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Conserved domains on  [gi|2462507684|ref|XP_054191858|]
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dynamin-3 isoform X4 [Homo sapiens]

Protein Classification

dynamin( domain architecture ID 11249456)

dynamin such as human dynamin-1, which is involved in clathrin-mediated endocytosis and other vesicular trafficking processes; contains an N-terminal GTPase domain that binds and hydrolyzes GTP, a middle domain involved in self-assembly and oligomerization, and a pleckstrin homology (PH) domain responsible for interactions with the GTPase effector domain (GED)

CATH:  1.20.120.1240|2.30.29.30|3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  15040446
SCOP:  4004047|4002395|4004048

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 3.71e-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: 470.52  E-value: 3.71e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684   86 CKGKKFTDFDEVRLEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  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 5.74e-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: 415.38  E-value: 5.74e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2462507684 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 526-683 3.58e-71

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: 229.90  E-value: 3.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 526 VIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEipsqtgllpdlqqgfpllpheiysnqrckehlnsyflqevfp 605
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEE------------------------------------------ 40

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462507684 606 dhlqlkEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKDYRFLELACDSQEDVDSWKASLLRAGVYPDK 683
Cdd:cd01256    41 ------EKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
GED pfam02212
Dynamin GTPase effector domain;
707-797 2.40e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.09  E-value: 2.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 707 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 786
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 2462507684 787 LKEALGIIGDI 797
Cdd:pfam02212  81 LKQAREILSEV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 806-890 1.88e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  806 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSS-SDSF 880
Cdd:PHA03247  2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPaANEP 2638

                           90
                   ....*....|
gi 2462507684  881 GAPPQVPSRP 890
Cdd:PHA03247  2639 DPHPPPTVPP 2648
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 3.71e-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: 470.52  E-value: 3.71e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684   86 CKGKKFTDFDEVRLEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  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 1.82e-146

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: 434.37  E-value: 1.82e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRLE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462507684 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 5.74e-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: 415.38  E-value: 5.74e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2462507684 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 526-683 3.58e-71

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: 229.90  E-value: 3.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 526 VIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEipsqtgllpdlqqgfpllpheiysnqrckehlnsyflqevfp 605
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEE------------------------------------------ 40

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462507684 606 dhlqlkEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKDYRFLELACDSQEDVDSWKASLLRAGVYPDK 683
Cdd:cd01256    41 ------EKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 3.53e-69

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 226.73  E-value: 3.53e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirEMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 2462507684 186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
707-797 2.40e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.09  E-value: 2.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 707 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 786
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 2462507684 787 LKEALGIIGDI 797
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
706-797 1.34e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 110.02  E-value: 1.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  706 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 785
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 2462507684  786 ALKEALGIIGDI 797
Cdd:smart00302  81 LLKKARQIIAAV 92
PHA03247 PHA03247
large tegument protein UL36; Provisional
 806-890 1.88e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  806 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSS-SDSF 880
Cdd:PHA03247  2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPaANEP 2638

                           90
                   ....*....|
gi 2462507684  881 GAPPQVPSRP 890
Cdd:PHA03247  2639 DPHPPPTVPP 2648
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 526-677 5.98e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 48.71  E-value: 5.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 526 VIRKGWLTISNIGImKGGSKGYWFVLTAESLSWYKDDEIPsqtgllpdlqqgfpllpheiysnqrckehlnsyflqevfp 605
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDKSG---------------------------------------- 39

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462507684 606 dhlqlKEKEKKYMLPLDNLKVRDVEKSFMSS-KHIFALFNTEQRNVykdyRFLELACDSQEDVDSWKASLLRA 677
Cdd:pfam00169  40 -----KSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTGK----RTYLLQAESEEERKDWIKAIQSA 103
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 526-677 7.23e-07

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: 48.31  E-value: 7.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  526 VIRKGWLTISNIGiMKGGSKGYWFVLTAESLSWYKDDEipsqtgllpdlqqgfpllpheiysnqrckehlnsyflqevfp 605
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKK------------------------------------------ 37

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462507684  606 dhlQLKEKEKKYMLPLDNLKVRD-VEKSFMSSKHIFALFNTEQRNVYkdyrfleLACDSQEDVDSWKASLLRA 677
Cdd:smart00233  38 ---DKKSYKPKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKTLL-------LQAESEEEREKWVEALRKA 100
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 824-891 1.16e-06

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 50.76  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 824 PSPTTQRRPTLSAPLARPTSGRGPAPAIP--SPGPHS---------GAPPVPFRP------GPLPPFPSSSDSFGAP--- 883
Cdd:pfam15822 135 AAPSGPWGSMSSGPWAPGMGGQYPAPNMPypSPGPYPavpppqspgAAPPVPWGTvppgpwGPPAPYPDPTGSYPMPgly 214

                          90
                  ....*....|....
gi 2462507684 884 P------QVPSRPT 891
Cdd:pfam15822 215 PtpnnpfQVPSGPS 228
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 815-890 3.98e-06

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: 50.39  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 815 IQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGA----PPQVPSRP 890
Cdd:NF041121   18 AAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPgaalPVRVPAPP 97
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 805-890 2.94e-05

