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Conserved domains on  [gi|1907066845|ref|XP_036021507|]
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dynamin-3 isoform X7 [Mus musculus]

Protein Classification

dynamin( domain architecture ID 12185953)

dynamin is a GTPase that regulates endocytic vesicle formation; similar to human dynamin-1, a microtubule-associated force-producing protein involved in producing microtubule bundles

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 1.04e-161

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


:

Pssm-ID: 197491  Cd Length: 240  Bit Score: 470.13  E-value: 1.04e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845   86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  166 RENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGK 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 7.75e-139

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


:

Pssm-ID: 460033  Cd Length: 287  Bit Score: 413.07  E-value: 7.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 295 NFRNKLQGQLLSIEHEVEAFKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVMQELINTVKKCTKRLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907066845 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 514-625 1.72e-81

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: 256.86  E-value: 1.72e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 514 NQVIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQRNVY 593
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907066845 594 KDYRFLELACDSQEDVDSWKASLLRAGVYPDK 625
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
645-735 1.71e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.47  E-value: 1.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 645 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 724
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1907066845 725 LKEALAIIGDI 735
Cdd:pfam02212  81 LKQAREILSEV 91
MISS super family cl25801
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 743-833 1.69e-08

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.


The actual alignment was detected with superfamily member pfam15822:

Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 56.15  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 743 PAPPPVDDSWlqHSRRSPPPSPTTQ-RRLTISAPLPRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPNSS 815
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205

                          90       100
                  ....*....|....*....|....*..
gi 1907066845 816 DSFGAP---P------QVPSRPTRAPP 833
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPSGAPP 232
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 1.04e-161

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 470.13  E-value: 1.04e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845   86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  166 RENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGK 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 29-294 2.76e-148

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: 437.06  E-value: 2.76e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRHE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907066845 258 FFLSHPAYRH-IADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:cd08771   241 FFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 7.75e-139

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


Pssm-ID: 460033  Cd Length: 287  Bit Score: 413.07  E-value: 7.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 295 NFRNKLQGQLLSIEHEVEAFKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVMQELINTVKKCTKRLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907066845 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 514-625 1.72e-81

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: 256.86  E-value: 1.72e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 514 NQVIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQRNVY 593
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907066845 594 KDYRFLELACDSQEDVDSWKASLLRAGVYPDK 625
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 3.25e-70

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 228.65  E-value: 3.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRHEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirDMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 1907066845 186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
645-735 1.71e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.47  E-value: 1.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 645 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 724
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1907066845 725 LKEALAIIGDI 735
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
644-735 3.19e-29

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 111.56  E-value: 3.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  644 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 723
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1907066845  724 ALKEALAIIGDI 735
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 516-619 6.53e-13

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: 65.65  E-value: 6.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  516 VIRKGWLTVSNIGiMKGGSKGYWFVLTAESLSWYKDDEEKEK---KYMLPLDNLKVRDVEKGFMSS-KHVFALFNTEQRN 591
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEIKTSDRKT 79

                           90       100
                   ....*....|....*....|....*...
gi 1907066845  592 VYkdyrfleLACDSQEDVDSWKASLLRA 619
Cdd:smart00233  80 LL-------LQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 516-619 2.58e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 63.74  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 516 VIRKGWLTVSNIGImKGGSKGYWFVLTAESLSWYKDD---EEKEKKYMLPLDNLKVRDVEKGFMSS-KHVFALFNTEQRN 591
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1907066845 592 VykdyRFLELACDSQEDVDSWKASLLRA 619
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 743-833 1.69e-08

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: 56.15  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 743 PAPPPVDDSWlqHSRRSPPPSPTTQ-RRLTISAPLPRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPNSS 815
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205

                          90       100
                  ....*....|....*....|....*..
gi 1907066845 816 DSFGAP---P------QVPSRPTRAPP 833
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPSGAPP 232
PHA03247 PHA03247
large tegument protein UL36; Provisional
 738-841 3.08e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 3.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  738 ATVSTPAPPPVddswlqhsRR--SPPPSPTTQrrltiSAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSS 815
Cdd:PHA03247  2873 AKPAAPARPPV--------RRlaRPAVSRSTE-----SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939

                           90       100
                   ....*....|....*....|....*....
gi 1907066845  816 DSFGAP---PQVPSRPTRAPPSvPRFGAV 841
Cdd:PHA03247  2940 QPPLAPttdPAGAGEPSGAVPQ-PWLGAL 2967
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 743-834 1.06e-06

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 51.83  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 743 PAPPPVDDSWLQHSRRSPPPSPTTqrrltisaPLPRPtsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSfgAPP 822
Cdd:NF040983   97 PPPPPPPPTPPPPPPPPPPPPPPS--------PPPPP-----PPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPI--QPT 161

                          90
                  ....*....|..
gi 1907066845 823 QVPSRPTRAPPS 834
Cdd:NF040983  162 QLPSIPNATPTS 173
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 737-836 1.47e-05

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: 46.22  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 737 TATVSTPAPPPVDDSwlqhsrrSPPPSPTTQRR----LTISAPLPRPtSGRG---------------PAPAIPSPGPHS- 796
Cdd:cd21975    43 AKGPGPPGPAWKPDG-------ADSPGLVTAAPhllaANVLAPLRGP-SVEGsslesgdadmgsdsdVAPASGAAASTSp 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907066845 797 ---GAPPVPFRPGPLPPFPNSSDSFGAPPQVPSRPTRAPPSVP 836
Cdd:cd21975   115 essSDAASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTP 157
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 752-837 4.05e-05

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: 46.92  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 752 WL-QHSRRSPPPS------PTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSFGAPPQV 824
Cdd:NF041121   10 WLaAQMGRAAAPPspegpaPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAAL 89

                          90
                  ....*....|...
gi 1907066845 825 PSRpTRAPPSVPR 837
Cdd:NF041121   90 PVR-VPAPPALPN 101
HpaP TIGR02557
type III secretion protein HpaP; This family of genes is always found in type III secretion ...
 761-842 1.17e-03

type III secretion protein HpaP; This family of genes is always found in type III secretion operons, althought its function in the processes of secretion and virulence is unclear. Hpa stands for Hrp-associated gene, where Hrp stands for hypersensitivity response and virulence.


Pssm-ID: 274200  Cd Length: 201  Bit Score: 41.03  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 761 PPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPvpfRPGPLPPFPnsSDSFGA-----PPQVPSRPTRAPPSv 835
Cdd:TIGR02557  14 DPARPARRRTPLAQLRRRDALAYAPPPRPEPPPPCDEDRP---EPRADTRAS--DPPPEAptdadPAQPPDDPDASAHT- 87


                  ....*..
gi 1907066845 836 pRFGAVK 842
Cdd:TIGR02557  88 -AAIASG 93
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 737-837 1.55e-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: 41.68  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 737 TATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPrptsgrGPAPAIPSPGPhsGAPPVPFRPGPLPPFPNSSD 816
Cdd:NF040712  228 ATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAA------EPDEATRDAGE--PPAPGAAETPEAAEPPAPAP 299

                          90       100
                  ....*....|....*....|....*.
gi 1907066845 817 SFGAPPQVPS-----RPTRAPPSVPR 837
Cdd:NF040712  300 AAPAAPAAPEaeepaRPEPPPAPKPK 325
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 1.04e-161

