLQVQSVPAG--RRSPTSSPTPQRRAPAVP--PARPGSRGPAPGPPPAGSALGGAP------PVP 816
Cdd:pfam16072 158 TTVINAGGQQPAAPAAPAYPVAPAAypAQAPAAAPAPAPGAPQTPlaPLNPVAAAPAAAAGAAAAPVVAAAapaaaaPPP 237

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759562 817 SRPGAsPDPFGPPPQ------VPSRpnrappgVPRKGPASPTR----------PAAP 857
Cdd:pfam16072 238 PAPAA-PPADAAPPApggiicVPVR-------VPEPDPKDATKtievekiacyPAPP 286
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
751-863 1.41e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 751 STPMPPPVDDSWLQVQSV---PAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 827
Cdd:PRK07003  421 TRAEAPPAAPAPPATADRgddAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPS 500

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759562 828 PPPQVPSRPNRAPPGVPRkgPASPTRPAAPRPSEAP 863
Cdd:PRK07003  501 AATPAAVPDARAPAAASR--EDAPAAAAPPAPEARP 534
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 775-845 1.59e-03

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: 41.13  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 775 PTSSPTPQrraPAVPPARPGsrgpapgpppagsalGGAPPVP---------SRPGASPDPFG--------PPP----QVP 833
Cdd:pfam15822 163 PYPSPGPY---PAVPPPQSP---------------GAAPPVPwgtvppgpwGPPAPYPDPTGsypmpglyPTPnnpfQVP 224

                          90
                  ....*....|....
gi 1958759562 834 SRPNRAP--PGVPR 845
Cdd:pfam15822 225 SGPSGAPpmPGGPH 238
PHA03247 PHA03247
large tegument protein UL36; Provisional
 750-863 1.63e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  750 VSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPagsalggaPPVPSRPGASPDPfGPP 829
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ--------PPLAPTTDPAGAG-EPS 2956

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958759562  830 PQVPSRPNRAPpgVPRKGPASPTRPAAPRPS-EAP 863
Cdd:PHA03247  2957 GAVPQPWLGAL--VPGRVAVPRFRVPQPAPSrEAP 2989
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 754-865 1.85e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 41.39  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 754 MPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVP-PArpgsrgpapgpppagsalggapPVPSRPGASPdPFGPPPQV 832
Cdd:PHA02682   73 MQRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVTcPA----------------------PAPACPPATA-PTCPPPAV 129

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958759562 833 PSRPNRAPPGVP---RKGPASPTRPAA-PRPSEAPLL 865
Cdd:PHA02682  130 CPAPARPAPACPpstRQCPPAPPLPTPkPAPAAKPIF 166
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
 772-864 1.86e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 41.42  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 772 RRSPTSSPTPQRRAPavPPARPGSRGPAPGPPPagsalggAPPVPSRPGASPDP--FGPPPQVPSRPNRAPPGVPRKGPA 849
Cdd:PHA03201    2 KRARSRSPSPPRRPS--PPRPTPPRSPDASPEE-------TPPSPPGPGAEPPPgrAAGPAAPRRRPRGCPAGVTFSSSA 72

                          90       100
                  ....*....|....*....|
gi 1958759562 850 sPTRPA-----APRPSEAPL 864
Cdd:PHA03201   73 -PPRPPlglddAPAATPPPL 91
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 753-863 1.88e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.02  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 753 PMPPPVDDSWlqvQSVPAGRRSPTSSPTPQRrAPAVPPARPGSRgpapgpPPAGSALGGAPPVPSRPGASPDPFGPPPQV 832
Cdd:pfam15240  65 PGPPPPGGPQ---QPPPQGGKQKPQGPPPQG-GPRPPPGKPQGP------PPQGGNQQQGPPPPGKPQGPPPQGGGPPPQ 134