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: 47.20  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 805 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTlsaplarptsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSfgAPP 884
Cdd:NF040983   97 PPPPPPPPTPPPPPPPPPPPPPPSPPPPP-------------PPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPI--QPT 161


                  ....*.
gi 2462507684 885 QVPSRP 890
Cdd:NF040983  162 QLPSIP 167
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 799-890 8.86e-04

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: 40.83  E-value: 8.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 799 TATVSTPAPPPVDDSwiqhsrrSPPPSPTTQRRPTLSAPLARP---TSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPS 875
Cdd:cd21975    43 AKGPGPPGPAWKPDG-------ADSPGLVTAAPHLLAANVLAPlrgPSVEGSSLESGDADMGSDSDVAPASGAAASTSPE 115

                          90
                  ....*....|....*
gi 2462507684 876 SSDSFGAPPQVPSRP 890
Cdd:cd21975   116 SSSDAASSPSPLSLL 130
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 800-890 2.93e-03

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 41.14  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 800 ATVSTPAPPPVDDSwiQHSRRSPPPSPTTQRRPTLSAPlarptsGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSSDS 879
Cdd:NF041121   20 APPSPEGPAPTAAS--QPATPPPPAAPPSPPGDPPEPP------APEPAPL-PAPYPGSLAPPPPPPPGPAGAAPGAALP 90

                          90
                  ....*....|..
gi 2462507684 880 FGAP-PQVPSRP 890
Cdd:NF041121   91 VRVPaPPALPNP 102
 
Name Accession Description Interval E-value
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 6-245 3.71e-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: 470.52  E-value: 3.71e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684    6 MEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLH 85
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684   86 CKGKKFTDFDEVRLEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFIT 165
Cdd:smart00053  81 CKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  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 1.82e-146

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: 434.37  E-value: 1.82e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  29 LELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFLHCKGKKFTDFDEVRLE 100
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSpsesdedeKEEWGEFLHLKSKEFTDFEELREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 101 IEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTD 180
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 181 LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERK 257
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462507684 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 5.74e-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: 415.38  E-value: 5.74e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 215 DARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLP 294
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 295 NFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSgDQVDTLELSGGAKINRIFHERFPFEI 374
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 375 VKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCE 454
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2462507684 455 ETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQR 502
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 526-683 3.58e-71

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: 229.90  E-value: 3.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 526 VIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEipsqtgllpdlqqgfpllpheiysnqrckehlnsyflqevfp 605
Cdd:cd01256     3 VIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEE------------------------------------------ 40

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462507684 606 dhlqlkEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKDYRFLELACDSQEDVDSWKASLLRAGVYPDK 683
Cdd:cd01256    41 ------EKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVYKDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
Dynamin_N pfam00350
Dynamin family;
34-207 3.53e-69

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 226.73  E-value: 3.53e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  34 IAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTS--------KAEYAEFlhckGKKFTDFDEVRLEIEAET 105
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESpgasegavKVEYKDG----EKKFEDFSELREEIEKET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 106 DRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQppdieyqirEMIMQFItRENCLILAVTPANTDLANSD 185
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146

                         170       180
                  ....*....|....*....|..
gi 2462507684 186 ALKLAKEVDPQGLRTIGVITKL 207
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
707-797 2.40e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 126.09  E-value: 2.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 707 LERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQA 786
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 2462507684 787 LKEALGIIGDI 797
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
706-797 1.34e-28

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 110.02  E-value: 1.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  706 QLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQ 785
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 2462507684  786 ALKEALGIIGDI 797
Cdd:smart00302  81 LLKKARQIIAAV 92
PHA03247 PHA03247
large tegument protein UL36; Provisional
 806-890 1.88e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  806 APPPVDDSWIQHSRRSP-PPSPTTQ---RRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSS-SDSF 880
Cdd:PHA03247  2559 APPAAPDRSVPPPRPAPrPSEPAVTsraRRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPaANEP 2638

                           90
                   ....*....|
gi 2462507684  881 GAPPQVPSRP 890
Cdd:PHA03247  2639 DPHPPPTVPP 2648
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 526-677 5.98e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 48.71  E-value: 5.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 526 VIRKGWLTISNIGImKGGSKGYWFVLTAESLSWYKDDEIPsqtgllpdlqqgfpllpheiysnqrckehlnsyflqevfp 605
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYKDDKSG---------------------------------------- 39

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462507684 606 dhlqlKEKEKKYMLPLDNLKVRDVEKSFMSS-KHIFALFNTEQRNVykdyRFLELACDSQEDVDSWKASLLRA 677
Cdd:pfam00169  40 -----KSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTGK----RTYLLQAESEEERKDWIKAIQSA 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 804-891 6.47e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 6.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  804 TPaPPPVDD--SWIQHSRRSPPPSPTTQRRPTLSAPLARPTSG------RGPAPA-IPSPGPHSGAPPVPFRP-GPLPPF 873
Cdd:PHA03247   360 TP-PSSLEDlsAGRHHPKRASLPTRKRRSARHAATPFARGPGGddqtrpAAPVPAsVPTPAPTPVPASAPPPPaTPLPSA 438

