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Conserved domains on  [gi|1720430187|ref|XP_030099906|]
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dynamin-2 isoform X17 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 57-344 1.11e-145

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: 425.78  E-value: 1.11e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  57 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 136
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 137 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 216
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 217 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 296
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1720430187 297 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQR 344
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 356-467 1.47e-72

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: 230.29  E-value: 1.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 356 NQVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVY 435
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720430187 436 KDLRQIELACDSQEDVDSWKASFLRAGVYPEK 467
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-87 3.29e-50

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member smart00053:

Pssm-ID: 476819  Cd Length: 240  Bit Score: 175.45  E-value: 3.29e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187    1 MILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRS 80
Cdd:smart00053 154 MIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRS 233


                   ....*..
gi 1720430187   81 QKDIEGK 87
Cdd:smart00053 234 QKDIEGK 240
GED pfam02212
Dynamin GTPase effector domain;
487-577 2.72e-30

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 114.15  E-value: 2.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 487 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 566
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1720430187 567 LKEALNIIGDI 577
Cdd:pfam02212  81 LKQAREILSEV 91
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 578-671 6.69e-07

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: 47.80  E-value: 6.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 578 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 655
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 1720430187 656 VFANNDP---FSAPPQIPS 671
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 57-344 1.11e-145

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: 425.78  E-value: 1.11e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  57 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 136
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 137 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 216
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 217 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 296
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1720430187 297 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQR 344
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 356-467 1.47e-72

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: 230.29  E-value: 1.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 356 NQVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVY 435
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720430187 436 KDLRQIELACDSQEDVDSWKASFLRAGVYPEK 467
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 1-136 1.64e-61

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: 207.10  E-value: 1.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187   1 MILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVV 77
Cdd:cd08771   139 MVKSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVV 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  78 NRSQKDIEGKKDIRAALAAERKFFLSHPAYRH-MADRMGTPHLQKTLNQQLTNHIRESLP 136
Cdd:cd08771   219 NRSQKDIDSGKSIEEALEAEEEFFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 1-87 3.29e-50

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: 175.45  E-value: 3.29e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187    1 MILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRS 80
Cdd:smart00053 154 MIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRS 233


                   ....*..
gi 1720430187   81 QKDIEGK 87
Cdd:smart00053 234 QKDIEGK 240
GED pfam02212
Dynamin GTPase effector domain;
487-577 2.72e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 114.15  E-value: 2.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 487 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 566
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1720430187 567 LKEALNIIGDI 577
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
486-577 1.63e-25

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 100.77  E-value: 1.63e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  486 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 565
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1720430187  566 ALKEALNIIGDI 577
Cdd:smart00302  81 LLKKARQIIAAV 92
Dynamin_N pfam00350
Dynamin family;
1-49 1.33e-13

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 69.18  E-value: 1.33e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720430187   1 MILQFIsRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKL 49
Cdd:pfam00350 121 LTKEYI-KPADIILAVTPANVDLSTSEALFLAREVDPNGKRTIGVLTKA 168
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 358-461 1.27e-10

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: 58.71  E-value: 1.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  358 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 433
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1720430187  434 VYKDLRQIELACDSQEDVDSWKASFLRA 461
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 358-461 2.75e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.88  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 358 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 433
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1720430187 434 VykdlRQIELACDSQEDVDSWKASFLRA 461
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 578-671 6.69e-07

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: 47.80  E-value: 6.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 578 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 655
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 1720430187 656 VFANNDP---FSAPPQIPS 671
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 575-674 5.26e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 5.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  575 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 654
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100
                   ....*....|....*....|
gi 1720430187  655 SVFANNDPFSAPPQIPSRPA 674
Cdd:PHA03247  2806 DPPAAVLAPAAALPPAASPA 2825
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 57-344 1.11e-145

