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Conserved domains on  [gi|350610879|pdb|3ZYS|E]
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Chain E, INTERFERON-INDUCED GTP-BINDING PROTEIN MX1

Protein Classification

dynamin-like protein( domain architecture ID 10171956)

dynamin-like protein is a GTPase responsible for endocytosis in the eukaryotic cell; similar to Homo sapiens interferon-induced GTP-binding protein Mx2, which is an interferon-induced dynamin-like GTPase with potent antiviral activity against human immunodeficiency virus type 1 (HIV-1)

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 ...
259-546 4.45e-120

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: 359.14  E-value: 4.45e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        259 KVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFENHPYFRDLleEGKATVPCLAEKLTSELITHICKS 338
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLL--ADKCGTPYLAKKLNQILVNHIRKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        339 LPLLENQIKETHQRITEELQKYGVDIPEDENEKMFFLIDKVNAFNQDITALMQGEETVGEEDIRLFTRLRHEFHKWSTII 418
Cdd:pfam01031  79 LPDLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEISTNELSGGARIRYIFNEIFPKS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        419 ENNFQEGHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLhtvtDMVRLAFTDVSIK---NFEEF 495
Cdd:pfam01031 159 LEKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCV----ELVYEELERIIHKctpELKRF 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
3ZYS_E        496 FNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQ-IVYCQDQVYRGALQKVR 546
Cdd:pfam01031 235 PNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELaYINTNHPDFIGGLNAVR 286
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
68-340 1.95e-119

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: 356.94  E-value: 1.95e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E       68 LALPAIAVIGDQSSGKSSVLEALSGV-ALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEI----EISDASEVEKE 142
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRdFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHlkskEFTDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E      143 INKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVD 222
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E      223 IATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTED-KVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKI 301
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAeDILLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                       250       260       270
                ....*....|....*....|....*....|....*....
3ZYS_E      302 FFENHPYFRDLLEEgKATVPCLAEKLTSELITHICKSLP 340
Cdd:cd08771 241 FFETHPWYKLLPAS-RVGTPALRKRLSKLLQKHIRESLP 278
GED smart00302
Dynamin GTPase effector domain;
571-660 6.59e-31

Dynamin GTPase effector domain;


:

Pssm-ID: 128597  Cd Length: 92  Bit Score: 115.80  E-value: 6.59e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E         571 DSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARL 650
Cdd:smart00302   3 DSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLELL 82
                           90
                   ....*....|
3ZYS_E         651 TQARRRLAQF 660
Cdd:smart00302  83 KKARQIIAAV 92
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
259-546 4.45e-120

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: 359.14  E-value: 4.45e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        259 KVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFENHPYFRDLleEGKATVPCLAEKLTSELITHICKS 338
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLL--ADKCGTPYLAKKLNQILVNHIRKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        339 LPLLENQIKETHQRITEELQKYGVDIPEDENEKMFFLIDKVNAFNQDITALMQGEETVGEEDIRLFTRLRHEFHKWSTII 418
Cdd:pfam01031  79 LPDLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEISTNELSGGARIRYIFNEIFPKS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        419 ENNFQEGHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLhtvtDMVRLAFTDVSIK---NFEEF 495
Cdd:pfam01031 159 LEKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCV----ELVYEELERIIHKctpELKRF 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
3ZYS_E        496 FNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQ-IVYCQDQVYRGALQKVR 546
Cdd:pfam01031 235 PNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELaYINTNHPDFIGGLNAVR 286
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
68-340 1.95e-119

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: 356.94  E-value: 1.95e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E       68 LALPAIAVIGDQSSGKSSVLEALSGV-ALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEI----EISDASEVEKE 142
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRdFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHlkskEFTDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E      143 INKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVD 222
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E      223 IATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTED-KVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKI 301
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAeDILLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                       250       260       270
                ....*....|....*....|....*....|....*....
3ZYS_E      302 FFENHPYFRDLLEEgKATVPCLAEKLTSELITHICKSLP 340
Cdd:cd08771 241 FFETHPWYKLLPAS-RVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
46-289 1.41e-101

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: 309.89  E-value: 1.41e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E          46 EEKVRPCIDLIDSLR-ALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKLVNEdkWRGK 123
Cdd:smart00053   1 MEELIPLVNKLQDAFsALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDfLPRGSGIVTRRPLILQLIKSKTE--YAEF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E         124 VSYQDYEIeiSDASEVEKEINKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIK 203
Cdd:smart00053  79 LHCKGKKF--TDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E         204 KYIQRQETISLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTEdkVVDVVRNLVFHLKKGYMIVKCRGQ 283
Cdd:smart00053 157 QFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTD--ARDILENKLLPLRRGYIGVVNRSQ 234

                   ....*.
3ZYS_E         284 QEIQDQ 289
Cdd:smart00053 235 KDIEGK 240
Dynamin_N pfam00350
Dynamin family;
73-249 1.70e-62

