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Conserved domains on  [gi|11342664|ref|NP_002454|]
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interferon-induced GTP-binding protein Mx2 [Homo sapiens]

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
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
116-387 3.78e-113

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: 342.69  E-value: 3.78e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664 116 LALPAIAVIGDQSSGKSSVLEALSGV-ALPRGSGIVTRCPLVLKLKKQP-CEAWAGRISYR----NTELELQDPGQVEKE 189
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRdFLPRGSGICTRRPLELQLRRSPsESDEDEKEEWGeflhLKSKEFTDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664 190 IHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRDIGLQIKALIKKYIQRQQTINLVVVPCNVD 269
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664 270 IATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEKSVMNV-VRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEIT 348
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLlLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 11342664 349 FFQTHPYFRvLLEEGSATVPRLAERLTTELIMHIQKSLP 387
Cdd:cd08771 241 FFETHPWYK-LLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
307-594 3.89e-103

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: 317.15  E-value: 3.89e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   307 VMNVVRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEITFFQTHPYFRVLleEGSATVPRLAERLTTELIMHIQKSL 386
Cdd:pfam01031   2 ALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLL--ADKCGTPYLAKKLNQILVNHIRKSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   387 PLLEGQIRESHQKATEELRRCGADIPSQEADKMFFLIEKIKMFNQDIEKLVEGEEVVRENETRLYNKIREDFKNWvgiLA 466
Cdd:pfam01031  80 PDLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEISTNELSGGARIRYIFNEI---FP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   467 TNTQKVKNIIH---EEVEKYEKQYRGKELLGFVNYKTFEIIVHQYIQQLVEPALSMLqkamEIIQQAFINVAKK---HFG 540
Cdd:pfam01031 157 KSLEKIDPLENlsdEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCV----ELVYEELERIIHKctpELK 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 11342664   541 EFFNLNQTVQSTIEDIKVKHTAKAENMIQLQFRMEQ-MVFCQDQIYSVVLKKVRE 594
Cdd:pfam01031 233 RFPNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELaYINTNHPDFIGGLNAVRE 287
GED smart00302
Dynamin GTPase effector domain;
621-709 7.15e-31

Dynamin GTPase effector domain;


:

Pssm-ID: 128597  Cd Length: 92  Bit Score: 116.18  E-value: 7.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664    621 SSFTEIGIHLNAYFLETSKRLANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYRLT 700
Cdd:smart00302   4 SELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLELLK 83

                   ....*....
gi 11342664    701 QARHALCQF 709
Cdd:smart00302  84 KARQIIAAV 92
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
116-387 3.78e-113

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: 342.69  E-value: 3.78e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664 116 LALPAIAVIGDQSSGKSSVLEALSGV-ALPRGSGIVTRCPLVLKLKKQP-CEAWAGRISYR----NTELELQDPGQVEKE 189
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRdFLPRGSGICTRRPLELQLRRSPsESDEDEKEEWGeflhLKSKEFTDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664 190 IHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRDIGLQIKALIKKYIQRQQTINLVVVPCNVD 269
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664 270 IATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEKSVMNV-VRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEIT 348
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLlLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 11342664 349 FFQTHPYFRvLLEEGSATVPRLAERLTTELIMHIQKSLP 387
Cdd:cd08771 241 FFETHPWYK-LLPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
94-336 4.50e-105

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: 320.29  E-value: 4.50e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664     94 EQKVRPCIDLIDSLR-ALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKQPCEaWAGRI 171
Cdd:smart00053   1 MEELIPLVNKLQDAFsALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDfLPRGSGIVTRRPLILQLIKSKTE-YAEFL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664    172 SYRNTELelQDPGQVEKEIHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRDIGLQIKALIKK 251
Cdd:smart00053  80 HCKGKKF--TDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664    252 YIQRQQTINLVVVPCNVDIATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEksVMNVVRNLTYPLKKGYMIVKCRGQQ 331
Cdd:smart00053 158 FISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTD--ARDILENKLLPLRRGYIGVVNRSQK 235

                   ....*
gi 11342664    332 EITNR 336
Cdd:smart00053 236 DIEGK 240
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
307-594 3.89e-103

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: 317.15  E-value: 3.89e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   307 VMNVVRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEITFFQTHPYFRVLleEGSATVPRLAERLTTELIMHIQKSL 386
Cdd:pfam01031   2 ALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLL--ADKCGTPYLAKKLNQILVNHIRKSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   387 PLLEGQIRESHQKATEELRRCGADIPSQEADKMFFLIEKIKMFNQDIEKLVEGEEVVRENETRLYNKIREDFKNWvgiLA 466
Cdd:pfam01031  80 PDLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEISTNELSGGARIRYIFNEI---FP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   467 TNTQKVKNIIH---EEVEKYEKQYRGKELLGFVNYKTFEIIVHQYIQQLVEPALSMLqkamEIIQQAFINVAKK---HFG 540
Cdd:pfam01031 157 KSLEKIDPLENlsdEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCV----ELVYEELERIIHKctpELK 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 11342664   541 EFFNLNQTVQSTIEDIKVKHTAKAENMIQLQFRMEQ-MVFCQDQIYSVVLKKVRE 594
Cdd:pfam01031 233 RFPNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELaYINTNHPDFIGGLNAVRE 287
Dynamin_N pfam00350
Dynamin family;
121-296 9.91e-61