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: 425.78  E-value: 1.11e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  57 DARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLP 136
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 137 TLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSgDQVDTLELSGGARINRIFHERFPFEL 216
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGE-SEISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 217 VKMEFDEKDLRREISYAIKNIHGVRTGLFTPDMAFEAIVKKQLVKLKEPSLKCVDLVVSELATVIKKCAEKLSSYPRLRE 296
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTPELKRFPNLRE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1720430187 297 ETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQR 344
Cdd:pfam01031 240 RIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
PH_dynamin cd01256
Dynamin pleckstrin homology (PH) domain; Dynamin is a GTPase that regulates endocytic vesicle ...
 356-467 1.47e-72

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: 230.29  E-value: 1.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 356 NQVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVY 435
Cdd:cd01256     1 NQVIRKGWLTINNIGFMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDGLKLRDVEKGFMSRKHIFALFNTDQRNVY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720430187 436 KDLRQIELACDSQEDVDSWKASFLRAGVYPEK 467
Cdd:cd01256    81 KDYKQLELSCETQEEVDSWKASFLRAGVYPEK 112
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 1-136 1.64e-61

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: 207.10  E-value: 1.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187   1 MILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVL---ENKLLPLRRGYIGVV 77
Cdd:cd08771   139 MVKSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVV 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  78 NRSQKDIEGKKDIRAALAAERKFFLSHPAYRH-MADRMGTPHLQKTLNQQLTNHIRESLP 136
Cdd:cd08771   219 NRSQKDIDSGKSIEEALEAEEEFFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 1-87 3.29e-50

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: 175.45  E-value: 3.29e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187    1 MILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRS 80
Cdd:smart00053 154 MIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRS 233


                   ....*..
gi 1720430187   81 QKDIEGK 87
Cdd:smart00053 234 QKDIEGK 240
GED pfam02212
Dynamin GTPase effector domain;
487-577 2.72e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 114.15  E-value: 2.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 487 LERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHA 566
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 1720430187 567 LKEALNIIGDI 577
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
486-577 1.63e-25

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 100.77  E-value: 1.63e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  486 QLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYH 565
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 1720430187  566 ALKEALNIIGDI 577
Cdd:smart00302  81 LLKKARQIIAAV 92
Dynamin_N pfam00350
Dynamin family;
1-49 1.33e-13

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 69.18  E-value: 1.33e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720430187   1 MILQFIsRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKL 49
Cdd:pfam00350 121 LTKEYI-KPADIILAVTPANVDLSTSEALFLAREVDPNGKRTIGVLTKA 168
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 358-461 1.27e-10

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: 58.71  E-value: 1.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  358 VIRRGWLTINNiSLMKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIfnteqrn 433
Cdd:smart00233   1 VIKEGWLYKKS-GGGKKSWKKRYFVLFNSTLLYYkskKDKKSYKPKGSIDLSGCTVREAPDPDSSKkPHCFEI------- 72

                           90       100
                   ....*....|....*....|....*...
gi 1720430187  434 VYKDLRQIELACDSQEDVDSWKASFLRA 461
Cdd:smart00233  73 KTSDRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 358-461 2.75e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.88  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 358 VIRRGWLTINNISLmKGGSKEYWFVLTAESLSWY---KDEEEKEKKYMLPLDNLKIRDVEKGFMSN-KHVFAIFNTEQRN 433
Cdd:pfam00169   1 VVKEGWLLKKGGGK-KKSWKKRYFVLFDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDSPKrKFCFELRTGERTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1720430187 434 VykdlRQIELACDSQEDVDSWKASFLRA 461
Cdd:pfam00169  80 K----RTYLLQAESEEERKDWIKAIQSA 103
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 360-454 1.94e-07

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


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 49.46  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 360 RRGWLTINNISLMKGGsKEYWFVLTAESLSWYKDEEEKEKKY--MLPLDN-LKIRDVEKGfmSNKHVFAIFNTEQRNVYk 436
Cdd:cd00821     1 KEGYLLKRGGGGLKSW-KKRWFVLFEGVLLYYKSKKDSSYKPkgSIPLSGiLEVEEVSPK--ERPHCFELVTPDGRTYY- 76

