NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|442618987|ref|NP_001262555|]
View 

uncharacterized protein Dmel_CG9297, isoform E [Drosophila melanogaster]

Protein Classification

sarcalumenin( domain architecture ID 11245857)

sarcalumenin (SAR), a Ca(2+)-binding protein located in the longitudinal sarcoplasmic reticulum (SR), regulates Ca(2+) reuptake into the SR by interacting with cardiac sarco(endo)plasmic reticulum Ca(2+)-ATPase 2a (SERCA2a); belongs to the TRAFAC class dynamin-like GTPase

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 574-813 4.27e-117

Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling.


:

Pssm-ID: 206740  Cd Length: 241  Bit Score: 357.74  E-value: 4.27e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 574 LILFMGPWSGGKSSILNYLTDNEYTpnSLRTGAEPSPAYFNILMWGNETEVLDGTQLAAD--YTFAGLQKFGQGLEERLR 651
Cdd:cd09913    1 MVLFLGQYSTGKSTFINYLLGQDYP--GLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDpdKPFRGLSKFGNGFLNKFE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 652 GLKMKSKILEKVNIVEIPGILEVRKQ-VSRVFPFNDACQWFIDRADIIFLVYDPAKLDVGPETEAILDQLKGREYQTRII 730
Cdd:cd09913   79 GSTLPHPLLESVTIVDTPGILSGEKQrQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 731 LNKADTVKPEELLRVQGALIWNISPLMSSAQPPLMYTTSLWTHPYQDGAPARLLLAQERAFLRDLRTAIDKRIEHKIASA 810
Cdd:cd09913  159 LNKADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDL 238


                 ...
gi 442618987 811 RRF 813
Cdd:cd09913  239 IKR 241
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
 539-570 9.08e-08

N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins.


:

Pssm-ID: 465295 [Multi-domain]  Cd Length: 33  Bit Score: 48.93  E-value: 9.08e-08
                          10        20        30
                  ....*....|....*....|....*....|..
gi 442618987  539 IKRIYENAVKPLETLYKYRDLSNRHFSDPEIF 570
Cdd:pfam16880   2 LKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 93-367 2.44e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 48.37  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987  93 DSTEDAKSANDLDGDGIPDDEDDDIDGDGIPNEKDDDIDGDGIPNDEDDDIDGDGIPNEDDDDIDGDGVPNSkDEDIDGD 172
Cdd:NF033609 611 DSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSD 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 173 GVPNSkDEDIDGDGKANHE-DDDLDGDgTPNHEDEDLDGDGVPNEEDDDLDGDGKINHEDEDLDGDGVKNDEDEDLDGDG 251
Cdd:NF033609 690 SDSDS-DSDSDSDSDSDSDsDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 767

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 252 KVNHEDEDLDGDgvkNEKDDDLDGDGTNNSqDEDLDGDGVPNEKDDDLDGDGILNEHDGDVDGDGVPNEHDHKDSGENAD 331
Cdd:NF033609 768 SDSDSDSDSDSD---SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 843

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442618987 332 DDDDDDDEDDKEAvKKRSKREVDAAPVLDIEAPPSP 367
Cdd:NF033609 844 SDSDSDSDSDSDS-ESDSNSDSESGSNNNVVPPNSP 878
 
Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 574-813 4.27e-117

Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling.


Pssm-ID: 206740  Cd Length: 241  Bit Score: 357.74  E-value: 4.27e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 574 LILFMGPWSGGKSSILNYLTDNEYTpnSLRTGAEPSPAYFNILMWGNETEVLDGTQLAAD--YTFAGLQKFGQGLEERLR 651
Cdd:cd09913    1 MVLFLGQYSTGKSTFINYLLGQDYP--GLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDpdKPFRGLSKFGNGFLNKFE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 652 GLKMKSKILEKVNIVEIPGILEVRKQ-VSRVFPFNDACQWFIDRADIIFLVYDPAKLDVGPETEAILDQLKGREYQTRII 730
Cdd:cd09913   79 GSTLPHPLLESVTIVDTPGILSGEKQrQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 731 LNKADTVKPEELLRVQGALIWNISPLMSSAQPPLMYTTSLWTHPYQDGAPARLLLAQERAFLRDLRTAIDKRIEHKIASA 810
Cdd:cd09913  159 LNKADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDL 238


                 ...
gi 442618987 811 RRF 813
Cdd:cd09913  239 IKR 241
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
 539-570 9.08e-08

N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins.