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958759562 833 PSRPNRAPPGVPRKGPASPTRPAAP-RPSEAP 863
Cdd:pfam15240 135 GGNQQGPPPPPPGNPQGPPQRPPQPgNPQGPP 166
PHA02030 PHA02030
hypothetical protein
 753-857 2.10e-03

hypothetical protein


Pssm-ID: 222843 [Multi-domain]  Cd Length: 336  Bit Score: 41.12  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 753 PMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARpgsrgpapgpppagsalgGAPPVPSRPGASpdpfgPPPQV 832
Cdd:PHA02030  254 IIKPKSKAAGSNLPAVPNVAADAGSAAAPAVPAAAAAVAQ------------------AAPSVPQVPNVA-----VLPDV 310

                          90       100
                  ....*....|....*....|....*
gi 1958759562 833 PSRPNRAPPGVPrKGPASPTRPAAP 857
Cdd:PHA02030  311 PQVAPVAAPAAP-EVPAVPVVPAAP 334
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 753-859 2.18e-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: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 753 PMPPPVDDSWLQVqSVPAGRRSPTSSPTPQRRAPAVPParpgsRGPAPGPPPAGSALGGA---PPVPSRPGASPDPfgPP 829
Cdd:pfam06346   1 PPPPPLPGDSSTI-PLPPGACIPTPPPLPGGGGPPPPP-----PLPGSAAIPPPPPLPGGtsiPPPPPLPGAASIP--PP 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958759562 830 PQVPSRPNRAPP-------GVPRKGPASPTRPAAPRP 859
Cdd:pfam06346  73 PPLPGSTGIPPPpplpggaGIPPPPPPLPGGAGVPPP 109
PHA03247 PHA03247
large tegument protein UL36; Provisional
 748-857 2.72e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  748 TTVSTPMPPPVDDSWlqvQSVPAGRRSPTSSPTPQrrAPAVP--PARPGSRGPapgpppagsalggaPPVPSRPGASPDP 825
Cdd:PHA03247  2715 LVSATPLPPGPAAAR---QASPALPAAPAPPAVPA--GPATPggPARPARPPT--------------TAGPPAPAPPAAP 2775

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958759562  826 FGPPPQVPSRPNRAPPGVPRKGPASPTRPAAP 857
Cdd:PHA03247  2776 AAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 738-863 2.99e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  738 ALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRR-APAVPPARPGSRGPAPGPPPAGSALGGAPPvp 816
Cdd:PHA03307   175 PLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPApAPGRSAADDAGASSSDSSSSESSGCGWGPE-- 252

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958759562  817 srpGASPDPFGPPPQVPSRPNRAPPGVPRKGPASPTRPAAPRPSEAP 863
Cdd:PHA03307   253 ---NECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP 296
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 751-863 3.07e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  751 STPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAV---PPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFG 827
Cdd:PHA03307   805 SGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAarpPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPG 884

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958759562  828 PPPQVPSRPNRAPPGVP-RKGPASPTRPAAPRPSEAP 863
Cdd:PHA03307   885 AAAPPKAAAAAPPAGAPaPRPRPAPRVKLGPMPPGGP 921
PHA03247 PHA03247
large tegument protein UL36; Provisional
 771-860 3.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  771 GRRSPTSSPTPQRRAPA----------VPPaRPGSRGPAPGPPPAGSALGGAPPV-PSRPGASPDPFGPPPQ-------- 831
Cdd:PHA03247  2502 GPPDPDAPPAPSRLAPAilpdepvgepVHP-RMLTWIRGLEELASDDAGDPPPPLpPAAPPAAPDRSVPPPRpaprpsep 2580

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958759562  832 ----------VPSRPNRapPGVPRKGPASPTRPAAPRPS 860
Cdd:PHA03247  2581 avtsrarrpdAPPQSAR--PRAPVDDRGDPRGPAPPSPL 2617
PHA03378 PHA03378
EBNA-3B; Provisional
 755-863 3.10e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.21  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 755 PPPVDDSWLQVQSVPAgRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAgsalggAPPVPS-RPGASPDPFGPPPQVP 833
Cdd:PHA03378  659 ITPYKPTWTQIGHIPY-QPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPA------APPGRAqRPAAATGRARPPAAAP 731

