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Conserved domains on  [gi|1958664755|ref|XP_038943983|]
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interferon-induced GTP-binding protein Mx2 isoform X1 [Rattus norvegicus]

Protein Classification

dynamin family protein( domain architecture ID 10171943)

dynamin family protein similar to dynamins and dynamin-like proteins (DLPs), which catalyze membrane fission during clathrin-mediated endocytosis 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); contains a dynamin GTPase effector domain (GED);

EC:  3.6.5.-
Gene Ontology:  GO:0003924|GO:0005525
SCOP:  4004047|4004048

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 ...
257-544 1.72e-113

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: 342.19  E-value: 1.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 257 KVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRALleDGKATVPCLAERLTMELISHICKS 336
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLL--ADKCGTPYLAKKLNQILVNHIRKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 337 LPLLENQIKESHQSTSEELQKYGADIPEDENEKTLFLIEKINAFNQDITAIVEGEEIVREKECRLFTKLRKEFflwSEEI 416
Cdd:pfam01031  79 LPDLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEISTNELSGGARIRYIF---NEIF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 417 ERNFQKG---SDALYKEVYTFEMQYRGRELPGFVNYKTFENIIRRQIKTLEEPAMEMLHKVTEIVRAAFTTvSEKNFSEF 493
Cdd:pfam01031 156 PKSLEKIdplENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHK-CTPELKRF 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958664755 494 FNLHRTTKSKLEDIRLEQETEAEKAIRLHFQMEQ-IIYCQDQIYRKALQKVR 544
Cdd:pfam01031 235 PNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELaYINTNHPDFIGGLNAVR 286
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
66-338 2.10e-110

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: 333.83  E-value: 2.10e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  66 LALPAIAVIGDQSSGKSSVLEALSGV-ALPRGSGIVTRCPLVLKLKKLNQGEEWKGKVTYDDIEV----ELSDPSEVEEA 140
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRdFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHlkskEFTDFEELREE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 141 INTGQNHIAGVGLGISDKLISLDVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQIKRLITNYIQKQETINLVVVPSNVD 220
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 221 IATTEALSMAQKVDPDGDRTIGILTKPDLVDRGTED-KVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQV 299
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAeDILLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958664755 300 FFKEHPQFRALLEDgKATVPCLAERLTMELISHICKSLP 338
Cdd:cd08771   241 FFETHPWYKLLPAS-RVGTPALRKRLSKLLQKHIRESLP 278
GED pfam02212
Dynamin GTPase effector domain;
567-657 7.63e-27

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 104.52  E-value: 7.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 567 QTSSMDEIFQHLNAYRQEAHNCISSHIPLIIQYFILKMFAEKLQKGMLQLLQDKDSCSWLLKEKSDTSEKRRFLKERLAR 646
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1958664755 647 LAQAQRRLAKF 657
Cdd:pfam02212  81 LKQAREILSEV 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 ...
257-544 1.72e-113

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: 342.19  E-value: 1.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 257 KVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRALleDGKATVPCLAERLTMELISHICKS 336
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLL--ADKCGTPYLAKKLNQILVNHIRKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 337 LPLLENQIKESHQSTSEELQKYGADIPEDENEKTLFLIEKINAFNQDITAIVEGEEIVREKECRLFTKLRKEFflwSEEI 416
Cdd:pfam01031  79 LPDLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEISTNELSGGARIRYIF---NEIF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 417 ERNFQKG---SDALYKEVYTFEMQYRGRELPGFVNYKTFENIIRRQIKTLEEPAMEMLHKVTEIVRAAFTTvSEKNFSEF 493
Cdd:pfam01031 156 PKSLEKIdplENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHK-CTPELKRF 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958664755 494 FNLHRTTKSKLEDIRLEQETEAEKAIRLHFQMEQ-IIYCQDQIYRKALQKVR 544
Cdd:pfam01031 235 PNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELaYINTNHPDFIGGLNAVR 286
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
66-338 2.10e-110

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: 333.83  E-value: 2.10e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  66 LALPAIAVIGDQSSGKSSVLEALSGV-ALPRGSGIVTRCPLVLKLKKLNQGEEWKGKVTYDDIEV----ELSDPSEVEEA 140
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRdFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHlkskEFTDFEELREE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 141 INTGQNHIAGVGLGISDKLISLDVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQIKRLITNYIQKQETINLVVVPSNVD 220
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 221 IATTEALSMAQKVDPDGDRTIGILTKPDLVDRGTED-KVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQV 299
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAeDILLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958664755 300 FFKEHPQFRALLEDgKATVPCLAERLTMELISHICKSLP 338
Cdd:cd08771   241 FFETHPWYKLLPAS-RVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
44-285 1.81e-100

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: 306.81  E-value: 1.81e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755   44 EEKVRPCIDLIDSLR-ALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKLNQgeEWKGK 121
Cdd:smart00053   1 MEELIPLVNKLQDAFsALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDfLPRGSGIVTRRPLILQLIKSKT--EYAEF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  122 VTYDDieVELSDPSEVEEAINTGQNHIAGVGLGISDKLISLDVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQIKRLIT 201
Cdd:smart00053  79 LHCKG--KKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  202 NYIQKQETINLVVVPSNVDIATTEALSMAQKVDPDGDRTIGILTKPDLVDRGTEdkVVDVVRNLVCHLKKGYMIVKCRGQ 281
Cdd:smart00053 157 QFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTD--ARDILENKLLPLRRGYIGVVNRSQ 234

                   ....
gi 1958664755  282 QDIQ 285
Cdd:smart00053 235 KDIE 238
Dynamin_N pfam00350
Dynamin family;
71-247 7.39e-59

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 195.14  E-value: 7.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  71 IAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKLNQGEEWKGKVTYDDIEVELSDPSEVEEAINTGQNHIA 149
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDiLPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKDGEKKFEDFSELREEIEKETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 150 GVGLGISDKLISLDVSSPHVPDLTLIDLPGITRVAVGNQpadigrqikRLITNYIqKQETINLVVVPSNVDIATTEALSM 229
Cdd:pfam00350  81 GTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSEALFL 150
                         170
                  ....*....|....*...
gi 1958664755 230 AQKVDPDGDRTIGILTKP 247
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
567-657 7.63e-27

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 104.52  E-value: 7.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 567 QTSSMDEIFQHLNAYRQEAHNCISSHIPLIIQYFILKMFAEKLQKGMLQLLQDKDSCSWLLKEKSDTSEKRRFLKERLAR 646
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1958664755 647 LAQAQRRLAKF 657
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
569-657 2.28e-22

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 91.53  E-value: 2.28e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  569 SSMDEIFQHLNAYRQEAHNCISSHIPLIIQYFILKMFAEKLQKGMLQLLQDKDSCSWLLKEKSDTSEKRRFLKERLARLA 648
Cdd:smart00302   4 SELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLELLK 83

                   ....*....
gi 1958664755  649 QAQRRLAKF 657
Cdd:smart00302  84 KARQIIAAV 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 ...
257-544 1.72e-113

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: 342.19  E-value: 1.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 257 KVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQVFFKEHPQFRALleDGKATVPCLAERLTMELISHICKS 336
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLL--ADKCGTPYLAKKLNQILVNHIRKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 337 LPLLENQIKESHQSTSEELQKYGADIPEDENEKTLFLIEKINAFNQDITAIVEGEEIVREKECRLFTKLRKEFflwSEEI 416
Cdd:pfam01031  79 LPDLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEISTNELSGGARIRYIF---NEIF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 417 ERNFQKG---SDALYKEVYTFEMQYRGRELPGFVNYKTFENIIRRQIKTLEEPAMEMLHKVTEIVRAAFTTvSEKNFSEF 493
Cdd:pfam01031 156 PKSLEKIdplENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHK-CTPELKRF 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958664755 494 FNLHRTTKSKLEDIRLEQETEAEKAIRLHFQMEQ-IIYCQDQIYRKALQKVR 544
Cdd:pfam01031 235 PNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELaYINTNHPDFIGGLNAVR 286
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
66-338 2.10e-110

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: 333.83  E-value: 2.10e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  66 LALPAIAVIGDQSSGKSSVLEALSGV-ALPRGSGIVTRCPLVLKLKKLNQGEEWKGKVTYDDIEV----ELSDPSEVEEA 140
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRdFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHlkskEFTDFEELREE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 141 INTGQNHIAGVGLGISDKLISLDVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQIKRLITNYIQKQETINLVVVPSNVD 220
Cdd:cd08771    81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 221 IATTEALSMAQKVDPDGDRTIGILTKPDLVDRGTED-KVVDVVRNLVCHLKKGYMIVKCRGQQDIQEQLSLAEALQKEQV 299
Cdd:cd08771   161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAeDILLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958664755 300 FFKEHPQFRALLEDgKATVPCLAERLTMELISHICKSLP 338
Cdd:cd08771   241 FFETHPWYKLLPAS-RVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
44-285 1.81e-100

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: 306.81  E-value: 1.81e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755   44 EEKVRPCIDLIDSLR-ALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKLNQgeEWKGK 121
Cdd:smart00053   1 MEELIPLVNKLQDAFsALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDfLPRGSGIVTRRPLILQLIKSKT--EYAEF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  122 VTYDDieVELSDPSEVEEAINTGQNHIAGVGLGISDKLISLDVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQIKRLIT 201
Cdd:smart00053  79 LHCKG--KKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  202 NYIQKQETINLVVVPSNVDIATTEALSMAQKVDPDGDRTIGILTKPDLVDRGTEdkVVDVVRNLVCHLKKGYMIVKCRGQ 281
Cdd:smart00053 157 QFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTD--ARDILENKLLPLRRGYIGVVNRSQ 234

                   ....
gi 1958664755  282 QDIQ 285
Cdd:smart00053 235 KDIE 238
Dynamin_N pfam00350
Dynamin family;
71-247 7.39e-59

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 195.14  E-value: 7.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  71 IAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKLNQGEEWKGKVTYDDIEVELSDPSEVEEAINTGQNHIA 149
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDiLPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKDGEKKFEDFSELREEIEKETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 150 GVGLGISDKLISLDVSSPHVPDLTLIDLPGITRVAVGNQpadigrqikRLITNYIqKQETINLVVVPSNVDIATTEALSM 229
Cdd:pfam00350  81 GTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSEALFL 150
                         170
                  ....*....|....*...
gi 1958664755 230 AQKVDPDGDRTIGILTKP 247
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
567-657 7.63e-27

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 104.52  E-value: 7.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755 567 QTSSMDEIFQHLNAYRQEAHNCISSHIPLIIQYFILKMFAEKLQKGMLQLLQDKDSCSWLLKEKSDTSEKRRFLKERLAR 646
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1958664755 647 LAQAQRRLAKF 657
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
569-657 2.28e-22

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 91.53  E-value: 2.28e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958664755  569 SSMDEIFQHLNAYRQEAHNCISSHIPLIIQYFILKMFAEKLQKGMLQLLQDKDSCSWLLKEKSDTSEKRRFLKERLARLA 648
Cdd:smart00302   4 SELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLELLK 83

                   ....*....
gi 1958664755  649 QAQRRLAKF 657
Cdd:smart00302  84 KARQIIAAV 92
 
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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