Pssm-ID: 465295 [Multi-domain]  Cd Length: 33  Bit Score: 48.93  E-value: 9.08e-08
                          10        20        30
                  ....*....|....*....|....*....|..
gi 442618987  539 IKRIYENAVKPLETLYKYRDLSNRHFSDPEIF 570
Cdd:pfam16880   2 LKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 93-367 2.44e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 48.37  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987  93 DSTEDAKSANDLDGDGIPDDEDDDIDGDGIPNEKDDDIDGDGIPNDEDDDIDGDGIPNEDDDDIDGDGVPNSkDEDIDGD 172
Cdd:NF033609 611 DSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSD 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 173 GVPNSkDEDIDGDGKANHE-DDDLDGDgTPNHEDEDLDGDGVPNEEDDDLDGDGKINHEDEDLDGDGVKNDEDEDLDGDG 251
Cdd:NF033609 690 SDSDS-DSDSDSDSDSDSDsDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 767

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 252 KVNHEDEDLDGDgvkNEKDDDLDGDGTNNSqDEDLDGDGVPNEKDDDLDGDGILNEHDGDVDGDGVPNEHDHKDSGENAD 331
Cdd:NF033609 768 SDSDSDSDSDSD---SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 843

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442618987 332 DDDDDDDEDDKEAvKKRSKREVDAAPVLDIEAPPSP 367
Cdd:NF033609 844 SDSDSDSDSDSDS-ESDSNSDSESGSNNNVVPPNSP 878
Dynamin_N pfam00350
Dynamin family;
575-701 2.40e-04

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 42.60  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987  575 ILFMGPWSGGKSSILNYLTDNEYTPnslrTGAEPSPAYFNILMWGNETEVLDGTQLAADYTF-AGLQKFGQGLEERLRG- 652
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILP----RGPGPTTRRPTVLRLGESPGASEGAVKVEYKDGeKKFEDFSELREEIEKEt 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442618987  653 ----------------LKMKSKILEKVNIVEIPGIL--EVRKQvsrvfpfnDACQWFIDRADIIFLV 701
Cdd:pfam00350  77 ekiagtgkgissepivLEILSPLVPGLTLVDTPGLDsvAVGDQ--------ELTKEYIKPADIILAV 135
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
695-743 7.41e-04

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 42.67  E-value: 7.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442618987 695 ADIIFLVYDPAKlDVGPETEAILDQLKgrEYQTRIIL--NKADTVKPEELL 743
Cdd:COG1159   83 VDVILFVVDATE-KIGEGDEFILELLK--KLKTPVILviNKIDLVKKEELL 130
 
Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 574-813 4.27e-117

Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling.


Pssm-ID: 206740  Cd Length: 241  Bit Score: 357.74  E-value: 4.27e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 574 LILFMGPWSGGKSSILNYLTDNEYTpnSLRTGAEPSPAYFNILMWGNETEVLDGTQLAAD--YTFAGLQKFGQGLEERLR 651
Cdd:cd09913    1 MVLFLGQYSTGKSTFINYLLGQDYP--GLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDpdKPFRGLSKFGNGFLNKFE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 652 GLKMKSKILEKVNIVEIPGILEVRKQ-VSRVFPFNDACQWFIDRADIIFLVYDPAKLDVGPETEAILDQLKGREYQTRII 730
Cdd:cd09913   79 GSTLPHPLLESVTIVDTPGILSGEKQrQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 731 LNKADTVKPEELLRVQGALIWNISPLMSSAQPPLMYTTSLWTHPYQDGAPARLLLAQERAFLRDLRTAIDKRIEHKIASA 810
Cdd:cd09913  159 LNKADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDL 238


                 ...
gi 442618987 811 RRF 813
Cdd:cd09913  239 IKR 241
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
 539-570 9.08e-08

N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins.