                          90
                  ....*....|....*...
gi 1720430187 437 dlrqieLACDSQEDVDSW 454
Cdd:cd00821    77 ------LQADSEEERQEW 88
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 578-671 6.69e-07

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: 47.80  E-value: 6.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 578 STSTVSTPVPPPVDDTWLQ-NTSGHSPTPQRRPVSSVHPPGRPPAVR-GPTPGPPlipmpvgaTSSFSAPpiPSRPGPQS 655
Cdd:pfam16058   2 SSSITEPPRDPSGSYGEPPrAPSSSYTEPQRDPSSSITEPPADPSSSyTEPPRDP--------SGSYTEP--QRDPSSSS 71

                          90
                  ....*....|....*....
gi 1720430187 656 VFANNDP---FSAPPQIPS 671
Cdd:pfam16058  72 TEPQRDPsssITEPPRDPS 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 575-674 5.26e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 5.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  575 GDISTSTVSTPVPPPVDDTwlQNTSGHSPTPQRRPVSSVHPPGRPPAVRgPTPGPPLIPMPVGATSSFSAPPIPSRPGPQ 654
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG--PATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPA 2805

                           90       100
                   ....*....|....*....|
gi 1720430187  655 SVFANNDPFSAPPQIPSRPA 674
Cdd:PHA03247  2806 DPPAAVLAPAAALPPAASPA 2825
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
 358-454 8.82e-05

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


Pssm-ID: 269954  Cd Length: 119  Bit Score: 42.69  E-value: 8.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 358 VIRRGWLtinnisLMKGGS----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKgfMSNKHVFAIFNTEQRN 433
Cdd:cd01252     3 PDREGWL------LKLGGRvkswKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSVREVED--KKKPFCFELYSPSNGQ 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720430187 434 VYK------DLRQIE-------LACDSQEDVDSW 454
Cdd:cd01252    75 VIKacktdsDGKVVEgnhtvyrISAASEEERDEW 108
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 601-662 8.88e-05

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 44.34  E-value: 8.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430187 601 HSPTPQRRPVSSVHPPgrppavrgptPGPPLIPMPVGATSSFSAPPIPSRPG----------PQSVFANNDP 662
Cdd:PHA03418   40 HHPNPQEDPDKNPSPP----------PDPPLTPRPPAQPNGHNKPPVTKQPGgegteedhqaPLAADADDDP 101
PHA03321 PHA03321
tegument protein VP11/12; Provisional
 602-675 4.23e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 43.79  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 602 SPTPQRRPVSSVHPPGRPPAVRGPTPGPP-------LIPMPVGAtssfSAPPIPSRPGPQSVFANNDPfSAPPQIPSRPA 674
Cdd:PHA03321  443 PPPPRARPGSTPACARRARAQRARDAGPEyvdplgaLRRLPAGA----APPPEPAAAPSPATYYTRMG-GGPPRLPPRNR 517


                  .
gi 1720430187 675 R 675
Cdd:PHA03321  518 A 518
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 576-675 4.61e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 4.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  576 DISTSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLipmpvGATSSFSAPPIPSRPGPQS 655
Cdd:PHA03307   177 SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDA-----GASSSDSSSSESSGCGWGP 251

                           90       100
                   ....*....|....*....|
gi 1720430187  656 VFANNDPFSAPPQIPSRPAR 675
Cdd:PHA03307   252 ENECPLPRPAPITLPTRIWE 271
PHA03247 PHA03247
large tegument protein UL36; Provisional
 585-655 5.08e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 5.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  585 PVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPP----------------LIPMPVGATSSFSAPPIP 648
Cdd:PHA03247  2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgagepsgavpqpwlgaLVPGRVAVPRFRVPQPAP 2984