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 205.16  E-value: 1.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E         73 IAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNAIA 151
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDiLPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKDGEKKFEDFSELREEIEKETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        152 GEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQpadigykikTLIKKYIQrQETISLVVVPSNVDIATTEALSM 231
Cdd:pfam00350  81 GTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYIK-PADIILAVTPANVDLSTSEALFL 150
                         170
                  ....*....|....*...
3ZYS_E        232 AQEVDPEGDRTIGILTKP 249
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
GED smart00302
Dynamin GTPase effector domain;
571-660 6.59e-31

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 115.80  E-value: 6.59e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E         571 DSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARL 650
Cdd:smart00302   3 DSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLELL 82
                           90
                   ....*....|
3ZYS_E         651 TQARRRLAQF 660
Cdd:smart00302  83 KKARQIIAAV 92
GED pfam02212
Dynamin GTPase effector domain;
571-660 7.46e-31

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.69  E-value: 7.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        571 DSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARL 650
Cdd:pfam02212   2 ESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEAL 81
                          90
                  ....*....|
3ZYS_E        651 TQARRRLAQF 660
Cdd:pfam02212  82 KQAREILSEV 91
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
259-546 4.45e-120

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: 359.14  E-value: 4.45e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        259 KVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFENHPYFRDLleEGKATVPCLAEKLTSELITHICKS 338
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLL--ADKCGTPYLAKKLNQILVNHIRKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        339 LPLLENQIKETHQRITEELQKYGVDIPEDENEKMFFLIDKVNAFNQDITALMQGEETVGEEDIRLFTRLRHEFHKWSTII 418
Cdd:pfam01031  79 LPDLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEISTNELSGGARIRYIFNEIFPKS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        419 ENNFQEGHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLhtvtDMVRLAFTDVSIK---NFEEF 495
Cdd:pfam01031 159 LEKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCV----ELVYEELERIIHKctpELKRF 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
3ZYS_E        496 FNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQ-IVYCQDQVYRGALQKVR 546
Cdd:pfam01031 235 PNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELaYINTNHPDFIGGLNAVR 286
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
68-340 1.95e-119

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: 356.94  E-value: 1.95e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E       68 LALPAIAVIGDQSSGKSSVLEALSGV-ALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEI----EISDASEVEKE 142
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRdFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHlkskEFTDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E      143 INKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVD 222
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E      223 IATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTED-KVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKI 301
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAeDILLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                       250       260       270
                ....*....|....*....|....*....|....*....
3ZYS_E      302 FFENHPYFRDLLEEgKATVPCLAEKLTSELITHICKSLP 340
Cdd:cd08771 241 FFETHPWYKLLPAS-RVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
46-289 1.41e-101

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: 309.89  E-value: 1.41e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E          46 EEKVRPCIDLIDSLR-ALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKLVNEdkWRGK 123
Cdd:smart00053   1 MEELIPLVNKLQDAFsALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDfLPRGSGIVTRRPLILQLIKSKTE--YAEF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E         124 VSYQDYEIeiSDASEVEKEINKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIK 203
Cdd:smart00053  79 LHCKGKKF--TDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E         204 KYIQRQETISLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTEdkVVDVVRNLVFHLKKGYMIVKCRGQ 283
Cdd:smart00053 157 QFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTD--ARDILENKLLPLRRGYIGVVNRSQ 234

                   ....*.
3ZYS_E         284 QEIQDQ 289
Cdd:smart00053 235 KDIEGK 240
Dynamin_N pfam00350
Dynamin family;
73-249 1.70e-62

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 205.16  E-value: 1.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E         73 IAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNAIA 151
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDiLPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKDGEKKFEDFSELREEIEKETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        152 GEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQpadigykikTLIKKYIQrQETISLVVVPSNVDIATTEALSM 231
Cdd:pfam00350  81 GTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYIK-PADIILAVTPANVDLSTSEALFL 150
                         170
                  ....*....|....*...
3ZYS_E        232 AQEVDPEGDRTIGILTKP 249
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
GED smart00302
Dynamin GTPase effector domain;
571-660 6.59e-31

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 115.80  E-value: 6.59e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E         571 DSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARL 650
Cdd:smart00302   3 DSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLELL 82
                           90
                   ....*....|
3ZYS_E         651 TQARRRLAQF 660
Cdd:smart00302  83 KKARQIIAAV 92
GED pfam02212
Dynamin GTPase effector domain;
571-660 7.46e-31

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 115.69  E-value: 7.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ZYS_E        571 DSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARL 650
Cdd:pfam02212   2 ESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEAL 81
                          90
                  ....*....|
3ZYS_E        651 TQARRRLAQF 660
Cdd:pfam02212  82 KQAREILSEV 91
 
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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