                           90
                   ....*....|....*...
gi 2462507684  874 PSSSDSFGAPPQVPSRPT 891
Cdd:PHA03247   439 EPGSDDGPAPPPERQPPA 456
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 526-677 7.23e-07

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: 48.31  E-value: 7.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  526 VIRKGWLTISNIGiMKGGSKGYWFVLTAESLSWYKDDEipsqtgllpdlqqgfpllpheiysnqrckehlnsyflqevfp 605
Cdd:smart00233   1 VIKEGWLYKKSGG-GKKSWKKRYFVLFNSTLLYYKSKK------------------------------------------ 37

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462507684  606 dhlQLKEKEKKYMLPLDNLKVRD-VEKSFMSSKHIFALFNTEQRNVYkdyrfleLACDSQEDVDSWKASLLRA 677
Cdd:smart00233  38 ---DKKSYKPKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKTLL-------LQAESEEEREKWVEALRKA 100
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 800-890 8.75e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 53.25  E-value: 8.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  800 ATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARP------TSGRGPAPAIPSPGPHSGAPpvpfrPGPLPPF 873
Cdd:PHA03307   119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAavasdaASSRQAALPLSSPEETARAP-----SSPPAEP 193

                           90
                   ....*....|....*....
gi 2462507684  874 PSSSDSFGAP--PQVPSRP 890
Cdd:PHA03307   194 PPSTPPAAASprPPRRSSP 212
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 824-891 1.16e-06

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 50.76  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 824 PSPTTQRRPTLSAPLARPTSGRGPAPAIP--SPGPHS---------GAPPVPFRP------GPLPPFPSSSDSFGAP--- 883
Cdd:pfam15822 135 AAPSGPWGSMSSGPWAPGMGGQYPAPNMPypSPGPYPavpppqspgAAPPVPWGTvppgpwGPPAPYPDPTGSYPMPgly 214

                          90
                  ....*....|....
gi 2462507684 884 P------QVPSRPT 891
Cdd:pfam15822 215 PtpnnpfQVPSGPS 228
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 800-890 1.22e-06

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 51.02  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 800 ATVSTPAPP--------PVDDSWIQHSRR---SPPPSPTT-QRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFrP 867
Cdd:PHA02682   32 ATIPAPAAPcppdadvdPLDKYSVKEAGRyyqSRLKANSAcMQRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVTC-P 110

                          90       100
                  ....*....|....*....|....*.
gi 2462507684 868 GPLPPFPSSSDSFGAPPQV---PSRP 890
Cdd:PHA02682  111 APAPACPPATAPTCPPPAVcpaPARP 136
PHA03247 PHA03247
large tegument protein UL36; Provisional
 795-891 1.88e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 1.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  795 GDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSG---RGPAPAIPSPGPHSGAPPVPFRPGPLP 871
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpprRLTRPAVASLSESRESLPSPWDPADPP 2808

                           90       100
                   ....*....|....*....|...
gi 2462507684  872 ---PFPSSSDSFGAPPQVPSRPT 891
Cdd:PHA03247  2809 aavLAPAAALPPAASPAGPLPPP 2831
PHA03247 PHA03247
large tegument protein UL36; Provisional
 799-890 2.81e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  799 TATVSTPAPPPVDDSWIQHS------------------RRSPPPSPTTQRRPTLSApLARPTSGRGPAP-AIPSPGPHS- 858
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSlplggsvapggdvrrrppSRSPAAKPAAPARPPVRR-LARPAVSRSTESfALPPDQPERp 2908

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462507684  859 GAPPVPFRPGPLPPFPSSSDSFGAPPQvPSRP 890
Cdd:PHA03247  2909 PQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRP 2939
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 815-890 3.98e-06

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: 50.39  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 815 IQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGA----PPQVPSRP 890
Cdd:NF041121   18 AAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPgaalPVRVPAPP 97
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 798-883 5.83e-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: 48.44  E-value: 5.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 798 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPT-LSAPlarPTSGRGPAPAIPSPGphsgaPPVPFrPGPLPPFPSS 876
Cdd:pfam15822  52 STAPSTVPFGPAPTGMYPSIPLTGPSPGPPAPFPPSgPSCP---PPGGPYPAPTVPGPG-----PIGPY-PTPNMPFPEL 122


                  ....*..
gi 2462507684 877 SDSFGAP 883
Cdd:pfam15822 123 PRPYGAP 129
PHA03247 PHA03247
large tegument protein UL36; Provisional
 797-891 8.80e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 8.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  797 ISTATVSTPAPPPVddswiQHSRRSPPPSPTTQRRPTLSAPL----ARPTSGRGPAPAIPSPGPHSGAPPVPFRPGP--- 869
Cdd:PHA03247  2891 VSRSTESFALPPDQ-----PERPPQPQAPPPPQPQPQPPPPPqpqpPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPwlg 2965