                   ....*..
gi 1720430187  649 SRPGPQS 655
Cdd:PHA03247  2985 SREAPAS 2991
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 585-673 5.32e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 41.18  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 585 PVPPPVDDtwlqntsGHSPTPQRRPVSSVHPPGR-------PPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVF 657
Cdd:pfam15240  56 PQPPASDD-------PPGPPPPGGPQQPPPQGGKqkpqgppPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQG 128

                          90
                  ....*....|....*.
gi 1720430187 658 ANNDPFSAPPQIPSRP 673
Cdd:pfam15240 129 GGPPPQGGNQQGPPPP 144
PHA03247 PHA03247
large tegument protein UL36; Provisional
 578-674 8.09e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 8.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  578 STSTVSTPVPPP--VDDTWLQNTSGHSPT------------------PQRRPVSSVHPPGRPPAVRGPTPGPPlipmpvG 637
Cdd:PHA03247  2820 PAASPAGPLPPPtsAQPTAPPPPPGPPPPslplggsvapggdvrrrpPSRSPAAKPAAPARPPVRRLARPAVS------R 2893

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1720430187  638 ATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPSRPA 674
Cdd:PHA03247  2894 STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
 547-653 1.08e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 42.13  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 547 MEESAEQAQRRDDMLRMYHALKEALNIIGDI-STSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPP---GRPPAV 622
Cdd:PRK14963  315 LDEQMERFARRSDALSLELALLHALLALGGApSEGVAAVAPPAPAPADLTQRLNRLEKEVRSLRSAPTAAAtaaGAPLPD 394

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720430187 623 RGPTPGPPliPMPVGATSSFSAPPIPSRPGP 653
Cdd:PRK14963  395 FDPRPRGP--PAPEPARSAEAPPLVAPAAAP 423
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
585-674 1.09e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 585 PVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPliPMPVGATssfsAPPIPSrPGPQSVFANNDPFS 664
Cdd:PRK12323  410 PAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPA--AAPAAAA----RPAAAG-PRPVAAAAAAAPAR 482

                          90
                  ....*....|
gi 1720430187 665 APPQIPSRPA 674
Cdd:PRK12323  483 AAPAAAPAPA 492
PHA03247 PHA03247
large tegument protein UL36; Provisional
 603-674 1.49e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  603 PTPQRR-------PVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSsfSAPPIPSRPGPQSVFANND-PFSAPPQIPSRPA 674
Cdd:PHA03247   381 PTRKRRsarhaatPFARGPGGDDQTRPAAPVPASVPTPAPTPVPA--SAPPPPATPLPSAEPGSDDgPAPPPERQPPAPA 458
PHA03247 PHA03247
large tegument protein UL36; Provisional
 603-674 1.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  603 PTPQRRPVSSVHPPGRPPAVRGPTPGPPLI-----PMPVGATSSFSAPPIPSRPGPQSVFANNDP--------------- 662
Cdd:PHA03247  2592 PPQSARPRAPVDDRGDPRGPAPPSPLPPDThapdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvsrprrarrlg 2671

                           90
                   ....*....|....*.
gi 1720430187  663 ----FSAPPQIPSRPA 674
Cdd:PHA03247  2672 raaqASSPPQRPRRRA 2687
PHA03247 PHA03247
large tegument protein UL36; Provisional
 604-674 1.78e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430187  604 TPQRRPvssvHPPGRPPAV-------RGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPfsAPPQIPSRPA 674
Cdd:PHA03247  2678 SPPQRP----RRRAARPTVgsltslaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP--APPAVPAGPA 2749
PHA03378 PHA03378
EBNA-3B; Provisional
 584-673 2.98e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.82  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 584 TPVPPPvddtwlqntsGHSPTPQRRPVSSVH----PPGRPPAVRGPTPGPPLIPMPVGATSSFSAP---PIPSRPgPQSV 656
Cdd:PHA03378  702 TPMRPP----------AAPPGRAQRPAAATGrarpPAAAPGRARPPAAAPGRARPPAAAPGRARPPaaaPGRARP-PAAA 770

                          90
                  ....*....|....*..
gi 1720430187 657 FANNDPfSAPPQIPSRP 673
Cdd:PHA03378  771 PGAPTP-QPPPQAPPAP 786
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 578-674 3.06e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 578 STSTVSTPVPPPVDDTWLQNTSGHSP----------TPQRRPvsSVHPPGR------PPAVRGPTPGPPLI---PMPVGA 638
Cdd:pfam03154 202 SAPSVPPQGSPATSQPPNQTQSTAAPhtliqqtptlHPQRLP--SPHPPLQpmtqppPPSQVSPQPLPQPSlhgQMPPMP 279

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720430187 639 TSSFSAPPIPSRPGPQSVFANNdPFSAPPQIPSRPA 674
Cdd:pfam03154 280 HSLQTGPSHMQHPVPPQPFPLT-PQSSQSQVPPGPS 314
PHA03379 PHA03379
EBNA-3A; Provisional
 578-669 3.18e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 40.81  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 578 STSTVSTPVPPPVDDTW---LQNTSGHSPTP----QRRPVSSVHPPGRPPAV-RGPTPGPPLIPMPVG------------ 637
Cdd:PHA03379  436 SHGSAQVPEPPPVHDLEpgpLHDQHSMAPCPvaqlPPGPLQDLEPGDQLPGVvQDGRPACAPVPAPAGpivrpweaslsq 515

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720430187 638 ----ATSSFSAPPIPSRPGPQSVFANNDPFS-APPQI 669
Cdd:PHA03379  516 vpgvAFAPVMPQPMPVEPVPVPTVALERPVCpAPPLI 552
PHA03247 PHA03247
large tegument protein UL36; Provisional
 577-673 3.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  577 ISTSTVSTPVPP-PVDDTWLQNTSGHSPTPQRRPVSSVHPPGRP-PAVRGPTPGPPLIPMPVG--------------ATS 640
Cdd:PHA03247  2791 LSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAqPTAPPPPPGPPPPSLPLGgsvapggdvrrrppSRS 2870

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1720430187  641 SFSAPPIPSRPGPQSVFA-----NNDPFSAPPQIPSRP 673
Cdd:PHA03247  2871 PAAKPAAPARPPVRRLARpavsrSTESFALPPDQPERP 2908
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 583-674 4.10e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 4.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  583 STPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPM--------------PVGATSSFSAPPIP 648
Cdd:PHA03307    86 STPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMlrpvgspgpppaasPPAAGASPAAVASD 165

                           90       100
                   ....*....|....*....|....*..
gi 1720430187  649 SRPGPQ-SVFANNDPFSAPPqiPSRPA 674
Cdd:PHA03307   166 AASSRQaALPLSSPEETARA--PSSPP 190
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 582-673 4.35e-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: 38.31  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 582 VSTPVPPPvddtwLQNTSGHSPTPQRRPVSSVHPPGR---------PPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPG 652
Cdd:pfam06346  31 GGPPPPPP-----LPGSAAIPPPPPLPGGTSIPPPPPlpgaasippPPPLPGSTGIPPPPPLPGGAGIPPPPPPLPGGAG 105

                          90       100
                  ....*....|....*....|....
gi 1720430187 653 ---PQSVFANNDPFSAPPQIPSRP 673
Cdd:pfam06346 106 vppPPPPLPGGPGIPPPPPFPGGP 129
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 358-454 4.98e-03

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


Pssm-ID: 270068  Cd Length: 104  Bit Score: 37.25  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 358 VIRRGWLTinnislMKGGS-----KEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGF-MSNKHVFAIFNTEQ 431
Cdd:cd13248     7 VVMSGWLH------KQGGSglknwRKRWFVLKDNCLYYYKDPEEEKALGSILLPSYTISPAPPSDeISRKFAFKAEHANM 80

                          90       100
                  ....*....|....*....|...
gi 1720430187 432 RNVYkdlrqieLACDSQEDVDSW 454
Cdd:cd13248    81 RTYY-------FAADTAEEMEQW 96
DUF4813 pfam16072
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ...
 575-674 5.27e-03

Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.