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


Pssm-ID: 197491  Cd Length: 240  Bit Score: 470.13  E-value: 1.04e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845   86 CKGKKFTDFDEVRHEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  166 RENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGK 245
Cdd:smart00053 161 REECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 29-294 2.76e-148

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: 437.06  E-value: 2.76e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRHE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIRDMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907066845 258 FFLSHPAYRH-IADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:cd08771   241 FFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 215-502 7.75e-139

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


Pssm-ID: 460033  Cd Length: 287  Bit Score: 413.07  E-value: 7.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 295 NFRNKLQGQLLSIEHEVEAFKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVMQELINTVKKCTKRLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907066845 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 514-625 1.72e-81

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: 256.86  E-value: 1.72e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 514 NQVIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQRNVY 593
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907066845 594 KDYRFLELACDSQEDVDSWKASLLRAGVYPDK 625
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 3.25e-70

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 228.65  E-value: 3.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRHEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirDMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 1907066845 186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
645-735 1.71e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.47  E-value: 1.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 645 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 724
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1907066845 725 LKEALAIIGDI 735
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
644-735 3.19e-29

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 111.56  E-value: 3.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  644 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 723
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1907066845  724 ALKEALAIIGDI 735
Cdd:smart00302  81 LLKKARQIIAAV 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 516-619 6.53e-13

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: 65.65  E-value: 6.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  516 VIRKGWLTVSNIGiMKGGSKGYWFVLTAESLSWYKDDEEKEK---KYMLPLDNLKVRDVEKGFMSS-KHVFALFNTEQRN 591
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKKDKKSykpKGSIDLSGCTVREAPDPDSSKkPHCFEIKTSDRKT 79

                           90       100
                   ....*....|....*....|....*...
gi 1907066845  592 VYkdyrfleLACDSQEDVDSWKASLLRA 619
Cdd:smart00233  80 LL-------LQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 516-619 2.58e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 63.74  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 516 VIRKGWLTVSNIGImKGGSKGYWFVLTAESLSWYKDD---EEKEKKYMLPLDNLKVRDVEKGFMSS-KHVFALFNTEQRN 591
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1907066845 592 VykdyRFLELACDSQEDVDSWKASLLRA 619
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 518-616 2.77e-11

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


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 60.63  E-value: 2.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 518 RKGWLTVSNIGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKY--MLPLDN-LKVRDVEKGfmSSKHVFALFNTEQRNVYk 594
Cdd:cd00821     1 KEGYLLKRGGGGLKSWKK-RWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                          90       100
                  ....*....|....*....|..
gi 1907066845 595 dyrfleLACDSQEDVDSWKASL 616
Cdd:cd00821    77 ------LQADSEEERQEWLKAL 92
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 516-619 3.31e-09

General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 and the related proteins ARNO (ARF nucleotide-binding site opener)/cytohesin-2 and cytohesin-1 are ARF exchange factors that contain a pleckstrin homology (PH) domain thought to target these proteins to cell membranes through binding polyphosphoinositides. The PH domains of all three proteins exhibit relatively high affinity for PtdIns(3,4,5)P3. Within the Grp1 family, diglycine (2G) and triglycine (3G) splice variants, differing only in the number of glycine residues in the PH domain, strongly influence the affinity and specificity for phosphoinositides. The 2G variants selectively bind PtdIns(3,4,5)P3 with high affinity,the 3G variants bind PtdIns(3,4,5)P3 with about 30-fold lower affinity and require the polybasic region for plasma membrane targeting. These ARF-GEFs share a common, tripartite structure consisting of an N-terminal coiled-coil domain, a central domain with homology to the yeast protein Sec7, a PH domain, and a C-terminal polybasic region. The Sec7 domain is autoinhibited by conserved elements proximal to the PH domain. GRP1 binds to the DNA binding domain of certain nuclear receptors (TRalpha, TRbeta, AR, ER, but not RXR), and can repress thyroid hormone receptor (TR)-mediated transactivation by decreasing TR-complex formation on thyroid hormone response elements. ARNO promotes sequential activation of Arf6, Cdc42 and Rac1 and insulin secretion. Cytohesin acts as a PI 3-kinase effector mediating biological responses including cell spreading and adhesion, chemotaxis, protein trafficking, and cytoskeletal rearrangements, only some of which appear to depend on their ability to activate ARFs. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269954  Cd Length: 119  Bit Score: 55.40  E-value: 3.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 516 VIRKGWLTvsnigiMKGGS----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKgfMSSKHVFALFNTEQRN 591
Cdd:cd01252     3 PDREGWLL------KLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907066845 592 VYKD----------------YRfleLACDSQEDVDSWKASLLRA 619
Cdd:cd01252    75 VIKAcktdsdgkvvegnhtvYR---ISAASEEERDEWIKSIKAS 115
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 743-833 1.69e-08

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: 56.15  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 743 PAPPPVDDSWlqHSRRSPPPSPTTQ-RRLTISAPLPRPtsgrGPAPAIPSPGPHSGAPPVPFRP------GPLPPFPNSS 815
Cdd:pfam15822 132 PAAAAPSGPW--GSMSSGPWAPGMGgQYPAPNMPYPSP----GPYPAVPPPQSPGAAPPVPWGTvppgpwGPPAPYPDPT 205

                          90       100
                  ....*....|....*....|....*..
gi 1907066845 816 DSFGAP---P------QVPSRPTRAPP 833
Cdd:pfam15822 206 GSYPMPglyPtpnnpfQVPSGPSGAPP 232
PHA03247 PHA03247
large tegument protein UL36; Provisional
 738-841 3.08e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 3.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  738 ATVSTPAPPPVddswlqhsRR--SPPPSPTTQrrltiSAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSS 815
Cdd:PHA03247  2873 AKPAAPARPPV--------RRlaRPAVSRSTE-----SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939

                           90       100
                   ....*....|....*....|....*....
gi 1907066845  816 DSFGAP---PQVPSRPTRAPPSvPRFGAV 841
Cdd:PHA03247  2940 QPPLAPttdPAGAGEPSGAVPQ-PWLGAL 2967
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 738-837 7.53e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 56.33  E-value: 7.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  738 ATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRP------TSGRGPAPAIPSPGPHSGAPpvpfrPGPLPPF 811
Cdd:PHA03307   119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAavasdaASSRQAALPLSSPEETARAP-----SSPPAEP 193

                           90       100
                   ....*....|....*....|....*...
gi 1907066845  812 PNSSDSFGAP--PQVPSRPTRAPPSVPR 837
Cdd:PHA03307   194 PPSTPPAAASprPPRRSSPISASASSPA 221
PHA03247 PHA03247
large tegument protein UL36; Provisional
 744-837 1.02e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  744 APPPVDDSWLQHSRRSP-PPSPTTQRRLTISAPLPRPTSGRGP--------APAIPSPGPHSGAPPVPFRPGPlPPFPNS 814
Cdd:PHA03247  2559 APPAAPDRSVPPPRPAPrPSEPAVTSRARRPDAPPQSARPRAPvddrgdprGPAPPSPLPPDTHAPDPPPPSP-SPAANE 2637

                           90       100
                   ....*....|....*....|...
gi 1907066845  815 SDSFGAPPQVPSRPTRAPPSVPR 837
Cdd:PHA03247  2638 PDPHPPPTVPPPERPRDDPAPGR 2660
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 705-841 2.07e-07

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: 53.39  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 705 MEESAEQAQRRDemlRMYQALkeALAIIGDINTATVSTPA-----PPPVddswlqhsrrSPPPSPTTqrrltiSAPLPRP 779
Cdd:pfam07174   1 MDQVDPNSTRRK---GLWATL--AIAAVAGASAVAVALPAvahadPEPA----------PPPPSTAT------APPAPPP 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907066845 780 TSgrgPAPAIPSPGPHSGAPPVPfRPGPLPPFPNSSDSFGAPPQVPSRPTRAPPSvPRFGAV 841
Cdd:pfam07174  60 PP---PAPAAPAPPPPPAAPNAP-NAPPPPADPNAPPPPPADPNAPPPPAVDPNA-PEPGRI 116
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
 503-619 2.99e-07

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: 49.55  E-value: 2.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 503 SSQVHKKSTIgnqviRKGWltvsnigimkggsKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNL----KVRDVEKgfmss 578
Cdd:cd13298     9 SGYLLKRSRK-----TKNW-------------KKRWVVLRPCQLSYYKDEKEYKLRRVINLSELlavaPLKDKKR----- 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907066845 579 KHVFALFNTEqrnvyKDYRFlelACDSQEDVDSWkASLLRA 619
Cdd:cd13298    66 KNVFGIYTPS-----KNLHF---RATSEKDANEW-VEALRE 97
PHA03247 PHA03247
large tegument protein UL36; Provisional
 744-836 6.58e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 6.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  744 APPPVDDswLQHSRRSPPPSPTtqrrltiSAPLPRPTSGRGPAPAIPSPGPHSgAPPVPFRPGPlPPFPNSSDSFGAPPQ 823
Cdd:PHA03247  2688 ARPTVGS--LTSLADPPPPPPT-------PEPAPHALVSATPLPPGPAAARQA-SPALPAAPAP-PAVPAGPATPGGPAR 2756

                           90
                   ....*....|...
gi 1907066845  824 VPSRPTRAPPSVP 836
Cdd:PHA03247  2757 PARPPTTAGPPAP 2769
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 743-834 1.06e-06

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 51.83  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 743 PAPPPVDDSWLQHSRRSPPPSPTTqrrltisaPLPRPtsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSfgAPP 822
Cdd:NF040983   97 PPPPPPPPTPPPPPPPPPPPPPPS--------PPPPP-----PPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPI--QPT 161

                          90
                  ....*....|..
gi 1907066845 823 QVPSRPTRAPPS 834
Cdd:NF040983  162 QLPSIPNATPTS 173
PHA03247 PHA03247
large tegument protein UL36; Provisional
 738-836 1.10e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  738 ATVSTPAPPPVDDSWLQHSRRSPPPSPTTqrrlTISAPLPRPTSGR--GPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSS 815
Cdd:PHA03247  2734 ALPAAPAPPAVPAGPATPGGPARPARPPT----TAGPPAPAPPAAPaaGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809

                           90       100
                   ....*....|....*....|.
gi 1907066845  816 DSFGAPPQVPSRPTRAPPSVP 836
Cdd:PHA03247  2810 AVLAPAAALPPAASPAGPLPP 2830
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 516-619 1.36e-06

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


Pssm-ID: 270068  Cd Length: 104  Bit Score: 47.65  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 516 VIRKGWLTvsnigimKGGSKGY------WFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGF-MSSKHVFALFNTE 588
Cdd:cd13248     7 VVMSGWLH-------KQGGSGLknwrkrWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHAN 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907066845 589 QRNVYkdyrfleLACDSQEDVDSWKASLLRA 619
Cdd:cd13248    80 MRTYY-------FAADTAEEMEQWMNAMSLA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 740-837 1.78e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  740 VSTPAPPPVDDSWLQ-----HSRRSPPPSPTTQRRLTISAPL----PRPTSGRGPAPAIPSPGPHSGAPPVPFRPGP--- 807
Cdd:PHA03247  2886 LARPAVSRSTESFALppdqpERPPQPQAPPPPQPQPQPPPPPqpqpPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPwlg 2965

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907066845  808 -LPPFPNSSDSFGAPPQVPSRPTRAPPSVPR 837
Cdd:PHA03247  2966 aLVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 735-848 2.17e-06

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 51.50  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 735 INTATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAI-------PSPGPHSGAP-------P 800
Cdd:PHA03321  404 LATELFRTGVPSEHYEASLRLLSSRQPPGAPAPRRDNDPPPPPRARPGSTPACARraraqraRDAGPEYVDPlgalrrlP 483

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907066845 801 VPFRPGPLPPFPNSSDSF-----GAPPQVPSR----PTRAPPSVPRFGAVKEEAVEP 848
Cdd:PHA03321  484 AGAAPPPEPAAAPSPATYytrmgGGPPRLPPRnratETLRPDWGPPAAAPPEQMEDP 540
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 738-836 2.42e-06

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 50.24  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 738 ATVSTPAPP--------PVDDSWLQHSRR---SPPPSPTT-QRRLTISAPL-PRPTSGrGPAPAIPSPGPHSGAPPVPFr 804
Cdd:PHA02682   32 ATIPAPAAPcppdadvdPLDKYSVKEAGRyyqSRLKANSAcMQRPSGQSPLaPSPACA-APAPACPACAPAAPAPAVTC- 109

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907066845 805 PGPLPPFPNSSDSFGAPPQVPSRPTRAPPSVP 836
Cdd:PHA02682  110 PAPAPACPPATAPTCPPPAVCPAPARPAPACP 141
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 735-845 2.42e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.33  E-value: 2.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  735 INTATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRL------TISAPLPRPTSGRGPAPAIPSPGP---------HSGAP 799
Cdd:PHA03307   195 PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADdagassSDSSSSESSGCGWGPENECPLPRPapitlptriWEASG 274

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907066845  800 PVPFRPGPLPPFPNSSDSFGAPPQVPSRPtRAPPSVPRFGAVKEEA 845
Cdd:PHA03307   275 WNGPSSRPGPASSSSSPRERSPSPSPSSP-GSGPAPSSPRASSSSS 319
PHA03247 PHA03247
large tegument protein UL36; Provisional
 742-848 3.04e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 3.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  742 TPaPPPVDD--SWLQHSRRSPPPSPTTQRRLTISAPLPRPTSG-RGPAPAIPSPGPhsgaPPVPFRPGPLPPFPNSSDSF 818
Cdd:PHA03247   360 TP-PSSLEDlsAGRHHPKRASLPTRKRRSARHAATPFARGPGGdDQTRPAAPVPAS----VPTPAPTPVPASAPPPPATP 434

                           90       100       110
                   ....*....|....*....|....*....|
gi 1907066845  819 GAPPQVPSRPTRAPPSVPRFGAVKEEAVEP 848
Cdd:PHA03247   435 LPSAEPGSDDGPAPPPERQPPAPATEPAPD 464
PHA03247 PHA03247
large tegument protein UL36; Provisional
 737-836 3.33e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  737 TATVSTPAPPPVDDSWLQhsRRSPPPSPTTQRRLTISAPLPR-----PTSGRGPAPAIP-SPGPHSGAPP----VPFRPG 806
Cdd:PHA03247  2763 TAGPPAPAPPAAPAAGPP--RRLTRPAVASLSESRESLPSPWdpadpPAAVLAPAAALPpAASPAGPLPPptsaQPTAPP 2840

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907066845  807 PLPPFPNSSDSFG---APPQVPSR--PTRAPPSVP 836
Cdd:PHA03247  2841 PPPGPPPPSLPLGgsvAPGGDVRRrpPSRSPAAKP 2875
DUF4813 pfam16072
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ...
 735-847 3.71e-06

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: 49.76  E-value: 3.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 735 INT--ATVSTPAPP--PVDDSWLQHSRRSPPPSP------TTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPvpfr 804
Cdd:pfam16072 161 INAggQQPAAPAAPayPVAPAAYPAQAPAAAPAPapgapqTPLAPLNPVAAAPAAAAGAAAAPVVAAAAPAAAAPP---- 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907066845 805 pgplPPFPNSSDSFGAPPQ---VPSRPTRAPPSVPRfGAVKEEAVE 847
Cdd:pfam16072 237 ----PPAPAAPPADAAPPApggIICVPVRVPEPDPK-DATKTIEVE 277
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 716-836 3.98e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 50.58  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 716 DEMLRM--YQALKEALAII-GDINTATVSTPAPPpvddswlqhsrRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSP 792
Cdd:PRK14950  338 DFQLRTtsYGQLPLELAVIeALLVPVPAPQPAKP-----------TAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRET 406

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907066845 793 GPHSGAPPVPFRPGPLPPFPNSSDSFGAPPQVPSRPTRAPPSVP 836
Cdd:PRK14950  407 ATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPP 450
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 742-837 6.15e-06

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 49.62  E-value: 6.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 742 TPAPPPVDDSwlqhsRRSPPPSPTTqrrltiSAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPF--PNSSDSFG 819
Cdd:PHA03264  274 SPAPPGDDRP-----EAKPEPGPVE------DGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDAdrPEGWPSLE 342

                          90
                  ....*....|....*...
gi 1907066845 820 APPQVPsrPTRAPPSVPR 837
Cdd:PHA03264  343 AITFPP--PTPATPAVPR 358
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 736-837 8.02e-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: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 736 NTATVSTPAPPPVDDSWLQHSRRSPPPSPttqrrltiSAPLPR------PTSGRGPAPAIPSPGphsgaPPVPFrPGPLP 809
Cdd:pfam15822  52 STAPSTVPFGPAPTGMYPSIPLTGPSPGP--------PAPFPPsgpscpPPGGPYPAPTVPGPG-----PIGPY-PTPNM 117

                          90       100
                  ....*....|....*....|....*...
gi 1907066845 810 PFPNSSDSFGAppqvPSRPTRAPPSVPR 837
Cdd:pfam15822 118 PFPELPRPYGA----PTDPAAAAPSGPW 141
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 697-833 9.82e-06

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: 49.38  E-value: 9.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 697 SSEDQNTLMEESAEQAQRRDEMLRMyQALKEAL--AIIGDINTATVSTPAPPPVDDSwlQHSRRSPPPSPTTQRRLTISA 774
Cdd:pfam03154 150 SPQDNESDSDSSAQQQILQTQPPVL-QAQSGAAspPSPPPPGTTQAATAGPTPSAPS--VPPQGSPATSQPPNQTQSTAA 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 775 P--------------LPRPTSGRGPAP-----------AIPSPGPHSGAPPVPFR--------PGPLPPFPNSSDSFGAP 821
Cdd:pfam03154 227 PhtliqqtptlhpqrLPSPHPPLQPMTqppppsqvspqPLPQPSLHGQMPPMPHSlqtgpshmQHPVPPQPFPLTPQSSQ 306

                         170
                  ....*....|..
gi 1907066845 822 PQVPSRPTRAPP 833
Cdd:pfam03154 307 SQVPPGPSPAAP 318
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
 516-618 1.44e-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: 44.94  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 516 VIRKGWLTVSNiGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMS-SKHVFALF---NTEQRN 591
Cdd:cd13378     3 VLKAGWLKKQR-SIMKNWQQ-RWFVLRGDQLFYYKDEEETKPQGCISLQGSQVNELPPNPEEpGKHLFEILpggAGDREK 80

                          90       100
                  ....*....|....*....|....*..
gi 1907066845 592 VYKDYRFLELACDSQEDVDSWKASLLR 618
Cdd:cd13378    81 VPMNHEAFLLMANSQSDMEDWVKAIRR 107
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 737-836 1.47e-05

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: 46.22  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 737 TATVSTPAPPPVDDSwlqhsrrSPPPSPTTQRR----LTISAPLPRPtSGRG---------------PAPAIPSPGPHS- 796
Cdd:cd21975    43 AKGPGPPGPAWKPDG-------ADSPGLVTAAPhllaANVLAPLRGP-SVEGsslesgdadmgsdsdVAPASGAAASTSp 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907066845 797 ---GAPPVPFRPGPLPPFPNSSDSFGAPPQVPSRPTRAPPSVP 836
Cdd:cd21975   115 essSDAASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTP 157
PHA03378 PHA03378
EBNA-3B; Provisional
 697-848 2.54e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.14  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 697 SSEDQNTLMEESAEQAQRRDEMLRMYQALKEALAIIGDINTATVSTPAPPP------VDDSWLQHSRRSPPPSPT--TQR 768
Cdd:PHA03378  605 TPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPHQPPqveitpYKPTWTQIGHIPYQPSPTgaNTM 684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 769 RLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPfPNSSDSFGAPPQvpSRPTRAPPSVPRFGAVKEEAVEP 848
Cdd:PHA03378  685 LPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARP-PAAAPGRARPPA--AAPGRARPPAAAPGRARPPAAAP 761
PHA03247 PHA03247
large tegument protein UL36; Provisional
 741-833 2.71e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  741 STPAPPPVDDswlqHSRRSPPPSP----TTQRRLTISAPLPRPTSGRGPAPA---------IPSPGPHSGAPPVPFRPGP 807
Cdd:PHA03247  2612 APPSPLPPDT----HAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGrvsrprrarRLGRAAQASSPPQRPRRRA 2687

                           90       100
                   ....*....|....*....|....*.
gi 1907066845  808 LPPFPNSSDSFGAPPQVPSRPTRAPP 833
Cdd:PHA03247  2688 ARPTVGSLTSLADPPPPPPTPEPAPH 2713
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 730-848 3.94e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 730 AIIGDINTATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPG--P 807
Cdd:PRK07764  661 DASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDpvP 740

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907066845 808 LPPFPnssDSFGAPPQVPSRPTRAPPSVPRFGAVKEEAVEP 848
Cdd:PRK07764  741 LPPEP---DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSP 778
PHA03247 PHA03247
large tegument protein UL36; Provisional
 737-841 4.00e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 4.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  737 TATVSTPAPPPVDDSWLQHSRRSPPPSPTT--QRRLTISAPLP-RPTSGRGPAPAIPSPGPHSGAPPVPFRPG---PLPP 810
Cdd:PHA03247  2748 PATPGGPARPARPPTTAGPPAPAPPAAPAAgpPRRLTRPAVASlSESRESLPSPWDPADPPAAVLAPAAALPPaasPAGP 2827

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907066845  811 FPNSSDSFGAPPQVPSRPTraPPSVPRFGAV 841
Cdd:PHA03247  2828 LPPPTSAQPTAPPPPPGPP--PPSLPLGGSV 2856
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 752-837 4.05e-05

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: 46.92  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 752 WL-QHSRRSPPPS------PTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSFGAPPQV 824
Cdd:NF041121   10 WLaAQMGRAAAPPspegpaPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAAL 89

                          90
                  ....*....|...
gi 1907066845 825 PSRpTRAPPSVPR 837
Cdd:NF041121   90 PVR-VPAPPALPN 101
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 736-848 4.12e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.02  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 736 NTATVSTPAPPPVDDSwlqHSRRSPPPSPTTQRRLTiSAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSS 815
Cdd:PRK14951  382 ARPEAAAPAAAPVAQA---AAAPAPAAAPAAAASAP-AAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAP 457

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907066845 816 DSFGAPPQVPSRPTRAPPSVPRFGAVKEEAVEP 848
Cdd:PRK14951  458 ETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
PHA03247 PHA03247
large tegument protein UL36; Provisional
 738-837 5.38e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  738 ATVSTPAPPPvddswlqhsrRSPPPSPTTqrrLTISAPLPR-PTSGRGPAPA-----IPSPGPHSGAPPVPFRPGPLPPF 811
Cdd:PHA03247  2696 TSLADPPPPP----------PTPEPAPHA---LVSATPLPPgPAAARQASPAlpaapAPPAVPAGPATPGGPARPARPPT 2762

                           90       100
                   ....*....|....*....|....*.
gi 1907066845  812 PNSSDSfGAPPQVPsrPTRAPPSVPR 837
Cdd:PHA03247  2763 TAGPPA-PAPPAAP--AAGPPRRLTR 2785
PHA03247 PHA03247
large tegument protein UL36; Provisional
 764-847 5.47e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  764 PTTQRRLTISAPL------PRPTSGRGPApAIPSPGPHSGAPPVPFRPGPLPPFPNSSDS--------FGAPPQVPSRPT 829
Cdd:PHA03247   236 PFVERRVVISHPLrgdiaaPAPPPVVGEG-ADRAPETARGATGPPPPPEAAAPNGAAAPPdgvwgaalAGAPLALPAPPD 314

                           90
                   ....*....|....*...
gi 1907066845  830 RAPPsvPRFGAVKEEAVE 847
Cdd:PHA03247   315 PPPP--APAGDAEEEDDE 330
PHA03247 PHA03247
large tegument protein UL36; Provisional
 744-835 6.76e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  744 APP-------PVDDSwlQHSRRSPPPSPTTQRrltiSAPLPRPTSGRGPAPAIPsPGPHSGAPPVPFRPGPLPPFPNSSD 816
Cdd:PHA03247  2591 APPqsarpraPVDDR--GDPRGPAPPSPLPPD----THAPDPPPPSPSPAANEP-DPHPPPTVPPPERPRDDPAPGRVSR 2663

                           90       100       110
                   ....*....|....*....|....*....|
gi 1907066845  817 S-----------FGAPPQVPSRPTrAPPSV 835
Cdd:PHA03247  2664 PrrarrlgraaqASSPPQRPRRRA-ARPTV 2692
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 743-834 7.43e-05

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: 46.68  E-value: 7.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 743 PAPPPVDDSWLQHSRRSPPPSPTTQrrltisapLPRPTSGRGPAPAiPSPGPHSGAPPvpfRPGPLPPFPNSSDSFGAPP 822
Cdd:pfam03154 292 PVPPQPFPLTPQSSQSQVPPGPSPA--------APGQSQQRIHTPP-SQSQLQSQQPP---REQPLPPAPLSMPHIKPPP 359

                          90
                  ....*....|..
gi 1907066845 823 QVPSRPTRAPPS 834
Cdd:pfam03154 360 TTPIPQLPNPQS 371
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 759-837 7.49e-05

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: 42.76  E-value: 7.49e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907066845 759 SPPPSPttqrrltisAPLPRPTSGRGPAPAIPSPgphsgaPPVPFRPGPLPPfpnSSDSFGAPPQVPSRPTRAPPSVPR 837
Cdd:pfam12526  30 SPPESA---------HPDPPPPVGDPRPPVVDTP------PPVSAVWVLPPP---SEPAAPEPDLVPPVTGPAGPPSPL 90
PHA03378 PHA03378
EBNA-3B; Provisional
 742-836 7.62e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.60  E-value: 7.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 742 TPAPPPVddswLQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPfPNSSDSFGAP 821
Cdd:PHA03378  702 TPMRPPA----APPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARP-PAAAPGAPTP 776

                          90
                  ....*....|....*...
gi 1907066845 822 ---PQVPSRPTRAPPSVP 836
Cdd:PHA03378  777 qppPQAPPAPQQRPRGAP 794
PHA03247 PHA03247
large tegument protein UL36; Provisional
 727-848 7.74e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 7.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  727 EALAIIGDINTATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRR-LTISAPLPRPTS-GRGPAPAIP--------SPGPHS 796
Cdd:PHA03247  2796 ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTApPPPPGPPPPSLPlGGSVAPGGDvrrrppsrSPAAKP 2875

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907066845  797 GAPP-VPFRPGPLPPFPNSSDSFGAPPQVPSR-PTRAPPSVPRFGAVKEEAVEP 848
Cdd:PHA03247  2876 AAPArPPVRRLARPAVSRSTESFALPPDQPERpPQPQAPPPPQPQPQPPPPPQP 2929
PH2_PH_fungal cd13299
Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal ...
 514-616 1.08e-04

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


Pssm-ID: 270111  Cd Length: 102  Bit Score: 42.23  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 514 NQVIRKGWLTVsnigiMKGGS----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNL-KVRDVEKGFMSSKHVFALFNTE 588
Cdd:cd13299     4 ERVIEQGYLQV-----LKKKGvnqwKKYWLVLRNRSLSFYKDQSEYSPVKIIPIDDIiDVVELDPLSKSKKWCLQIITPE 78

                          90       100
                  ....*....|....*....|....*...
gi 1907066845 589 QRnvykdYRFlelACDSQEDVDSWKASL 616
Cdd:cd13299    79 KR-----IRF---CADDEESLIKWLGAL 98
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
 513-616 1.16e-04

Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the third MyoX PH repeat. PLEKHH3/Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) member 3 is also part of this CD and like MyoX contains a FERM domain, a MyTH4 domain, and a single PH domain. Not much is known about the function of PLEKHH3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270109  Cd Length: 126  Bit Score: 42.81  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 513 GNQVIRKGWLT--VSNIGIMKGGS-KGYWFVLTAESLSWYKD-DEEKEKKYMLPLDNL--KVRDVEKgfMSSKHVFALFn 586
Cdd:cd13297    10 GQDVIERGWLYkeGGKGGARGNLTkKKRWFVLTGNSLDYYKSsEKNSLKLGTLVLNSLcsVVPPDEK--MAKETGYWTF- 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907066845 587 teqrNVYKDYRFLELACDSQEDVDSWKASL 616
Cdd:cd13297    87 ----TVHGRKHSFRLYTKLQEEAMRWVNAI 112
PHA03378 PHA03378
EBNA-3B; Provisional
 738-833 1.49e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 738 ATVSTPAPPPvddswlqhSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPfPNSSDS 817
Cdd:PHA03378  692 GTMQPPPRAP--------TPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARP-PAAAPG 762

                          90
                  ....*....|....*..
gi 1907066845 818 FGAPPQ-VPSRPTRAPP 833
Cdd:PHA03378  763 RARPPAaAPGAPTPQPP 779
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 734-836 1.61e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 734 DINTATVSTPAP----PPVDDSWLQHSRRSPPPSPTTQrrltiSAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLP 809
Cdd:pfam03154 140 DNRSTSPSIPSPqdneSDSDSSAQQQILQTQPPVLQAQ-----SGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT 214