Pssm-ID: 465295 [Multi-domain]  Cd Length: 33  Bit Score: 48.93  E-value: 9.08e-08
                          10        20        30
                  ....*....|....*....|....*....|..
gi 442618987  539 IKRIYENAVKPLETLYKYRDLSNRHFSDPEIF 570
Cdd:pfam16880   2 LKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 93-367 2.44e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 48.37  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987  93 DSTEDAKSANDLDGDGIPDDEDDDIDGDGIPNEKDDDIDGDGIPNDEDDDIDGDGIPNEDDDDIDGDGVPNSkDEDIDGD 172
Cdd:NF033609 611 DSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSD 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 173 GVPNSkDEDIDGDGKANHE-DDDLDGDgTPNHEDEDLDGDGVPNEEDDDLDGDGKINHEDEDLDGDGVKNDEDEDLDGDG 251
Cdd:NF033609 690 SDSDS-DSDSDSDSDSDSDsDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 767

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 252 KVNHEDEDLDGDgvkNEKDDDLDGDGTNNSqDEDLDGDGVPNEKDDDLDGDGILNEHDGDVDGDGVPNEHDHKDSGENAD 331
Cdd:NF033609 768 SDSDSDSDSDSD---SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 843

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442618987 332 DDDDDDDEDDKEAvKKRSKREVDAAPVLDIEAPPSP 367
Cdd:NF033609 844 SDSDSDSDSDSDS-ESDSNSDSESGSNNNVVPPNSP 878
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 576-755 2.58e-05

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 45.53  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 576 LFMGPWSGGKSSILNYLTDNEYTPNSLRTGaepspayfnilmwgnETEVLDgtqlaadytfaglqkfgqgleerlRGLKM 655
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPG---------------TTRDPD------------------------VYVKE 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987 656 KSKILEKVNIVEIPGILEVRKQVSRvfpfnDACQWFIDRADIIFLVYDPAKLDVGPE-TEAILDQLKGREYQTRIILNKA 734
Cdd:cd00882   42 LDKGKVKLVLVDTPGLDEFGGLGRE-----ELARLLLRGADLILLVVDSTDRESEEDaKLLILRRLRKEGIPIILVGNKI 116

                        170       180
                 ....*....|....*....|.
gi 442618987 735 DTVKPEELLRVQGALIWNISP 755
Cdd:cd00882  117 DLLEEREVEELLRLEELAKIL 137
Dynamin_N pfam00350
Dynamin family;
575-701 2.40e-04

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 42.60  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618987  575 ILFMGPWSGGKSSILNYLTDNEYTPnslrTGAEPSPAYFNILMWGNETEVLDGTQLAADYTF-AGLQKFGQGLEERLRG- 652
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILP----RGPGPTTRRPTVLRLGESPGASEGAVKVEYKDGeKKFEDFSELREEIEKEt 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442618987  653 ----------------LKMKSKILEKVNIVEIPGIL--EVRKQvsrvfpfnDACQWFIDRADIIFLV 701
Cdd:pfam00350  77 ekiagtgkgissepivLEILSPLVPGLTLVDTPGLDsvAVGDQ--------ELTKEYIKPADIILAV 135
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
695-743 7.41e-04

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 42.67  E-value: 7.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442618987 695 ADIIFLVYDPAKlDVGPETEAILDQLKgrEYQTRIIL--NKADTVKPEELL 743
Cdd:COG1159   83 VDVILFVVDATE-KIGEGDEFILELLK--KLKTPVILviNKIDLVKKEELL 130
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH