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Conserved domains on  [gi|377520165|ref|NP_001243698|]
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myxovirus influenza virus resistance 1 [Xenopus laevis]

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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 ...
34-304 2.81e-109

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: 332.67  E-value: 2.81e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  34 LPSIAVIGDQSSGKSSVLEALSGVT-LPRGSGIVTRCPLELKLKKATKSTTWSGKISYRDHELT----IASAAEVENQVK 108
Cdd:cd08771    3 LPQIVVVGDQSSGKSSVLEALVGRDfLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHLkskeFTDFEELREEIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 109 QAQNLMAGNGKGISDELISLEVISPDVPDLTLIDLPGITRVALPDQPKDIGQQIKKMIRKYIQRQETINLVVVPSNVDIA 188
Cdd:cd08771   83 KETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVDLA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 189 TTEALEMAREVDPNGERTLGILTKPDLVDRGAES-DVVSVVRNLVYSLQKGYMIVKCRGQLEIQENLSLKEALDNEQNFF 267
Cdd:cd08771  163 NSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAeDILLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEEFF 242
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 377520165 268 KEHEHFSvLLEEGNATIACLAEKLTNELVDHIVKTLP 304
Cdd:cd08771  243 ETHPWYK-LLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This region lies between the GTPase domain, see pfam00350, and the ...
225-511 1.56e-83

Dynamin central region; This region lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169.


:

Pssm-ID: 279383  Cd Length: 285  Bit Score: 265.92  E-value: 1.56e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  225 VSVVRNLVYSLQKGYMIVKCRGQLEIQENLSLKEALDNEQNFFKEHEHFSVLleEGNATIACLAEKLTNELVDHIVKTLP 304
Cdd:pfam01031   1 VDILRNRVIPLKLGYVGVVNRSQKDINGKKSIEEALQAEREFFETHPAYRLL--ADRCGTPYLAKKLNQILVNHIRKSLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  305 ALDTQIRKKLNEAEEKLRNLGTSVPdSETEKLRFLIDKITRFAGAIINATQGDEEMTNGSLKLFTVIRkhFYFWESFIQT 384
Cdd:pfam01031  79 DLKKKINELLQKLEKELEKYGPGIP-SPAEKGKFLLQIITKFNEDFKNLIDGEEVSDTNELSGGARIR--YIFNEIFPKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  385 QSK--SFQDKSRDDISEFENKYRGRELPGFISFKVFENIARGQIRCLEEPAMEKLKEVTEIVKAHFNQIAMKHFLAFPNL 462
Cdd:pfam01031 156 LEKidPLENLLDEEIRTAIRNSRGIRLPLFVPEKAFEVLVKQQIKRLEEPALKCVELVYEELERIVQKCLTPELKRFPNL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 377520165  463 YRGAKVRIEDICHKQVWEAERTIRTQFKMEK-IIYCQDRLYSGRLNEVRS 511
Cdd:pfam01031 236 RDEIKEVVEDLLRERLEPTKKMIRNLIDMELaYINTNHPDFIGGLNAIRE 285
GED pfam02212
Dynamin GTPase effector domain;
534-622 1.50e-19

Dynamin GTPase effector domain;


:

Pssm-ID: 280391  Cd Length: 89  Bit Score: 84.09  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  534 ISCDEMHYHVQAYFKSLKERLSNQIPMIIQYYILHEFSEKLQNQMMQLIQEREKLNTLLAEKTDITRVRDNLSNRIERLT 613
Cdd:pfam02212   1 SEVEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKDSLQKELLAQLYKSELLDELLKEDPEIAQKRKELKKRLEALK 80

                  ....*....
gi 377520165  614 AASHKLAKF 622
Cdd:pfam02212  81 QAREILSEV 89
CrfC COG0699
Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, ...
119-455 1.21e-10

Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, recombination and repair];


:

Pssm-ID: 223771 [Multi-domain]  Cd Length: 546  Bit Score: 63.00  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 119 KGISDELISLEVISPDVPDLTLIDLPGITRVALPDQPKDIGQQIKKMIRKYIQRQETINLVVVPSNVDIATTEALEMARE 198
Cdd:COG0699   36 SGITEVIIELKIAAERLLQLTDVDLPGLRKVPLSLEPEDIAQEDELLDLGKIEIENALILLGIAPNADEEAELSIEVIRE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 199 VDPngertlgILTKPDLVDRGaesdvvsvvRNLVYSLQKGYMIVKCRGQLEIQENLSLKEALDNEQNFFKEHEH-----F 273
Cdd:COG0699  116 ADR-------VPTKINFLNGG---------TNLTLILGNGDVLVVDALETDIQLLKTALEALVKELEYFAEHPLledneK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 274 SVLLEEgnatiacLAEKLTNELVDHIVKTLP--ALDTQIRKKLNEAEEKLRNLGTSVPD--SETEKLRFLIDKITRFAGA 349
Cdd:COG0699  180 LVLLPY-------LKKLLSKILELHLRLLPKydKLQDVIQLSQDLFENEVLAVIQTLLKrlSELVRGARIRLNIILFSDL 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 350 I-INATQGDEEMTNGSLKLFTVIRKHFYFwESFIQTQSKSFQDKSRDDISE-----FENKYRGRELPGFISFKVFENIAR 423
Cdd:COG0699  253 EeVSDSPVLLKELASKGERPSLLSGLTLL-DTLVETPIGQFDTQINQLLRKliselVRILLKELESASSSPFPKLSEALE 331
                        330       340       350
                 ....*....|....*....|....*....|...
gi 377520165 424 GQIRCLEEPAMEKLKEVTEIVKAHFNQ-IAMKH 455
Cdd:COG0699  332 EVVNQLKNKVDSGLESGLLAIIDIEERyINTKH 364
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
34-304 2.81e-109

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: 332.67  E-value: 2.81e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  34 LPSIAVIGDQSSGKSSVLEALSGVT-LPRGSGIVTRCPLELKLKKATKSTTWSGKISYRDHELT----IASAAEVENQVK 108
Cdd:cd08771    3 LPQIVVVGDQSSGKSSVLEALVGRDfLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHLkskeFTDFEELREEIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 109 QAQNLMAGNGKGISDELISLEVISPDVPDLTLIDLPGITRVALPDQPKDIGQQIKKMIRKYIQRQETINLVVVPSNVDIA 188
Cdd:cd08771   83 KETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVDLA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 189 TTEALEMAREVDPNGERTLGILTKPDLVDRGAES-DVVSVVRNLVYSLQKGYMIVKCRGQLEIQENLSLKEALDNEQNFF 267
Cdd:cd08771  163 NSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAeDILLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEEFF 242
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 377520165 268 KEHEHFSvLLEEGNATIACLAEKLTNELVDHIVKTLP 304
Cdd:cd08771  243 ETHPWYK-LLPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
10-251 5.44e-103

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: 314.89  E-value: 5.44e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165    10 EEKIRPCIDLIDSLR-ALGVDKDLGLPSIAVIGDQSSGKSSVLEALSGVT-LPRGSGIVTRCPLELKLKKAtkSTTWSGK 87
Cdd:smart00053   1 MEELIPLVNKLQDAFsALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDfLPRGSGIVTRRPLILQLIKS--KTEYAEF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165    88 ISYRDHELTiaSAAEVENQVKQAQNLMAGNGKGISDELISLEVISPDVPDLTLIDLPGITRVALPDQPKDIGQQIKKMIR 167
Cdd:smart00053  79 LHCKGKKFT--DFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165   168 KYIQRQETINLVVVPSNVDIATTEALEMAREVDPNGERTLGILTKPDLVDRGaeSDVVSVVRNLVYSLQKGYMIVKCRGQ 247
Cdd:smart00053 157 QFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEG--TDARDILENKLLPLRRGYIGVVNRSQ 234

                   ....
gi 377520165   248 LEIQ 251
Cdd:smart00053 235 KDIE 238
Dynamin_M pfam01031
Dynamin central region; This region lies between the GTPase domain, see pfam00350, and the ...
225-511 1.56e-83

Dynamin central region; This region lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169.


Pssm-ID: 279383  Cd Length: 285  Bit Score: 265.92  E-value: 1.56e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  225 VSVVRNLVYSLQKGYMIVKCRGQLEIQENLSLKEALDNEQNFFKEHEHFSVLleEGNATIACLAEKLTNELVDHIVKTLP 304
Cdd:pfam01031   1 VDILRNRVIPLKLGYVGVVNRSQKDINGKKSIEEALQAEREFFETHPAYRLL--ADRCGTPYLAKKLNQILVNHIRKSLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  305 ALDTQIRKKLNEAEEKLRNLGTSVPdSETEKLRFLIDKITRFAGAIINATQGDEEMTNGSLKLFTVIRkhFYFWESFIQT 384
Cdd:pfam01031  79 DLKKKINELLQKLEKELEKYGPGIP-SPAEKGKFLLQIITKFNEDFKNLIDGEEVSDTNELSGGARIR--YIFNEIFPKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  385 QSK--SFQDKSRDDISEFENKYRGRELPGFISFKVFENIARGQIRCLEEPAMEKLKEVTEIVKAHFNQIAMKHFLAFPNL 462
Cdd:pfam01031 156 LEKidPLENLLDEEIRTAIRNSRGIRLPLFVPEKAFEVLVKQQIKRLEEPALKCVELVYEELERIVQKCLTPELKRFPNL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 377520165  463 YRGAKVRIEDICHKQVWEAERTIRTQFKMEK-IIYCQDRLYSGRLNEVRS 511
Cdd:pfam01031 236 RDEIKEVVEDLLRERLEPTKKMIRNLIDMELaYINTNHPDFIGGLNAIRE 285
Dynamin_N pfam00350
Dynamin family;
37-213 1.37e-59

Dynamin family;


Pssm-ID: 278765  Cd Length: 168  Bit Score: 198.21  E-value: 1.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165   37 IAVIGDQSSGKSSVLEALSGVT-LPRGSGIVTRCPLELKLKKATKSTTWSGKISYRDHELTIASAAEVENQVKQAQNLMA 115
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDiLPRGPGPTTRRPLVLRLGESPGASEGAVKVEYKDGLKKFEDFSELREEIENETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  116 GNGKGISDELISLEVISPDVPDLTLIDLPGITRVALPDQpkdigqqikKMIRKYIQRqETINLVVVPSNVDIATTEALEM 195
Cdd:pfam00350  81 GTGKGVSSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYIKP-ADIILAVTPANVDLSTSEALFL 150
                         170
                  ....*....|....*...
gi 377520165  196 AREVDPNGERTLGILTKP 213
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
534-622 1.50e-19

Dynamin GTPase effector domain;


Pssm-ID: 280391  Cd Length: 89  Bit Score: 84.09  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  534 ISCDEMHYHVQAYFKSLKERLSNQIPMIIQYYILHEFSEKLQNQMMQLIQEREKLNTLLAEKTDITRVRDNLSNRIERLT 613
Cdd:pfam02212   1 SEVEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKDSLQKELLAQLYKSELLDELLKEDPEIAQKRKELKKRLEALK 80

                  ....*....
gi 377520165  614 AASHKLAKF 622
Cdd:pfam02212  81 QAREILSEV 89
GED smart00302
Dynamin GTPase effector domain;
533-622 2.06e-17

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 78.43  E-value: 2.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165   533 QISCDEMHYHVQAYFKSLKERLSNQIPMIIQYYILHEFSEKLQNQMMQLIQEREKLNTLLAEKTDITRVRDNLSNRIERL 612
Cdd:smart00302   3 DSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLELL 82
                           90
                   ....*....|
gi 377520165   613 TAASHKLAKF 622
Cdd:smart00302  83 KKARQIIAAV 92
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
136-230 6.02e-04

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670  Cd Length: 179  Bit Score: 39.76  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  136 PDLTLIDLPG--ITRValpdqPKDIGQQIKKMIRKYIQRQETINLVVV-------PSNVDIattEALEMAREvdpNGERT 206
Cdd:TIGR03598  64 DGFRLVDLPGygYAKV-----SKEEKEKWQKLIEEYLEKRENLKGVVLlmdirhpLKELDL---EMIEWLRE---RGIPV 132
                          90       100
                  ....*....|....*....|....
gi 377520165  207 LGILTKPDLVDRGAESDVVSVVRN 230
Cdd:TIGR03598 133 LIVLTKADKLKKSELNKQLKKIKK 156
engB PRK00454
GTP-binding protein YsxC; Reviewed
136-230 5.87e-03

GTP-binding protein YsxC; Reviewed


Pssm-ID: 234770  Cd Length: 196  Bit Score: 37.02  E-value: 5.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 136 PDLTLIDLPG--ITRValpdqPKDIGQQIKKMIRKYIQRQETINLVVV-------PSNVDIattEALEMArevDPNGERT 206
Cdd:PRK00454  70 DKLRLVDLPGygYAKV-----SKEEKEKWQKLIEEYLRTRENLKGVVLlidsrhpLKELDL---QMIEWL---KEYGIPV 138
                         90       100
                 ....*....|....*....|....
gi 377520165 207 LGILTKPDLVDRGAESDVVSVVRN 230
Cdd:PRK00454 139 LIVLTKADKLKKGERKKQLKKVRK 162
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
140-232 6.23e-03

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 223296  Cd Length: 200  Bit Score: 37.21  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 140 LIDLPG--ITRValpdqPKDIGQQIKKMIRKYIQRQETINLVVV-------PSNVDIattEALEMAREVDPNgerTLGIL 210
Cdd:COG0218   74 LVDLPGygYAKV-----PKEVKEKWKKLIEEYLEKRANLKGVVLlidarhpPKDLDR---EMIEFLLELGIP---VIVVL 142
                         90       100
                 ....*....|....*....|..
gi 377520165 211 TKPDLVDRGAESDVVSVVRNLV 232
Cdd:COG0218  143 TKADKLKKSERNKQLNKVAEEL 164
CrfC COG0699
Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, ...
119-455 1.21e-10

Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, recombination and repair];


Pssm-ID: 223771 [Multi-domain]  Cd Length: 546  Bit Score: 63.00  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 119 KGISDELISLEVISPDVPDLTLIDLPGITRVALPDQPKDIGQQIKKMIRKYIQRQETINLVVVPSNVDIATTEALEMARE 198
Cdd:COG0699   36 SGITEVIIELKIAAERLLQLTDVDLPGLRKVPLSLEPEDIAQEDELLDLGKIEIENALILLGIAPNADEEAELSIEVIRE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 199 VDPngertlgILTKPDLVDRGaesdvvsvvRNLVYSLQKGYMIVKCRGQLEIQENLSLKEALDNEQNFFKEHEH-----F 273
Cdd:COG0699  116 ADR-------VPTKINFLNGG---------TNLTLILGNGDVLVVDALETDIQLLKTALEALVKELEYFAEHPLledneK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 274 SVLLEEgnatiacLAEKLTNELVDHIVKTLP--ALDTQIRKKLNEAEEKLRNLGTSVPD--SETEKLRFLIDKITRFAGA 349
Cdd:COG0699  180 LVLLPY-------LKKLLSKILELHLRLLPKydKLQDVIQLSQDLFENEVLAVIQTLLKrlSELVRGARIRLNIILFSDL 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 350 I-INATQGDEEMTNGSLKLFTVIRKHFYFwESFIQTQSKSFQDKSRDDISE-----FENKYRGRELPGFISFKVFENIAR 423
Cdd:COG0699  253 EeVSDSPVLLKELASKGERPSLLSGLTLL-DTLVETPIGQFDTQINQLLRKliselVRILLKELESASSSPFPKLSEALE 331
                        330       340       350
                 ....*....|....*....|....*....|...
gi 377520165 424 GQIRCLEEPAMEKLKEVTEIVKAHFNQ-IAMKH 455
Cdd:COG0699  332 EVVNQLKNKVDSGLESGLLAIIDIEERyINTKH 364
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
34-304 2.81e-109

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: 332.67  E-value: 2.81e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  34 LPSIAVIGDQSSGKSSVLEALSGVT-LPRGSGIVTRCPLELKLKKATKSTTWSGKISYRDHELT----IASAAEVENQVK 108
Cdd:cd08771    3 LPQIVVVGDQSSGKSSVLEALVGRDfLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHLkskeFTDFEELREEIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 109 QAQNLMAGNGKGISDELISLEVISPDVPDLTLIDLPGITRVALPDQPKDIGQQIKKMIRKYIQRQETINLVVVPSNVDIA 188
Cdd:cd08771   83 KETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVDLA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 189 TTEALEMAREVDPNGERTLGILTKPDLVDRGAES-DVVSVVRNLVYSLQKGYMIVKCRGQLEIQENLSLKEALDNEQNFF 267
Cdd:cd08771  163 NSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAeDILLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEEFF 242
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 377520165 268 KEHEHFSvLLEEGNATIACLAEKLTNELVDHIVKTLP 304
Cdd:cd08771  243 ETHPWYK-LLPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
10-251 5.44e-103

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: 314.89  E-value: 5.44e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165    10 EEKIRPCIDLIDSLR-ALGVDKDLGLPSIAVIGDQSSGKSSVLEALSGVT-LPRGSGIVTRCPLELKLKKAtkSTTWSGK 87
Cdd:smart00053   1 MEELIPLVNKLQDAFsALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDfLPRGSGIVTRRPLILQLIKS--KTEYAEF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165    88 ISYRDHELTiaSAAEVENQVKQAQNLMAGNGKGISDELISLEVISPDVPDLTLIDLPGITRVALPDQPKDIGQQIKKMIR 167
Cdd:smart00053  79 LHCKGKKFT--DFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165   168 KYIQRQETINLVVVPSNVDIATTEALEMAREVDPNGERTLGILTKPDLVDRGaeSDVVSVVRNLVYSLQKGYMIVKCRGQ 247
Cdd:smart00053 157 QFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEG--TDARDILENKLLPLRRGYIGVVNRSQ 234

                   ....
gi 377520165   248 LEIQ 251
Cdd:smart00053 235 KDIE 238
Dynamin_M pfam01031
Dynamin central region; This region lies between the GTPase domain, see pfam00350, and the ...
225-511 1.56e-83

Dynamin central region; This region lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169.


Pssm-ID: 279383  Cd Length: 285  Bit Score: 265.92  E-value: 1.56e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  225 VSVVRNLVYSLQKGYMIVKCRGQLEIQENLSLKEALDNEQNFFKEHEHFSVLleEGNATIACLAEKLTNELVDHIVKTLP 304
Cdd:pfam01031   1 VDILRNRVIPLKLGYVGVVNRSQKDINGKKSIEEALQAEREFFETHPAYRLL--ADRCGTPYLAKKLNQILVNHIRKSLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  305 ALDTQIRKKLNEAEEKLRNLGTSVPdSETEKLRFLIDKITRFAGAIINATQGDEEMTNGSLKLFTVIRkhFYFWESFIQT 384
Cdd:pfam01031  79 DLKKKINELLQKLEKELEKYGPGIP-SPAEKGKFLLQIITKFNEDFKNLIDGEEVSDTNELSGGARIR--YIFNEIFPKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  385 QSK--SFQDKSRDDISEFENKYRGRELPGFISFKVFENIARGQIRCLEEPAMEKLKEVTEIVKAHFNQIAMKHFLAFPNL 462
Cdd:pfam01031 156 LEKidPLENLLDEEIRTAIRNSRGIRLPLFVPEKAFEVLVKQQIKRLEEPALKCVELVYEELERIVQKCLTPELKRFPNL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 377520165  463 YRGAKVRIEDICHKQVWEAERTIRTQFKMEK-IIYCQDRLYSGRLNEVRS 511
Cdd:pfam01031 236 RDEIKEVVEDLLRERLEPTKKMIRNLIDMELaYINTNHPDFIGGLNAIRE 285
Dynamin_N pfam00350
Dynamin family;
37-213 1.37e-59

Dynamin family;


Pssm-ID: 278765  Cd Length: 168  Bit Score: 198.21  E-value: 1.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165   37 IAVIGDQSSGKSSVLEALSGVT-LPRGSGIVTRCPLELKLKKATKSTTWSGKISYRDHELTIASAAEVENQVKQAQNLMA 115
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDiLPRGPGPTTRRPLVLRLGESPGASEGAVKVEYKDGLKKFEDFSELREEIENETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  116 GNGKGISDELISLEVISPDVPDLTLIDLPGITRVALPDQpkdigqqikKMIRKYIQRqETINLVVVPSNVDIATTEALEM 195
Cdd:pfam00350  81 GTGKGVSSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYIKP-ADIILAVTPANVDLSTSEALFL 150
                         170
                  ....*....|....*...
gi 377520165  196 AREVDPNGERTLGILTKP 213
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
534-622 1.50e-19

Dynamin GTPase effector domain;


Pssm-ID: 280391  Cd Length: 89  Bit Score: 84.09  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  534 ISCDEMHYHVQAYFKSLKERLSNQIPMIIQYYILHEFSEKLQNQMMQLIQEREKLNTLLAEKTDITRVRDNLSNRIERLT 613
Cdd:pfam02212   1 SEVEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKDSLQKELLAQLYKSELLDELLKEDPEIAQKRKELKKRLEALK 80

                  ....*....
gi 377520165  614 AASHKLAKF 622
Cdd:pfam02212  81 QAREILSEV 89
GED smart00302
Dynamin GTPase effector domain;
533-622 2.06e-17

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 78.43  E-value: 2.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165   533 QISCDEMHYHVQAYFKSLKERLSNQIPMIIQYYILHEFSEKLQNQMMQLIQEREKLNTLLAEKTDITRVRDNLSNRIERL 612
Cdd:smart00302   3 DSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLELL 82
                           90
                   ....*....|
gi 377520165   613 TAASHKLAKF 622
Cdd:smart00302  83 KKARQIIAAV 92
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
136-242 4.13e-06

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 45.96  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 136 PDLTLIDLPG--ITRValpdqPKDIGQQIKKMIRKYIQRQETINLVVV-------PSNVDIattEALEMAREVDPNgerT 206
Cdd:cd01876   45 DKFRLVDLPGygYAKV-----SKEVREKWGKLIEEYLENRENLKGVVLlidarhgPTPIDL---EMLEFLEELGIP---F 113
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 377520165 207 LGILTKPDLVDRGAESDVVSVVRNLVYSLQKGYMIV 242
Cdd:cd01876  114 LIVLTKADKLKKSELAKVLKKIKEELNLFNILPPVI 149
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
136-230 6.02e-04

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670  Cd Length: 179  Bit Score: 39.76  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165  136 PDLTLIDLPG--ITRValpdqPKDIGQQIKKMIRKYIQRQETINLVVV-------PSNVDIattEALEMAREvdpNGERT 206
Cdd:TIGR03598  64 DGFRLVDLPGygYAKV-----SKEEKEKWQKLIEEYLEKRENLKGVVLlmdirhpLKELDL---EMIEWLRE---RGIPV 132
                          90       100
                  ....*....|....*....|....
gi 377520165  207 LGILTKPDLVDRGAESDVVSVVRN 230
Cdd:TIGR03598 133 LIVLTKADKLKKSELNKQLKKIKK 156
engB PRK00454
GTP-binding protein YsxC; Reviewed
136-230 5.87e-03

GTP-binding protein YsxC; Reviewed


Pssm-ID: 234770  Cd Length: 196  Bit Score: 37.02  E-value: 5.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 136 PDLTLIDLPG--ITRValpdqPKDIGQQIKKMIRKYIQRQETINLVVV-------PSNVDIattEALEMArevDPNGERT 206
Cdd:PRK00454  70 DKLRLVDLPGygYAKV-----SKEEKEKWQKLIEEYLRTRENLKGVVLlidsrhpLKELDL---QMIEWL---KEYGIPV 138
                         90       100
                 ....*....|....*....|....
gi 377520165 207 LGILTKPDLVDRGAESDVVSVVRN 230
Cdd:PRK00454 139 LIVLTKADKLKKGERKKQLKKVRK 162
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
140-232 6.23e-03

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 223296  Cd Length: 200  Bit Score: 37.21  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 140 LIDLPG--ITRValpdqPKDIGQQIKKMIRKYIQRQETINLVVV-------PSNVDIattEALEMAREVDPNgerTLGIL 210
Cdd:COG0218   74 LVDLPGygYAKV-----PKEVKEKWKKLIEEYLEKRANLKGVVLlidarhpPKDLDR---EMIEFLLELGIP---VIVVL 142
                         90       100
                 ....*....|....*....|..
gi 377520165 211 TKPDLVDRGAESDVVSVVRNLV 232
Cdd:COG0218  143 TKADKLKKSERNKQLNKVAEEL 164
CrfC COG0699
Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, ...
119-455 1.21e-10

Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, recombination and repair];


Pssm-ID: 223771 [Multi-domain]  Cd Length: 546  Bit Score: 63.00  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 119 KGISDELISLEVISPDVPDLTLIDLPGITRVALPDQPKDIGQQIKKMIRKYIQRQETINLVVVPSNVDIATTEALEMARE 198
Cdd:COG0699   36 SGITEVIIELKIAAERLLQLTDVDLPGLRKVPLSLEPEDIAQEDELLDLGKIEIENALILLGIAPNADEEAELSIEVIRE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 199 VDPngertlgILTKPDLVDRGaesdvvsvvRNLVYSLQKGYMIVKCRGQLEIQENLSLKEALDNEQNFFKEHEH-----F 273
Cdd:COG0699  116 ADR-------VPTKINFLNGG---------TNLTLILGNGDVLVVDALETDIQLLKTALEALVKELEYFAEHPLledneK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 274 SVLLEEgnatiacLAEKLTNELVDHIVKTLP--ALDTQIRKKLNEAEEKLRNLGTSVPD--SETEKLRFLIDKITRFAGA 349
Cdd:COG0699  180 LVLLPY-------LKKLLSKILELHLRLLPKydKLQDVIQLSQDLFENEVLAVIQTLLKrlSELVRGARIRLNIILFSDL 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377520165 350 I-INATQGDEEMTNGSLKLFTVIRKHFYFwESFIQTQSKSFQDKSRDDISE-----FENKYRGRELPGFISFKVFENIAR 423
Cdd:COG0699  253 EeVSDSPVLLKELASKGERPSLLSGLTLL-DTLVETPIGQFDTQINQLLRKliselVRILLKELESASSSPFPKLSEALE 331
                        330       340       350
                 ....*....|....*....|....*....|...
gi 377520165 424 GQIRCLEEPAMEKLKEVTEIVKAHFNQ-IAMKH 455
Cdd:COG0699  332 EVVNQLKNKVDSGLESGLLAIIDIEERyINTKH 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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