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 201.31  E-value: 9.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   121 IAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKQP-CEAWAGRISYRNTELELQDPGQVEKEIHKAQNVMA 198
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDiLPRGPGPTTRRPTVLRLGESPgASEGAVKVEYKDGEKKFEDFSELREEIEKETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   199 GNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQprdiglqikALIKKYIQrQQTINLVVVPCNVDIATTEALSM 278
Cdd:pfam00350  81 GTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYIK-PADIILAVTPANVDLSTSEALFL 150
                         170
                  ....*....|....*...
gi 11342664   279 AHEVDPEGDRTIGILTKP 296
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
GED smart00302
Dynamin GTPase effector domain;
621-709 7.15e-31

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 116.18  E-value: 7.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664    621 SSFTEIGIHLNAYFLETSKRLANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYRLT 700
Cdd:smart00302   4 SELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLELLK 83

                   ....*....
gi 11342664    701 QARHALCQF 709
Cdd:smart00302  84 KARQIIAAV 92
GED pfam02212
Dynamin GTPase effector domain;
619-709 1.06e-29

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 112.61  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   619 SVSSFTEIGIHLNAYFLETSKRLANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYR 698
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 11342664   699 LTQARHALCQF 709
Cdd:pfam02212  81 LKQAREILSEV 91
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
116-387 3.78e-113

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: 342.69  E-value: 3.78e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664 116 LALPAIAVIGDQSSGKSSVLEALSGV-ALPRGSGIVTRCPLVLKLKKQP-CEAWAGRISYR----NTELELQDPGQVEKE 189
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRdFLPRGSGICTRRPLELQLRRSPsESDEDEKEEWGeflhLKSKEFTDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664 190 IHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRDIGLQIKALIKKYIQRQQTINLVVVPCNVD 269
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664 270 IATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEKSVMNV-VRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEIT 348
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLlLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 11342664 349 FFQTHPYFRvLLEEGSATVPRLAERLTTELIMHIQKSLP 387
Cdd:cd08771 241 FFETHPWYK-LLPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
94-336 4.50e-105

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: 320.29  E-value: 4.50e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664     94 EQKVRPCIDLIDSLR-ALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKQPCEaWAGRI 171
Cdd:smart00053   1 MEELIPLVNKLQDAFsALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDfLPRGSGIVTRRPLILQLIKSKTE-YAEFL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664    172 SYRNTELelQDPGQVEKEIHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRDIGLQIKALIKK 251
Cdd:smart00053  80 HCKGKKF--TDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664    252 YIQRQQTINLVVVPCNVDIATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEksVMNVVRNLTYPLKKGYMIVKCRGQQ 331
Cdd:smart00053 158 FISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTD--ARDILENKLLPLRRGYIGVVNRSQK 235

                   ....*
gi 11342664    332 EITNR 336
Cdd:smart00053 236 DIEGK 240
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
307-594 3.89e-103

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: 317.15  E-value: 3.89e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   307 VMNVVRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEITFFQTHPYFRVLleEGSATVPRLAERLTTELIMHIQKSL 386
Cdd:pfam01031   2 ALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLL--ADKCGTPYLAKKLNQILVNHIRKSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   387 PLLEGQIRESHQKATEELRRCGADIPSQEADKMFFLIEKIKMFNQDIEKLVEGEEVVRENETRLYNKIREDFKNWvgiLA 466
Cdd:pfam01031  80 PDLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEISTNELSGGARIRYIFNEI---FP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   467 TNTQKVKNIIH---EEVEKYEKQYRGKELLGFVNYKTFEIIVHQYIQQLVEPALSMLqkamEIIQQAFINVAKK---HFG 540
Cdd:pfam01031 157 KSLEKIDPLENlsdEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCV----ELVYEELERIIHKctpELK 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 11342664   541 EFFNLNQTVQSTIEDIKVKHTAKAENMIQLQFRMEQ-MVFCQDQIYSVVLKKVRE 594
Cdd:pfam01031 233 RFPNLRERIKEVVEDLLRERLEPTEKMIRSLIEMELaYINTNHPDFIGGLNAVRE 287
Dynamin_N pfam00350
Dynamin family;
121-296 9.91e-61

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 201.31  E-value: 9.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   121 IAVIGDQSSGKSSVLEALSGVA-LPRGSGIVTRCPLVLKLKKQP-CEAWAGRISYRNTELELQDPGQVEKEIHKAQNVMA 198
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDiLPRGPGPTTRRPTVLRLGESPgASEGAVKVEYKDGEKKFEDFSELREEIEKETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   199 GNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQprdiglqikALIKKYIQrQQTINLVVVPCNVDIATTEALSM 278
Cdd:pfam00350  81 GTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYIK-PADIILAVTPANVDLSTSEALFL 150
                         170
                  ....*....|....*...
gi 11342664   279 AHEVDPEGDRTIGILTKP 296
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
GED smart00302
Dynamin GTPase effector domain;
621-709 7.15e-31

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 116.18  E-value: 7.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664    621 SSFTEIGIHLNAYFLETSKRLANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYRLT 700
Cdd:smart00302   4 SELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLELLK 83

                   ....*....
gi 11342664    701 QARHALCQF 709
Cdd:smart00302  84 KARQIIAAV 92
GED pfam02212
Dynamin GTPase effector domain;
619-709 1.06e-29

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 112.61  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11342664   619 SVSSFTEIGIHLNAYFLETSKRLANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYR 698
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 11342664   699 LTQARHALCQF 709
Cdd:pfam02212  81 LKQAREILSEV 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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