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958759562 834 S--RPNRAPPGVPRKGPASPTRpaAPRPSEAP 863
Cdd:PHA03378  732 GraRPPAAAPGRARPPAAAPGR--ARPPAAAP 761
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 753-862 3.20e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  753 PMPPPVDDSWLQVQSVPA-GRRSPTSSPTP--QRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPgaSPDPFGPP 829
Cdd:PHA03307   126 PPPSPAPDLSEMLRPVGSpGPPPAASPPAAgaSPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPP--STPPAAAS 203

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958759562  830 PQVPSRPNRAPPGVPRKGPASPTRPAAPRPSEA 862
Cdd:PHA03307   204 PRPPRRSSPISASASSPAPAPGRSAADDAGASS 236
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 779-866 3.49e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 40.76  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 779 PTPQRRAPAvPPARPGSRGPAPgpppagsalgGAPPVPSRPGASPDPFGPPPQvPSRPNRAPPGVPRKGPASPTrPAAPR 858
Cdd:PHA03264  268 PAPSGGSPA-PPGDDRPEAKPE----------PGPVEDGAPGRETGGEGEGPE-PAGRDGAAGGEPKPGPPRPA-PDADR 334


                  ....*...
gi 1958759562 859 PSEAPLLD 866
Cdd:PHA03264  335 PEGWPSLE 342
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 813-859 3.55e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 39.25  E-value: 3.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958759562 813 PPVPSRPGASPDPFGPPPqvPSRPNRAPPGVPRKGPASPTRPAAPRP 859
Cdd:pfam15240  52 GGFPPQPPASDDPPGPPP--PGGPQQPPPQGGKQKPQGPPPQGGPRP 96
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 770-863 3.61e-03

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


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 38.13  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 770 AGRRSPTSSPTPqrRAPAVPPARPGSRGPAPGPPPAgsalggAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPRKgPA 849
Cdd:pfam12526  23 SGFSSCFSPPES--AHPDPPPPVGDPRPPVVDTPPP------VSAVWVLPPPSEPAAPEPDLVPPVTGPAGPPSPLA-PP 93

                          90
                  ....*....|....
gi 1958759562 850 SPTRPaAPRPSEAP 863
Cdd:pfam12526  94 APAQK-PPLPPPRP 106
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
752-863 3.66e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 752 TPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQrRAPAVPPArpgsrgpaPGPPPAGSALGGAPPVPSRPGA--SPDPFGPP 829
Cdd:PRK12323  427 SPAPEALAAARQASARGPGGAPAPAPAPAAA-PAAAARPA--------AAGPRPVAAAAAAAPARAAPAAapAPADDDPP 497

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958759562 830 P--QVPSRPNRAPPGVPRKGPASPTRPAAPRPSEAP 863
Cdd:PRK12323  498 PweELPPEFASPAPAQPDAAPAGWVAESIPDPATAD 533
PHA03247 PHA03247
large tegument protein UL36; Provisional
 810-863 4.05e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 4.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958759562  810 GGAPPVPSRpGASPDPFGPPPQVPSRPNRAPPGV---PRKGpASPTRPAAP-RPSEAP 863
Cdd:PHA03247   265 ADRAPETAR-GATGPPPPPEAAAPNGAAAPPDGVwgaALAG-APLALPAPPdPPPPAP 320
Aim21 pfam11489
Altered inheritance of mitochondria protein 21; This is a family of proteins conserved in ...
 748-866 4.24e-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: 40.73  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 748 TTVSTP----MPPPVDDSWLQVQSVPAGRRSPtsSPTPQRRAPAVP-------PARPGSRGPAPGPPPAGSAlggaPPVP 816
Cdd:pfam11489 502 TTVETPdevkSTSPGVPTKPAIPARPKSGKPT--SPTEKRKPPPVPkkpkpqiPARPAKAQPQQAGEEFKPK----PRVP 575