Pssm-ID: 435117 [Multi-domain]  Cd Length: 288  Bit Score: 39.36  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 575 GDISTSTVSTpvpppvdDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGP-------PLIPM-PVGATSSFSA-- 644
Cdd:pfam16072 147 GSVTTTSAGS-------GTTVINAGGQQPAAPAAPAYPVAPAAYPAQAPAAAPAPapgapqtPLAPLnPVAAAPAAAAga 219

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720430187 645 --PPIPSRPGPQSvfanndpfSAPPqiPSRPA 674
Cdd:pfam16072 220 aaAPVVAAAAPAA--------AAPP--PPAPA 241
PHA03247 PHA03247
large tegument protein UL36; Provisional
 578-674 5.49e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 5.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187  578 STSTVSTPVPPPvddtwlqntsghsPTPQRRP---VSSVHPPGRPPAVRGPTPGPPLIPMPV---------GATSSFSAP 645
Cdd:PHA03247  2694 SLTSLADPPPPP-------------PTPEPAPhalVSATPLPPGPAAARQASPALPAAPAPPavpagpatpGGPARPARP 2760

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720430187  646 PI---PSRPGPQSvfannDPFSAPPQIPSRPA 674
Cdd:PHA03247  2761 PTtagPPAPAPPA-----APAAGPPRRLTRPA 2787
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
 355-391 6.34e-03

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


Pssm-ID: 275402  Cd Length: 116  Bit Score: 37.22  E-value: 6.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720430187 355 PNQVIRRGWLTInnISLMKGGSKEYWFVLTAESLSWY 391
Cdd:cd13215    18 SGAVIKSGYLSK--RSKRTLRYTRYWFVLKGDTLSWY 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 598-674 6.45e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 6.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720430187  598 TSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPsrPGPQSVFANNDPFSAPPQIPSRPA 674
Cdd:PHA03247   399 PGGDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPP--PERQPPAPATEPAPDDPDDATRKA 473
PHA01929 PHA01929
putative scaffolding protein
 579-674 6.81e-03

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 39.27  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 579 TSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGP----TPGPPLIPMPVGATSSFSAPPIPSRPGPQ 654
Cdd:PHA01929    1 TTQNEQQLPPGLAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAPqqlaIPTQQPQPVPTSAMTPHVVQQAPAQPAPA 80

                          90       100
                  ....*....|....*....|
gi 1720430187 655 SVFANNDPFSAPPQIPSRPA 674
Cdd:PHA01929   81 APPAAGAALPEALEVPPPPA 100
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 573-682 7.41e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 573 IIGDISTSTVSTPVPPPVDDTWL-QNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPG--PPLIPMPVGATSSFSAPPIPS 649
Cdd:PRK07764  662 ASDGGDGWPAKAGGAAPAAPPPApAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAaqPPQAAQGASAPSPAADDPVPL 741

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720430187 650 RPGPQSVFANNDPFSAPPQIPSRPARIPPGIPP 682
Cdd:PRK07764  742 PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 579-673 9.35e-03

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 38.43  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430187 579 TSTVSTPVP--PPvddtwlQNTSGHSPTPQRRPVSSVhPPGRPPAVRGPTPgpPLIPMPVGATSSFsaPPIPSRPGPQSV 656
Cdd:pfam15822  15 TSAVSNPKPgqPP------QGWPGSNPWNNPSAPPAV-PSGLPPSTAPSTV--PFGPAPTGMYPSI--PLTGPSPGPPAP 83

                          90
                  ....*....|....*..
gi 1720430187 657 FANNDPFSAPPQIPSRP 673
Cdd:pfam15822  84 FPPSGPSCPPPGGPYPA 100
 
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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