                          90       100
                  ....*....|....*....|....*....
gi 1907066845 810 PFPNSSDSFGAPPQ--VPSRPTRAPPSVP 836
Cdd:pfam03154 215 SQPPNQTQSTAAPHtlIQQTPTLHPQRLP 243
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
709-848 1.69e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.25  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 709 AEQAQRRDEMLRMYQALKEALAIIGDINTATVSTPAPPPVddswlqhSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPA 788
Cdd:PRK12323  420 AAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPA-------AAARPAAAGPRPVAAAAAAAPARAAPAAAPAPA 492

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907066845 789 IPSPGPHSGAPPVPFRPGPLPPFP-------NSSDSFGAPPQVPSRPTRAPPSVPRFGAVKEEAVEP 848
Cdd:PRK12323  493 DDDPPPWEELPPEFASPAPAQPDAapagwvaESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEP 559
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
 514-616 1.77e-04

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275402  Cd Length: 116  Bit Score: 41.84  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 514 NQVIRKGWLTvsnigiMKGGSKG----YWFVLTAESLSWYKDDEEkekKYmLPLDNLKVRDV-----EKGFMSSKHVFAL 584
Cdd:cd13215    19 GAVIKSGYLS------KRSKRTLrytrYWFVLKGDTLSWYNSSTD---LY-FPAGTIDLRYAtsielSKSNGEATTSFKI 88

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907066845 585 FNTEQRnvykdYRFLelaCDSQEDVDSWKASL 616
Cdd:cd13215    89 VTNSRT-----YKFK---ADSETSADEWVKAL 112
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 736-848 1.86e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 736 NTATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTisAPLPRPTSGRGPAPAIP----SPGPHSGAPPVPFRPGP-LPP 810
Cdd:PRK07764  672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA--TPPAGQADDPAAQPPQAaqgaSAPSPAADDPVPLPPEPdDPP 749

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907066845 811 FPNSSDSFGAPPQVPSRPTrAPPSVPRFGAVKEEAVEP 848
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAA-APAAAPPPSPPSEEEEMA 786
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
737-833 2.15e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 737 TATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRltiSAPLPRPTSGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPNSSD 816
Cdd:PRK12323  405 APAAAPAAAAAARAVAAAPARRSPAPEALAAAR---QASARGPGGAPAPAPA-PAAAPAAAARPAAAGPRPVAAAAAAAP 480

                          90
                  ....*....|....*..
gi 1907066845 817 SFGAPPQVPSRPTRAPP 833
Cdd:PRK12323  481 ARAAPAAAPAPADDDPP 497
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 741-837 3.00e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  741 STPAPPPVDDSWLQHSRRSPPPSPttqrrltiSAPLPRPTSGRGPAPaiPSPGPHSGAPPVPFRPGPLPPFPNSSDSFGA 820
Cdd:PHA03307   308 APSSPRASSSSSSSRESSSSSTSS--------SSESSRGAAVSPGPS--PSRSPSPSRPPPPADPSSPRKRPRPSRAPSS 377

                           90       100
                   ....*....|....*....|....
gi 1907066845  821 PPQVPSRPTR-------APPSVPR 837
Cdd:PHA03307   378 PAASAGRPTRrraraavAGRARRR 401
TYA pfam01021
Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a ...
 735-826 3.57e-04

Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a fusion protein of TYA and TYB. The TYA protein is analogous to the gag protein of retroviruses. TYA a is cleaved to form 46kd protein which can form mature virion like particles. This entry corresponds to the capsid protein from Ty1 and Ty2 transposons.


Pssm-ID: 425992  Cd Length: 384  Bit Score: 43.79  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 735 INTATVSTPAPPPVDDSwlqHSRRSPPPSpttqrrltiSAPLPR--PTSGRG---PAPAIPSPGPHSGAP---------- 799
Cdd:pfam01021  34 ANSQQTTTPGSSAVPEN---HHHASPQPA---------SVPPPQngPYSQQCmmtPNQANPSGWPFYGHPsmmpytpyqm 101

                          90       100
                  ....*....|....*....|....*...
gi 1907066845 800 -PVPFRPGPLPPFPNSSDSFGAPPQVPS 826
Cdd:pfam01021 102 sPMYFPPGPQSQFPQYPSSVGTPLSTPS 129
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
 703-825 3.94e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 44.06  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 703 TLMEESAEQAQRRDEMLRMYQALKEAL-AIIGDINTATVSTPAPPPVDDSWLQHSRRSPPPSPTTqrrltisaplprPTS 781
Cdd:PRK14963  313 TALDEQMERFARRSDALSLELALLHALlALGGAPSEGVAAVAPPAPAPADLTQRLNRLEKEVRSL------------RSA 380

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907066845 782 GRGPAPAIPSPGPHSGapPVPFR-PGPLPPFPNSSDSFGAPPQVP 825
Cdd:PRK14963  381 PTAAATAAGAPLPDFD--PRPRGpPAPEPARSAEAPPLVAPAAAP 423
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 727-848 4.14e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 4.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  727 EALAIIGDINTATVSTPAP---PPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPhsgaPPVPF 803
Cdd:PHA03307    49 ELAAVTVVAGAAACDRFEPptgPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPP----TPPPA 124

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907066845  804 RPGPLPPFPNSSDSFGAPPQVPSRPTRAPPSVPRFGAVKEEAVEP 848
Cdd:PHA03307   125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASS 169
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
 538-618 4.15e-04

Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of cytoplasmic protein tyrosine kinases that includes BMX, IL2-inducible T-cell kinase (Itk) and Tec. Btk plays a role in the maturation of B cells. Tec proteins general have an N-terminal PH domain, followed by a Tek homology (TH) domain, a SH3 domain, a SH2 domain and a kinase domain. The Btk PH domain binds phosphatidylinositol 3,4,5-trisphosphate and responds to signalling via phosphatidylinositol 3-kinase. The PH domain is also involved in membrane anchoring which is confirmed by the discovery of a mutation of a critical arginine residue in the BTK PH domain. This results in severe human immunodeficiency known as X-linked agammaglobulinemia (XLA) in humans and a related disorder is mice.PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269944 [Multi-domain]  Cd Length: 140  Bit Score: 41.44  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 538 WFVLTAESLSWYKDDEEKEKKY--MLPLDnlKVRDVEK----GFMSSKHVFALfnteqrnVYKDYrFLELACDSQEDVDS 611
Cdd:cd01238    24 WFVLTKSSLSYYEGDGEKRGKEkgSIDLS--KVRCVEEvkdeAFFERKYPFQV-------VYDDY-TLYVFAPSEEDRDE 93


                  ....*..
gi 1907066845 612 WKASLLR 618
Cdd:cd01238    94 WIAALRK 100
PHA03247 PHA03247
large tegument protein UL36; Provisional
 743-837 4.80e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 4.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  743 PAPPPVDDswlqhsrrspPPSPTTQRRLTISAPLPRPtsgrgPAPAIPSPGPHSGAPPVPFRPG---------PLPPFPN 813
Cdd:PHA03247  2551 PPPPLPPA----------APPAAPDRSVPPPRPAPRP-----SEPAVTSRARRPDAPPQSARPRapvddrgdpRGPAPPS 2615

                           90       100
                   ....*....|....*....|....
gi 1907066845  814 SsdsfgAPPQVPsrPTRAPPSVPR 837
Cdd:PHA03247  2616 P-----LPPDTH--APDPPPPSPS 2632
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 736-848 4.82e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 736 NTATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRPTSG-----RGPAPAIPSPGPHSGAPPVPfRPGPLPP 810
Cdd:PRK07764  642 APAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAapaapAGAAPAQPAPAPAATPPAGQ-ADDPAAQ 720

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907066845 811 FPNSSDSFGAPPQVPSRPTRAPPSVPRFGAVKEEAVEP 848
Cdd:PRK07764  721 PPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP 758
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 760-848 5.41e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 43.64  E-value: 5.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 760 PPPSPTTqrrLTISAPLPRPTSGrGPAPAI-PSPGPHSGAPPVPFRPGPLPPFPNSSDSfgAPPQVPSRPTRAPPSVPRF 838
Cdd:PRK14950  362 PVPAPQP---AKPTAAAPSPVRP-TPAPSTrPKAAAAANIPPKEPVRETATPPPVPPRP--VAPPVPHTPESAPKLTRAA 435

                          90
                  ....*....|
gi 1907066845 839 GAVKEEAVEP 848
Cdd:PRK14950  436 IPVDEKPKYT 445
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 759-837 6.24e-04

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


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 40.06  E-value: 6.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907066845 759 SPPPSPTTQRRLTISAPLPRPtsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSdsfgAPPQVPSRPTRAPPSVPR 837
Cdd:pfam12526  38 DPPPPVGDPRPPVVDTPPPVS-----AVWVLPPPSEPAAPEPDLVPPVTGPAGPPSP----LAPPAPAQKPPLPPPRPQ 107
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
 753-846 7.29e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 43.19  E-value: 7.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 753 LQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSF-GAPPQVPSRPTRA 831
Cdd:PRK14965  374 LEALERGAPAPPSAAWGAPTPAAPAAPPPAAAPPVPPAAPARPAAARPAPAPAPPAAAAPPARSADpAAAASAGDRWRAF 453

                          90
                  ....*....|....*....
gi 1907066845 832 PPSV----PRFGAVKEEAV 846
Cdd:PRK14965  454 VAFVkgkkPALGASLEQGS 472
PH_SWAP-70 cd13273
Switch-associated protein-70 Pleckstrin homology (PH) domain; SWAP-70 (also called ...
 516-564 8.40e-04

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


Pssm-ID: 270092  Cd Length: 110  Bit Score: 39.59  E-value: 8.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907066845 516 VIRKGWLtvsnigiMKGGSK-----GYWFVLTAESLSWYKDDEEKEKKYMLPLD 564
Cdd:cd13273     8 VIKKGYL-------WKKGHLlptwtERWFVLKPNSLSYYKSEDLKEKKGEIALD 54
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
 515-619 9.36e-04

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the first PH domain repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270113  Cd Length: 108  Bit Score: 39.66  E-value: 9.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 515 QVIRKGWLtvsnigiMKGGS-----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQ 589
Cdd:cd13301     2 GIIKEGYL-------VKKGHvvnnwKARWFVLKEDGLEYYKKKTDSSPKGMIPLKGCTITSPCLEYGKRPLVFKLTTAKG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907066845 590 rnvyKDYrFLElACdSQEDVDSWKASLLRA 619
Cdd:cd13301    75 ----QEH-FFQ-AC-SREERDAWAKDITKA 97
HpaP TIGR02557
type III secretion protein HpaP; This family of genes is always found in type III secretion ...
 761-842 1.17e-03

type III secretion protein HpaP; This family of genes is always found in type III secretion operons, althought its function in the processes of secretion and virulence is unclear. Hpa stands for Hrp-associated gene, where Hrp stands for hypersensitivity response and virulence.


Pssm-ID: 274200  Cd Length: 201  Bit Score: 41.03  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 761 PPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPvpfRPGPLPPFPnsSDSFGA-----PPQVPSRPTRAPPSv 835
Cdd:TIGR02557  14 DPARPARRRTPLAQLRRRDALAYAPPPRPEPPPPCDEDRP---EPRADTRAS--DPPPEAptdadPAQPPDDPDASAHT- 87


                  ....*..
gi 1907066845 836 pRFGAVK 842
Cdd:TIGR02557  88 -AAIASG 93
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 737-843 1.27e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 737 TATVSTPAPPPVDDswlQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAiPSPGPHSGAPPVPfRPGPLPPFPNSSD 816
Cdd:PRK07764  417 PAAAAAPAPAAAPQ---PAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ-PAPAPAAAPEPTA-APAPAPPAAPAPA 491

                          90       100
                  ....*....|....*....|....*..
gi 1907066845 817 sfgAPPQVPSRPTrAPPSVPRFGAVKE 843
Cdd:PRK07764  492 ---AAPAAPAAPA-APAGADDAATLRE 514
Tymo_45kd_70kd pfam03251
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a ...
 745-838 1.28e-03

Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a protein of unknown function that has been named based on its molecular weight. Tymoviruses such as the ononis yellow mosaic tymovirus encode only three proteins. Of these two are overlapping this protein overlaps a larger ORF that is thought to be the polymerase.


Pssm-ID: 281269 [Multi-domain]  Cd Length: 468  Bit Score: 42.09  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 745 PPPVDDS--------WLQHSRRSPPPSPTTqrrltisaPLPRPTSGRGPAPAIPSPGPHSGAPPVPFR----PGPLPPFP 812
Cdd:pfam03251 231 PPPLSDDpgilgprpLAPHSTRDPPPRPIT--------PGPSNTHDLRPLSVLPRTSPRRGLLPNPRRhrtsTGHIPPTT 302

                          90       100
                  ....*....|....*....|....*....
gi 1907066845 813 NSSDSfgAPPQVPSRPT---RAPPSVPRF 838
Cdd:pfam03251 303 TSRPT--GPPSRLQRPVhlyQSSPHTPNF 329
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
 512-619 1.31e-03

Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP2 contains two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. The members here are most sequence similar to TAPP2 proteins, but may not be actual TAPP2 proteins. 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: 270075  Cd Length: 110  Bit Score: 39.32  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 512 IGNQVIRKGWLtvsnigiMKGGS-----KGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLK-VRDVEKGfmSSKHVFALF 585
Cdd:cd13255     2 ISEAVLKAGYL-------EKKGErrktwKKRWFVLRPTKLAYYKNDKEYRLLRLIDLTDIHtCTEVQLK--KHDNTFGIV 72

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907066845 586 nTEQRNVYkdyrfleLACDSQEDVDSWKASLLRA 619
Cdd:cd13255    73 -TPARTFY-------VQADSKAEMESWISAINLA 98
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
737-848 1.55e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 737 TATVSTPAPPPVddswlqhsRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPnssd 816
Cdd:PRK07003  416 AAAAATRAEAPP--------AAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASD---- 483

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907066845 817 sfgAPPQVPSRPtrAPPSVPRFGAVKEEAVEP 848
Cdd:PRK07003  484 ---APPDAAFEP--APRAAAPSAATPAAVPDA 510
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 737-837 1.55e-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: 41.68  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 737 TATVSTPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPrptsgrGPAPAIPSPGPhsGAPPVPFRPGPLPPFPNSSD 816
Cdd:NF040712  228 ATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAA------EPDEATRDAGE--PPAPGAAETPEAAEPPAPAP 299

                          90       100
                  ....*....|....*....|....*.
gi 1907066845 817 SFGAPPQVPS-----RPTRAPPSVPR 837
Cdd:NF040712  300 AAPAAPAAPEaeepaRPEPPPAPKPK 325
PH_CNK_mammalian-like cd01260
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
 520-619 1.65e-03

Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and, with the exception of CNK3, a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from mammals, chickens, amphibians, fish, and crustacea. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269962  Cd Length: 114  Bit Score: 38.93  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 520 GWLTV--SNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKV---RDVEKgfmssKHVFALfnteQRNVYK 594
Cdd:cd01260    17 GWLWKkkEAKSFFGQKWKKYWFVLKGSSLYWYSNQQDEKAEGFINLPDFKIeraSECKK-----KYAFKA----CHPKIK 87

                          90       100
                  ....*....|....*....|....*
gi 1907066845 595 DYRFlelACDSQEDVDSWKASLLRA 619
Cdd:cd01260    88 TFYF---AAENLDDMNKWLSKLNMA 109
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 725-848 1.75e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  725 LKEALAIIGDINTATVSTPAPPPVD---------------------DSWLQHSRRSPPPS-PTTQRRLTISAPLPRPTSG 782
Cdd:PHA03307    10 LIEAAAEGGEFFPRPPATPGDAADDllsgsqgqlvsdsaelaavtvVAGAAACDRFEPPTgPPPGPGTEAPANESRSTPT 89

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907066845  783 RGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSFGAPPQVPSRPTRAPPSVPRFGAVKEEAVEP 848
Cdd:PHA03307    90 WSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAA 155
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 739-836 2.06e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845  739 TVSTPAPPPVDDSWLQHSRRSPPPSPTTqrrltISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSF 818
Cdd:PHA03307    93 STLAPASPAREGSPTPPGPSSPDPPPPT-----PPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAA 167

                           90       100
                   ....*....|....*....|...
gi 1907066845  819 GAPP-----QVPSRPTRAPPSVP 836
Cdd:PHA03307   168 SSRQaalplSSPEETARAPSSPP 190
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 738-848 2.07e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 738 ATVSTPAPPPVddswlqhSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPfrpgPLPPFPNSSDS 817
Cdd:PRK07764  391 AGAPAAAAPSA-------AAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNA----PAGGAPSPPPA 459

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907066845 818 FGAPPQVPSRPTRAPPSVPRFGAVKEEAVEP 848
Cdd:PRK07764  460 AAPSAQPAPAPAAAPEPTAAPAPAPPAAPAP 490
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 741-837 2.60e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 741 STPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPL----PRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSd 816
Cdd:PRK07764  628 APAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASdggdGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA- 706

                          90       100
                  ....*....|....*....|.
gi 1907066845 817 sFGAPPQVPSRPTRAPPSVPR 837
Cdd:PRK07764  707 -ATPPAGQADDPAAQPPQAAQ 726
PH_Boi cd13316
Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally ...
 519-619 2.66e-03

Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally redundant and important for cell growth with Boi mutants displaying defects in bud formation and in the maintenance of cell polarity.They appear to be linked to Rho-type GTPase, Cdc42 and Rho3. Boi1 and Boi2 display two-hybrid interactions with the GTP-bound ("active") form of Cdc42, while Rho3 can suppress of the lethality caused by deletion of Boi1 and Boi2. These findings suggest that Boi1 and Boi2 are targets of Cdc42 that promote cell growth in a manner that is regulated by Rho3. Boi proteins contain a N-terminal SH3 domain, followed by a SAM (sterile alpha motif) domain, a proline-rich region, which mediates binding to the second SH3 domain of Bem1, and C-terminal PH domain. The PH domain is essential for its function in cell growth and is important for localization to the bud, while the SH3 domain is needed for localization to the neck. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270126  Cd Length: 97  Bit Score: 38.12  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 519 KGWLTvsnigiMKGGSKGYW----FVLTAESLSWYKDDEEKEKKYMLPLDNLKV-RDVEKGFMSSKHVFALFNTEQRNVY 593
Cdd:cd13316     3 SGWMK------KRGERYGTWktryFVLKGTRLYYLKSENDDKEKGLIDLTGHRVvPDDSNSPFRGSYGFKLVPPAVPKVH 76

                          90       100
                  ....*....|....*....|....*.
gi 1907066845 594 kdYrfleLACDSQEDVDSWKASLLRA 619
Cdd:cd13316    77 --Y----FAVDEKEELREWMKALMKA 96
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 741-848 3.35e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.85  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 741 STPAPPPvddswlqhSRRSPPPSPTTQRrltiSAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSFGA 820
Cdd:PRK14951  369 AAEAAAP--------AEKKTPARPEAAA----PAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAA 436

                          90       100
                  ....*....|....*....|....*...
gi 1907066845 821 PPQVPSRPTRAPPSVPRFGAVKEEAVEP 848
Cdd:PRK14951  437 APAAAPAAVALAPAPPAQAAPETVAIPV 464
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
 516-619 3.43e-03

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270083  Cd Length: 114  Bit Score: 38.13  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 516 VIRKGWLTVSNiGIMKGGSKgYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVE-KGFMSSKHVFALF----NTEQR 590
Cdd:cd13263     3 PIKSGWLKKQG-SIVKNWQQ-RWFVLRGDQLYYYKDEDDTKPQGTIPLPGNKVKEVPfNPEEPGKFLFEIIpgggGDRMT 80

                          90       100
                  ....*....|....*....|....*....
gi 1907066845 591 NVYKDYRfleLACDSQEDVDSWKASLLRA 619
Cdd:cd13263    81 SNHDSYL---LMANSQAEMEEWVKVIRRV 106
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 741-829 3.73e-03

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 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 KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 39.64  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 741 STPAPPPVDDSWLQHSRRSPP--------PSPTTQRRLTISAPLPrptsgrgPAPAIPSPGPHSGAPPVPFRPGPLP--- 809
Cdd:cd21577    36 SSSSSSSSSSSSSPSSRASPPspysksspPSPPQQRPLSPPLSLP-------PPVAPPPLSPGSVPGGLPVISPVMVqpv 108

                          90       100
                  ....*....|....*....|
gi 1907066845 810 PFPNSSdSFGAPPQVPSRPT 829
Cdd:cd21577   109 PVLYPP-HLHQPIMVSSSPP 127
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 742-836 4.45e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 742 TPAPPPVddswlqhsrRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPG-------PHSGAPPVPFRPGPLPPFPNS 814
Cdd:PRK07764  407 AAAPAPA---------AAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPaggapspPPAAAPSAQPAPAPAAAPEPT 477

                          90       100
                  ....*....|....*....|...
gi 1907066845 815 SDSFGAPPQVPSRPTR-APPSVP 836
Cdd:PRK07764  478 AAPAPAPPAAPAPAAApAAPAAP 500
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 741-840 4.73e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907066845 741 STPAPPPVDDSWLQHSRRSPPPSPTTQRRLTISAPLPRPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPNSSDSfGA 820
Cdd:PRK07764  627 PAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP-AP 705

                          90       100
                  ....*....|....*....|
gi 1907066845 821 PPQVPSRPTRAPPSVPRFGA 840
Cdd:PRK07764  706 AATPPAGQADDPAAQPPQAA 725
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
 518-556 4.84e-03

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270094  Cd Length: 104  Bit Score: 37.31  E-value: 4.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907066845 518 RKGWLtvsnigiMKGGSKG-----YWFVLTAESLSWYKD--DEEKE 556
Cdd:cd13275     1 KKGWL-------MKQGSRQgewskHWFVLRGAALKYYRDpsAEEAG 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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