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958759562 817 SRPGASP-------------DPFGPPPQVPSRPNRAPPGVprKGPASPTRPAAPRPSEAPLLD 866
Cdd:pfam11489 576 ARPGGSKisalragfasdlnGRLQLGPQAPKKVVEEDKEP--SEEKGDKEEEEDTKEKAPLSD 636
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 541-616 4.41e-03

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269964  Cd Length: 121  Bit Score: 38.03  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 541 YWFVLTAENLS-W-YKDDEEKeKKYMLSVD-----NLKLRDVEKGFMSSKHIFAL-FNTEQRNVYKDYRQLE----LACE 608
Cdd:cd01263    23 RWCVLRGGYLSfWkYPDDEEK-KKPIGSIDltkciTEKVEPAPRELCARPNTFLLeTLRPAEDDDRDDTNEKirvlLSAD 101


                  ....*...
gi 1958759562 609 TQEEVDSW 616
Cdd:cd01263   102 TKEERIEW 109
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 752-863 4.63e-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: 40.91  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 752 TPMPPPVddswlqvqsvPAGRRSPTSSPTPQRRAPaVPParpgsrgpapgpppAGSALGGAPPVPSRPGAsPDPFGPPP- 830
Cdd:pfam03154 250 QPMTQPP----------PPSQVSPQPLPQPSLHGQ-MPP--------------MPHSLQTGPSHMQHPVP-PQPFPLTPq 303

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958759562 831 ----QVPSRPNRAPPGVPRKGPASPTRPAAPRPSEAP 863
Cdd:pfam03154 304 ssqsQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPP 340
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 762-863 5.05e-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: 40.37  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 762 WLQVQSvpAGRRSPTSSPTPQRRAPAVPPARPGSRgpapgpppagsalgGAPPVPSRPGASPDPFGPPPQVPSRPNRAPP 841
Cdd:NF041121   10 WLAAQM--GRAAAPPSPEGPAPTAASQPATPPPPA--------------APPSPPGDPPEPPAPEPAPLPAPYPGSLAPP 73

                          90       100
                  ....*....|....*....|..
gi 1958759562 842 GVPRKGPAsPTRPAAPRPSEAP 863
Cdd:NF041121   74 PPPPPGPA-GAAPGAALPVRVP 94
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 755-863 5.10e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 5.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562  755 PPPVDDSWLQVQSVP------AGRRSPTSSP--TPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPF 826
Cdd:PHA03307    87 TPTWSLSTLAPASPAregsptPPGPSSPDPPppTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDA 166

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958759562  827 GPPPQ------VPSRPNRAPPGVPRKGPASPTRPAAPRPSEAP 863
Cdd:PHA03307   167 ASSRQaalplsSPEETARAPSSPPAEPPPSTPPAAASPRPPRR 209
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 715-866 5.66e-03

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 39.91  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 715 MEESAEQAQRRdemlrmyHALKEALSIIGDINTTTVSTPMPppvddSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPArpg 794
Cdd:pfam07174   1 MDQVDPNSTRR-------KGLWATLAIAAVAGASAVAVALP-----AVAHADPEPAPPPPSTATAPPAPPPPPPAPA--- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958759562 795 srGPAPGPPPAGSALGGAPPVPSRPGASP----DPFGPPPQvPSRPNRAPPG-VPRK-GPASPTRPAAPRPSEAPLLD 866
Cdd:pfam07174  66 --APAPPPPPAAPNAPNAPPPPADPNAPPpppaDPNAPPPP-AVDPNAPEPGrIDNAvGGFSYVVPAGWVESDATHLD 140
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 769-863 5.86e-03

N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 39.03  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 769 PAGRRSPT--SSPTPQRRAPAVP-PARPGsrgpapgpppagsalgGAPPVPSRPGASPDPFGPppqvpsrpNRAPPGVPR 845
Cdd:cd21576   116 PARGSSPTlgSEPAPASGEDAVSgPESSF----------------GAPAIPSAPAAPGAPAVS--------GEVPGGAPG 171