                           90       100
                   ....*....|....*....|...
gi 2462507684  870 -LPPFPSSSDSFGAPPQVPSRPT 891
Cdd:PHA03247  2966 aLVPGRVAVPRFRVPQPAPSREA 2988
PHA03247 PHA03247
large tegument protein UL36; Provisional
 806-890 1.74e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  806 APPPVDDswIQHSRRSPPPSPTTQRRPT-----LSAPLArPTSGRGPAPA-----IPSPGPHSGAPPVPFRPGPLPPFPS 875
Cdd:PHA03247  2688 ARPTVGS--LTSLADPPPPPPTPEPAPHalvsaTPLPPG-PAAARQASPAlpaapAPPAVPAGPATPGGPARPARPPTTA 2764

                           90
                   ....*....|....*
gi 2462507684  876 SSDSfGAPPQVPSRP 890
Cdd:PHA03247  2765 GPPA-PAPPAAPAAG 2778
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 767-890 2.42e-05

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: 47.23  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 767 MEESAEQAQRRDemlRMYQALkeALGIIGDISTATVSTPApppvddswIQHSRRSP-PPSPTTQRRPTLSAPLARPTSGR 845
Cdd:pfam07174   1 MDQVDPNSTRRK---GLWATL--AIAAVAGASAVAVALPA--------VAHADPEPaPPPPSTATAPPAPPPPPPAPAAP 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462507684 846 GPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRP 890
Cdd:pfam07174  68 APPPP-PAAPNAPNAPPPPADPNAPPPPPADPNAPPPPAVDPNAP 111
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
 805-890 2.94e-05

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: 47.20  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 805 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTlsaplarptsgrgPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSfgAPP 884
Cdd:NF040983   97 PPPPPPPPTPPPPPPPPPPPPPPSPPPPP-------------PPSPPPSPPPPTTTPPTRTTPSTTTPTPSMHPI--QPT 161


                  ....*.
gi 2462507684 885 QVPSRP 890
Cdd:NF040983  162 QLPSIP 167
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 803-890 4.41e-05

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 46.92  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 803 STP-APPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPF--PSSSDS 879
Cdd:PHA03264  261 SKGyEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDAdrPEGWPS 340

                          90
                  ....*....|....
gi 2462507684 880 FGA---PPQVPSRP 890
Cdd:PHA03264  341 LEAitfPPPTPATP 354
PHA03247 PHA03247
large tegument protein UL36; Provisional
 807-890 1.30e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  807 PPPVDDSWIQHSRRSPPPSPTTQRRPTL-SAPLARPTSGRGPAPAI--------PSPGPHSGAPPVPFRPG-PLPPFPSS 876
Cdd:PHA03247  2648 PPERPRDDPAPGRVSRPRRARRLGRAAQaSSPPQRPRRRAARPTVGsltsladpPPPPPTPEPAPHALVSAtPLPPGPAA 2727

                           90
                   ....*....|....*
gi 2462507684  877 S-DSFGAPPQVPSRP 890
Cdd:PHA03247  2728 ArQASPALPAAPAPP 2742
PHA03378 PHA03378
EBNA-3B; Provisional
 804-890 1.32e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.83  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 804 TPAPPPVddswIQHSRRSPPPSPTTQRRPTLSAPLA--RPTSGRGPAPAiPSPGPHSGAPPVPfRPGPLPPfPSSSDSFG 881
Cdd:PHA03378  702 TPMRPPA----APPGRAQRPAAATGRARPPAAAPGRarPPAAAPGRARP-PAAAPGRARPPAA-APGRARP-PAAAPGAP 774

                          90
                  ....*....|..
gi 2462507684 882 AP---PQVPSRP 890
Cdd:PHA03378  775 TPqppPQAPPAP 786
PHA03247 PHA03247
large tegument protein UL36; Provisional
 798-890 1.36e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  798 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTS-GRGPAPAIPSPGPHSG-----APPVPFRPGPLP 871
Cdd:PHA03247  2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSeSRESLPSPWDPADPPAavlapAAALPPAASPAG 2826

                           90
                   ....*....|....*....
gi 2462507684  872 PFPSSSDSFGAPPQVPSRP 890
Cdd:PHA03247  2827 PLPPPTSAQPTAPPPPPGP 2845
PHA03377 PHA03377
EBNA-3C; Provisional
 801-890 1.66e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 45.43  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  801 TVSTPAPP---PVDD---SWIQHSRRSPPP-SPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPV-------PFR 866
Cdd:PHA03377   525 SVTQPAKPhrkVQDGfqrSGRRQKRATPPKvSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPStgprqqaKCK 604

                           90       100
                   ....*....|....*....|....
gi 2462507684  867 PGPlppfPSSSDSFGAPPQvpSRP 890
Cdd:PHA03377   605 DGP----PASGPHEKQPPS--SAP 622
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 792-891 1.99e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 792 GIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTlSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLP 871
Cdd:PRK07764  661 DASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA-PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPV 739

                          90       100
                  ....*....|....*....|
gi 2462507684 872 PFPSSSDSFGAPPQVPSRPT 891
Cdd:PRK07764  740 PLPPEPDDPPDPAGAPAQPP 759
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
 819-889 2.42e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 44.73  E-value: 2.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462507684 819 RRSPPPSPTTQRRPTlSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSF-GAPPQVPSR 889
Cdd:PRK14965  379 RGAPAPPSAAWGAPT-PAAPAAPPPAAAPPVPPAAPARPAAARPAPAPAPPAAAAPPARSADpAAAASAGDR 449
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 798-891 2.88e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 798 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPtlsAPLARPTSGRGPAPAIPSPGP-HSGAPPVPFRPGPLPPFPSS 876
Cdd:PRK07764  401 AAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAP---APAPAPPSPAGNAPAGGAPSPpPAAAPSAQPAPAPAAAPEPT 477

                          90
                  ....*....|....*
gi 2462507684 877 SDSFGAPPQVPSRPT 891
Cdd:PRK07764  478 AAPAPAPPAAPAPAA 492
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 797-889 3.00e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 44.56  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 797 ISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAI-------PSPGPHSGAP-------P 862
Cdd:PHA03321  404 LATELFRTGVPSEHYEASLRLLSSRQPPGAPAPRRDNDPPPPPRARPGSTPACARraraqraRDAGPEYVDPlgalrrlP 483

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462507684 863 VPFRPGPLPPFPSSSDSF-----GAPPQVPSR 889
Cdd:PHA03321  484 AGAAPPPEPAAAPSPATYytrmgGGPPRLPPR 515
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 759-891 3.41e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 759 SSEDQNTLMEESAEQAQRRDEMLrmyqALKEALGII-----GDISTATVSTPAPPPVDDSwiQHSRRSPPPSPTTQRRPT 833
Cdd:pfam03154 150 SPQDNESDSDSSAQQQILQTQPP----VLQAQSGAAsppspPPPGTTQAATAGPTPSAPS--VPPQGSPATSQPPNQTQS 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 834 LSAPLARPTSG------RGPAP-------------------AIPSPGPHSGAPPVPFR--------PGPLPPFPSSSDSF 880
Cdd:pfam03154 224 TAAPHTLIQQTptlhpqRLPSPhpplqpmtqppppsqvspqPLPQPSLHGQMPPMPHSlqtgpshmQHPVPPQPFPLTPQ 303

                         170
                  ....*....|.
gi 2462507684 881 GAPPQVPSRPT 891
Cdd:pfam03154 304 SSQSQVPPGPS 314
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 781-891 3.44e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 44.42  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 781 LRMYQALKEALgiigdISTATVSTPAPPpvddswiqhsrRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGA 860
Cdd:PRK14950  349 LPLELAVIEAL-----LVPVPAPQPAKP-----------TAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPV 412

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462507684 861 PPVPFRPGPLPPFPSSSDSFGAPPQVPSRPT 891
Cdd:PRK14950  413 PPRPVAPPVPHTPESAPKLTRAAIPVDEKPK 443
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 799-890 4.42e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.93  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 799 TATVSTPAPPPVddswiQHSRRSPPPSPTTQRRPTlSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSD 878
Cdd:PRK14951  385 EAAAPAAAPVAQ-----AAAAPAPAAAPAAAASAP-AAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPE 458

                          90
                  ....*....|..
gi 2462507684 879 SFGAPPQVPSRP 890
Cdd:PRK14951  459 TVAIPVRVAPEP 470
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 794-891 4.44e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  794 IGDISTATVSTPAPPPVDDSwiqhsRRSPPPSP--------TTQRRPT----------LSAPLARPTSGRGPAPAI---P 852
Cdd:PHA03307   273 SGWNGPSSRPGPASSSSSPR-----ERSPSPSPsspgsgpaPSSPRASssssssressSSSTSSSSESSRGAAVSPgpsP 347

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462507684  853 SPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRPT 891
Cdd:PHA03307   348 SRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPT 386
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 822-890 8.38e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.13  E-value: 8.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462507684 822 PPPSpttQRRPTLSAPLARPTSGRG----PAPA-IPSPG-PHSGAPPVPFRPGpLPPFPSSSdsFGAPPQVPSRP 890
Cdd:PRK14959  398 PTPG---TQGPQGTAPAAGMTPSSAapatPAPSaAPSPRvPWDDAPPAPPRSG-IPPRPAPR--MPEASPVPGAP 466
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 799-890 8.86e-04

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: 40.83  E-value: 8.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 799 TATVSTPAPPPVDDSwiqhsrrSPPPSPTTQRRPTLSAPLARP---TSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPS 875
Cdd:cd21975    43 AKGPGPPGPAWKPDG-------ADSPGLVTAAPHLLAANVLAPlrgPSVEGSSLESGDADMGSDSDVAPASGAAASTSPE 115

                          90
                  ....*....|....*
gi 2462507684 876 SSDSFGAPPQVPSRP 890
Cdd:cd21975   116 SSSDAASSPSPLSLL 130
PHA03247 PHA03247
large tegument protein UL36; Provisional
 798-891 9.88e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 9.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  798 STATVSTPAPPPVDDSWIQhsRRSPPP-----SPTTQRRPTLSAPLARPTSGRGPA--------PAIPSPGPHSGAP-PV 863
Cdd:PHA03247  2762 TTAGPPAPAPPAAPAAGPP--RRLTRPavaslSESRESLPSPWDPADPPAAVLAPAaalppaasPAGPLPPPTSAQPtAP 2839

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2462507684  864 PFRPGPLPPFPSSSDSF------------GAPPQVPSRPT 891
Cdd:PHA03247  2840 PPPPGPPPPSLPLGGSVapggdvrrrppsRSPAAKPAAPA 2879
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 797-904 1.01e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  797 ISTATVSTPAPPPVDDSWIQHSRRSPPPSPT----TQRRPTLSAPLARPTSGRGPAPAIPSPGPH-----------SGAP 861
Cdd:PHA03307   195 PSTPPAAASPRPPRRSSPISASASSPAPAPGrsaaDDAGASSSDSSSSESSGCGWGPENECPLPRpapitlptriwEASG 274

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2462507684  862 PVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRAPPSVPRRPPPA 904
Cdd:PHA03307   275 WNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSS 317
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 805-872 1.03e-03

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


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 39.68  E-value: 1.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462507684 805 PAPPPVDDSWIQHSrrSPPPSPTTQRRPTLSAPlARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPP 872
Cdd:pfam12526  39 PPPPVGDPRPPVVD--TPPPVSAVWVLPPPSEP-AAPEPDLVPPVTGPAGPPSPLAPPAPAQKPPLPP 103
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
785-879 1.03e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 42.64  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 785 QALKEALG-------IIGDISTATVSTPAPPPVDDSwIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPH 857
Cdd:PRK14948  496 QAFAKVLGrsiklnlESQSGSASNTAKTPPPPQKSP-PPPAPTPPLPQPTATAPPPTPPPPPPTATQASSNAPAQIPADS 574

                          90       100
                  ....*....|....*....|..
gi 2462507684 858 SGAPPVPFRPGPLPPFPSSSDS 879
Cdd:PRK14948  575 SPPPPIPEEPTPSPTKDSSPEE 596
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 790-888 1.27e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 790 ALGIIGDISTATVSTPAPPPVddSWIQHSRRSPPPS---PTTQRRPTLSAPLAR--PTSGRGPAPAIPSPGPHSGAPPVP 864
Cdd:pfam03154 395 ALKPLSSLSTHHPPSAHPPPL--QLMPQSQQLPPPPaqpPVLTQSQSLPPPAAShpPTSGLHQVPSQSPFPQHPFVPGGP 472

                          90       100
                  ....*....|....*....|....*.
gi 2462507684 865 frPGPLPPF--PSSSDSFGAPPQVPS 888
Cdd:pfam03154 473 --PPITPPSgpPTSTSSAMPGIQPPS 496
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 805-890 1.29e-03

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


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 40.24  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 805 PAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPApaIPSPGPHSGAPPVPfrpgPLPPFPSSSdSFGAPP 884
Cdd:pfam06346   1 PPPPPLPGDSSTIPLPPGACIPTPPPLPGGGGPPPPPPLPGSAA--IPPPPPLPGGTSIP----PPPPLPGAA-SIPPPP 73


                  ....*.
gi 2462507684 885 QVPSRP 890
Cdd:pfam06346  74 PLPGST 79
PHA03378 PHA03378
EBNA-3B; Provisional
 759-890 1.33e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.75  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 759 SSEDQNTLMEESAEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPL 838
Cdd:PHA03378  605 TPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTM 684

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462507684 839 ARPTSGRG---PAPAIPSPGPHSGAPPVPFRP-----GPLPPfPSSSDSFGAPPQV---PSRP 890
Cdd:PHA03378  685 LPIQWAPGtmqPPPRAPTPMRPPAAPPGRAQRpaaatGRARP-PAAAPGRARPPAAapgRARP 746
PHA03247 PHA03247
large tegument protein UL36; Provisional
 798-888 1.33e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  798 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLS--APLAR-PTSGrgPAPAIPSPGPHsgaPPVpfRPGPLPPFP 874
Cdd:PHA03247  2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVApgGDVRRrPPSR--SPAAKPAAPAR---PPV--RRLARPAVS 2892

                           90
                   ....*....|....
gi 2462507684  875 SSSDSFGAPPQVPS 888
Cdd:PHA03247  2893 RSTESFALPPDQPE 2906
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
798-889 1.46e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 798 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRptlSAPLARPTSGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSS 877
Cdd:PRK12323  404 AAPAAAPAAAAAARAVAAAPARRSPAPEALAAAR---QASARGPGGAPAPAPA-PAAAPAAAARPAAAGPRPVAAAAAAA 479

                          90
                  ....*....|..
gi 2462507684 878 DSFGAPPQVPSR 889
Cdd:PRK12323  480 PARAAPAAAPAP 491
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 774-888 1.92e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 774 AQRRDEMLRmyQALKEALGIigdisTATVS-TPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLS-APLARPTSGRGPAPAI 851
Cdd:PRK07764  563 SPGNAEVLV--TALAEELGG-----DWQVEaVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPaAPAAPAAPAPAGAAAA 635

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462507684 852 PSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPS 888
Cdd:PRK07764  636 PAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAK 672
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 759-890 2.15e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.02  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 759 SSEDQNTLMEESAEQAQRRDEmlrmyQALKEALGIIGDISTATVSTPAPPPVDDSwiqHSRRSPPPSPTTQRRPTLSAPL 838
Cdd:pfam15240  24 SQEDSPSLISEEEGQSQQGGQ-----GPQGPPPGGFPPQPPASDDPPGPPPPGGP---QQPPPQGGKQKPQGPPPQGGPR 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462507684 839 ARPTSGRGPAPaipSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRP 890
Cdd:pfam15240  96 PPPGKPQGPPP---QGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPP 144
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 799-891 2.16e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 799 TATVSTPAPPPVDDswiQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAiPSPGPHSGAPPVPfRPGPLPPFPSSSD 878
Cdd:PRK07764  417 PAAAAAPAPAAAPQ---PAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ-PAPAPAAAPEPTA-APAPAPPAAPAPA 491

                          90
                  ....*....|...
gi 2462507684 879 sfgAPPQVPSRPT 891
Cdd:PRK07764  492 ---AAPAAPAAPA 501
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 805-886 2.34e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 805 PAPPPVDDSWIQHSRRSPPPSPTT------QRRPTLSAPLARPTSGR----GPAPAIPSPGPHSGAPPVPfrpgPLPPFP 874
Cdd:pfam03154 292 PVPPQPFPLTPQSSQSQVPPGPSPaapgqsQQRIHTPPSQSQLQSQQppreQPLPPAPLSMPHIKPPPTT----PIPQLP 367

                          90
                  ....*....|..
gi 2462507684 875 SSSdSFGAPPQV 886
Cdd:pfam03154 368 NPQ-SHKHPPHL 378
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 803-890 2.76e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 40.95  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 803 STPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPG--PHSGAPPVPFRPGPLPPFPSSSDS- 879
Cdd:pfam15279 136 LPPPPLPPKKGRRHRPGLHPPLGRPPGSPPMSMTPRGLLGKPQQHPPPSPLPAfmEPSSMPPPFLRPPPSIPQPNSPLSn 215

                          90
                  ....*....|....*
gi 2462507684 880 ----FGAPPQVPSRP 890
Cdd:pfam15279 216 pmlpGIGPPPKPPRN 230
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 800-890 2.93e-03

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 41.14  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 800 ATVSTPAPPPVDDSwiQHSRRSPPPSPTTQRRPTLSAPlarptsGRGPAPAiPSPGPHSGAPPVPFRPGPLPPFPSSSDS 879
Cdd:NF041121   20 APPSPEGPAPTAAS--QPATPPPPAAPPSPPGDPPEPP------APEPAPL-PAPYPGSLAPPPPPPPGPAGAAPGAALP 90

                          90
                  ....*....|..
gi 2462507684 880 FGAP-PQVPSRP 890
Cdd:NF041121   91 VRVPaPPALPNP 102
PHA03247 PHA03247
large tegument protein UL36; Provisional
 786-890 3.30e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  786 ALKEALGIIGDISTATVSTPAPPPVDDSWI---------QHSRRSPPPSPTTQ-RRPTLSAPLARPTSGRGPAPAIPSpG 855
Cdd:PHA03247  2687 AARPTVGSLTSLADPPPPPPTPEPAPHALVsatplppgpAAARQASPALPAAPaPPAVPAGPATPGGPARPARPPTTA-G 2765

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2462507684  856 PHSGAPPV-----PFRPGPLPPFPSSSDSFGAPPQvPSRP 890
Cdd:PHA03247  2766 PPAPAPPAapaagPPRRLTRPAVASLSESRESLPS-PWDP 2804
DUF4639 pfam15479
Domain of unknown function (DUF4639); This family of proteins is found in eukaryotes. Proteins ...
 826-891 3.59e-03

Domain of unknown function (DUF4639); This family of proteins is found in eukaryotes. Proteins in this family are typically between 161 and 601 amino acids in length.


Pssm-ID: 464739  Cd Length: 580  Bit Score: 40.95  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 826 PTTQRRPtLSAPLARPTSGRGPAPAIP-SPGPHSGAPP---------VPFR---PGPLPPFPS-----SSDSFG------ 881
Cdd:pfam15479 361 PDSEARP-LEAYRGRQRSEKTKARAGPqAPGPGVRVSPaaffplppgVPFRalgPGPGLQFPTlnlglPSPSFGsklpfp 439

                          90       100
                  ....*....|....*....|.
gi 2462507684 882 -----------APPQVPSRPT 891
Cdd:pfam15479 440 spglrflathpVLPDVARSPS 460
PHA03379 PHA03379
EBNA-3A; Provisional
 798-887 3.69e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.20  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 798 STATVSTPAPPPVDDSWIQ--HSRRSPPPSPTTQRRPTLSAPLAR-------PTSGRG---PAPAI---------PSPGP 856
Cdd:PHA03379  436 SHGSAQVPEPPPVHDLEPGplHDQHSMAPCPVAQLPPGPLQDLEPgdqlpgvVQDGRPacaPVPAPagpivrpweASLSQ 515

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462507684 857 HSGAPPVPFRPGPLP----PFPSSSDSFGAPPQVP 887
Cdd:PHA03379  516 VPGVAFAPVMPQPMPvepvPVPTVALERPVCPAPP 550
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
 526-563 3.95e-03

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: 38.18  E-value: 3.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462507684 526 VIRKGWLTISNIGIMKGGS---KGYWFVLTAESLSWYKDDE 563
Cdd:cd13297    13 VIERGWLYKEGGKGGARGNltkKKRWFVLTGNSLDYYKSSE 53
SSDP pfam04503
Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA ...
 780-879 4.13e-03

Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA binding proteins with specificity to a pyrimidine-rich element found in the promoter region of the alpha2(I) collagen gene.


Pssm-ID: 461334 [Multi-domain]  Cd Length: 293  Bit Score: 40.32  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 780 MLRMYQALKEALGIIGdISTATVSTPAPPPvddswiqHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSG 859
Cdd:pfam04503 128 MQRMNPPRGPGMGPMG-PQSYGPGMRGPPP-------NSTDGPGGMPPMNMGPGGRRPWPQPNASNPLPYSSSSPGSYGG 199

                          90       100
                  ....*....|....*....|
gi 2462507684 860 APPVPFRPGPLPPFPSSSDS 879
Cdd:pfam04503 200 PPGGGGPPGPTPIMPSPQDS 219
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 798-890 4.57e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 798 STATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSG-----RGPAPAIPSPGPHSGAPPVPfRPGPLPP 872
Cdd:PRK07764  642 APAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAapaapAGAAPAQPAPAPAATPPAGQ-ADDPAAQ 720

                          90
                  ....*....|....*...
gi 2462507684 873 FPSSSDSFGAPPQVPSRP 890
Cdd:PRK07764  721 PPQAAQGASAPSPAADDP 738
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 822-888 5.89e-03

Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated lipase, where is O-glycosylated. This region is composed of biased amino acid composition that is likely to be disordered. The region contains many repeats of an approximately 11 residue degenerate repeat.


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 37.01  E-value: 5.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 822 PPPSPTT-QRRPTLS--APLARPTSGRGPAPAIPSPGphSGAPPVPfrpgplppfPSSSdsFGAPPQVPS 888
Cdd:pfam16058   1 PSSSITEpPRDPSGSygEPPRAPSSSYTEPQRDPSSS--ITEPPAD---------PSSS--YTEPPRDPS 57
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 803-891 6.74e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 6.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  803 STPAPPPVDDSWIQHSRRSPPPspTTQRRPTLSAPLARPTSGRGPAPAiPSPGPHsgAPPVPFRPGPLPPFPSSSDSFGA 882
Cdd:PHA03307    67 PPTGPPPGPGTEAPANESRSTP--TWSLSTLAPASPAREGSPTPPGPS-SPDPPP--PTPPPASPPPSPAPDLSEMLRPV 141


                   ....*....
gi 2462507684  883 PPQVPSRPT 891
Cdd:PHA03307   142 GSPGPPPAA 150
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 800-891 6.76e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 800 ATVSTPAPPPvddswiqhsRRSPPPSPTtqrrptLSAPLARPTSGRGPAPAI---PSPGPHSGAPPVPfRPGPLPPFPSS 876
Cdd:PRK07764  391 AGAPAAAAPS---------AAAAAPAAA------PAPAAAAPAAAAAPAPAAapqPAPAPAPAPAPPS-PAGNAPAGGAP 454

                          90
                  ....*....|....*
gi 2462507684 877 SDSFGAPPQVPSRPT 891
Cdd:PRK07764  455 SPPPAAAPSAQPAPA 469
PHA03377 PHA03377
EBNA-3C; Provisional
 814-890 7.91e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.04  E-value: 7.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  814 WIQHSRRSPPPSPTTQRRPTLSaPLARPTSGrgPAPAIPSPGPHSGAPPVPFRP----GPLPPFPSSSDSFGAP------ 883
Cdd:PHA03377   813 WSQYPGHGHPQGPWAPRPPHLP-PQWDGSAG--HGQDQVSQFPHLQSETGPPRLqlsqVPQLPYSQTLVSSSAPswsspq 889


                   ....*..
gi 2462507684  884 PQVPSRP 890
Cdd:PHA03377   890 PRAPIRP 896
PHA03247 PHA03247
large tegument protein UL36; Provisional
 800-889 8.08e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 8.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684  800 ATVSTPAPPPVDdSWIQ--------HSRRSPPPSPTTQRRPTlsAPLARPTSG---RGPAPAIPSPGPHSGAPPVPFRP- 867
Cdd:PHA03247  2523 EPVGEPVHPRML-TWIRgleelasdDAGDPPPPLPPAAPPAA--PDRSVPPPRpapRPSEPAVTSRARRPDAPPQSARPr 2599

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462507684  868 ----------GPLPPFPSSSDSFGAPPQVPSR 889
Cdd:PHA03247  2600 apvddrgdprGPAPPSPLPPDTHAPDPPPPSP 2631
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
771-888 8.87e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507684 771 AEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPVDdswiqhsrRSPPPSPTTQRRP-TLSAPLARPTSGRGPAP 849
Cdd:PRK12323  420 AAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAA--------AARPAAAGPRPVAaAAAAAPARAAPAAAPAP 491

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462507684 850 AIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPS 888
Cdd:PRK12323  492 ADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPA 530
 
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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