                          90
                  ....*....|....*...
gi 1958759562 846 KGPASPTRPAAPRPSEAP 863
Cdd:cd21576   172 AGPAPAAGPAPRRRPVTP 189
PHA03378 PHA03378
EBNA-3B; Provisional
 772-863 5.92e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 772 RRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPS---RPGASPDPFGPPPQVPS--RPNRAPPGvPRK 846
Cdd:PHA03378  637 RMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANtmlPIQWAPGTMQPPPRAPTpmRPPAAPPG-RAQ 715

                          90
                  ....*....|....*..
gi 1958759562 847 GPASPTRPAAPrPSEAP 863
Cdd:PHA03378  716 RPAAATGRARP-PAAAP 731
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 766-863 5.92e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 39.44  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 766 QSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgpppagsalggAPPVPSRPGASPDPFGPPPQVPSRPNRAPPgvPR 845
Cdd:PLN02983  143 QPPPPAPVVMMQPPPPHAMPPASPPA--------------------AQPAPSAPASSPPPTPASPPPAKAPKSSHP--PL 200

                          90
                  ....*....|....*...
gi 1958759562 846 KGPASPTRPAAPRPSEAP 863
Cdd:PLN02983  201 KSPMAGTFYRSPAPGEPP 218
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
 782-863 6.06e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 40.11  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 782 QRRAPAVPPARPGSRGPapgpppagsalggAPPVPSRPGASPDPFGPPP--QVPSRPNRAPPGVPRKGPASPTRPAAPRP 859
Cdd:PRK14965  378 ERGAPAPPSAAWGAPTP-------------AAPAAPPPAAAPPVPPAAParPAAARPAPAPAPPAAAAPPARSADPAAAA 444


                  ....
gi 1958759562 860 SEAP 863
Cdd:PRK14965  445 SAGD 448
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 768-860 6.38e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 39.94  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 768 VPAGRRSPTSSPTPQRRAPavPPARPGSrgpapgpppagsalggaPPVPSRPGASPDPFGP----PPQVPSRPNRAPPGV 843
Cdd:PHA03291  204 VPATPRPTPRTTASPETTP--TPSTTTS-----------------PPSTTIPAPSTTIAAPqagtTPEAEGTPAPPTPGG 264

                          90
                  ....*....|....*..
gi 1958759562 844 PRKGPASPTRpaAPRPS 860
Cdd:PHA03291  265 GEAPPANATP--APEAS 279
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 748-864 8.61e-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: 39.75  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759562 748 TTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPArpgsrgpapgpPPAGSALGGAPPVPSRPGASPDPF- 826
Cdd:pfam03154 400 SSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPP-----------AASHPPTSGLHQVPSQSPFPQHPFv 468

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958759562 827 --GPPPQVPsrPNRAPPGVPRKGPASPTRPAAPRPSEAPL 864
Cdd:pfam03154 469 pgGPPPITP--PSGPPTSTSSAMPGIQPPSSASVSSSGPV 506
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 812-864 8.63e-03

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


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 38.13  E-value: 8.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958759562 812 APPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPRKGPASPTRPAAPRPSEAPL 864
Cdd:cd21975   103 APASGAAASTSPESSSDAASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGV 155
DUF6264 pfam19779
Family of unknown function (DUF6264); This family of putative integral membrane proteins is ...
 782-859 8.77e-03

Family of unknown function (DUF6264); This family of putative integral membrane proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 179 and 218 amino acids in length.


Pssm-ID: 466182  Cd Length: 182  Bit Score: 38.01  E-value: 8.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958759562 782 QRRAPAVPPARPgsrgpapgpppagsalggAPPVPSRPGASPDPfgpPPQVPSRPNRAPPGVPRKGPASPTRPAAPRP 859
Cdd:pfam19779  13 QRAPIGDPAAAA------------------AAAPPAAPAPAAPA---PPAAPAAPPAAPPPPGAPAPGAPAAARRARR 69
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH