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Conserved domains on  [gi|1707052555|ref|NP_001358562|]
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sarcalumenin isoform 1 precursor [Rattus norvegicus]

Protein Classification

EHD domain-containing protein; EHD domain-containing protein; EHD_N and EHD domain-containing protein; sarcalumenin; EHD_N and EHD domain-containing protein( domain architecture ID 13454768)

EHD domain-containing protein; EHD domain-containing protein; protein containing domains PHA02664, EHD_N, and EHD; 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; protein containing domains PHA02664, EHD_N, and EHD

Graphical summary

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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 ...
 526-767 4.55e-152

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: 447.11  E-value: 4.55e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 526 MVLFLGPWSVGKSTMINYLLGLEDTryQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMAADSARSFSPLEKFGQNFLEKLI 605
Cdd:cd09913     1 MVLFLGQYSTGKSTFINYLLGQDYP--GLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 606 GIEVPHKLLERVTFVDTPGIIENRKQ-QERGYPFNDVCQWFIDRADLIFVVFDPTKLDVGLELEMLFRQLKGRESQIRII 684
Cdd:cd09913    79 GSTLPHPLLESVTIVDTPGILSGEKQrQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 685 LNKADNLATQMLMRVYGALFWSLAPLINVTEPPRVYVSSFWPQDYKPDTHRDLFLKEEISLLEDLNQVIENRLENKIAFI 764
Cdd:cd09913   159 LNKADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDL 238


                  ...
gi 1707052555 765 RQH 767
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 ...
 490-522 6.17e-10

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: 54.71  E-value: 6.17e-10
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1707052555 490 RLRKIYHTSIKPLEQSYKYNELRQHEITDGEIT 522
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 271-483 3.67e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 51.15  E-value: 3.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  271 DPHAVSDMASSEVGAEEDAEdskAEVDAETGEEAEDQGEPRPSLEAGSARE--ASEKSEDTQSSEVRETEGQASGMSEED 348
Cdd:TIGR00927  637 EAEHTGERTGEEGERPTEAE---GENGEESGGEAEQEGETETKGENESEGEipAERKGEQEGEGEIEAKEADHKGETEAE 713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  349 LAEASSEEEGGEEDGRENGGLPSKEESGEDSGDG-ASSEEEGSTSGEAAEPQKTPRATGHEEEG-------AQLDVE-DL 419
Cdd:TIGR00927  714 EVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGeAEGKHEVETEGDRKETEHEGETEAEGKEDedegeiqAGEDGEmKG 793

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707052555  420 NTGSEGVKTQDTEAEASEERQQGRGNPVIAHQEEAEDVSEEAPMRDRSHIEKTlmlNEDKPADD 483
Cdd:TIGR00927  794 DEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAK---QDEKGVDG 854
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 76-309 7.52e-06

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.98  E-value: 7.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  76 AESFEQPPAGAPSTANGQGSESEASlSNSSAAESAPPGDVEGPGEEEEGPHAAGTLPPGGAEGPEERPEFSSGEEAGQEE 155
Cdd:PRK07764  594 AAGGEGPPAPASSGPPEEAARPAAP-AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAK 672

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 156 AGVGLPTEGAANMEAEAQEELQGRlgdgpmeeaaagaaepVAPQSTEGEEAEGEGSIGSDHQSTELDGAQDAIPAGEDSD 235
Cdd:PRK07764  673 AGGAAPAAPPPAPAPAAPAAPAGA----------------APAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAAD 736

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707052555 236 ADVAAEAREEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSDMASSEVGAEEDAEdskaEVDAETGEEAEDQGE 309
Cdd:PRK07764  737 DPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAP----SMDDEDRRDAEEVAM 806
 
Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 526-767 4.55e-152

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: 447.11  E-value: 4.55e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 526 MVLFLGPWSVGKSTMINYLLGLEDTryQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMAADSARSFSPLEKFGQNFLEKLI 605
Cdd:cd09913     1 MVLFLGQYSTGKSTFINYLLGQDYP--GLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 606 GIEVPHKLLERVTFVDTPGIIENRKQ-QERGYPFNDVCQWFIDRADLIFVVFDPTKLDVGLELEMLFRQLKGRESQIRII 684
Cdd:cd09913    79 GSTLPHPLLESVTIVDTPGILSGEKQrQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 685 LNKADNLATQMLMRVYGALFWSLAPLINVTEPPRVYVSSFWPQDYKPDTHRDLFLKEEISLLEDLNQVIENRLENKIAFI 764
Cdd:cd09913   159 LNKADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDL 238


                  ...
gi 1707052555 765 RQH 767
Cdd:cd09913   239 IKR 241
Dynamin_N pfam00350
Dynamin family;
527-688 3.60e-15

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 74.19  E-value: 3.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 527 VLFLGPWSVGKSTMINYLLGLEdtryQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMA--ADSARSFSPLEKFGQNF---- 600
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRD----ILPRGPGPTTRRPTVLRLGESPGASEGAVKVeyKDGEKKFEDFSELREEIeket 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 601 ----------LEKLIGIEVPHKLLERVTFVDTPGIIENRKQQErgypfnDVCQWFIDRADLIFVVFDPTKLDVGLELEML 670
Cdd:pfam00350  77 ekiagtgkgiSSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ------ELTKEYIKPADIILAVTPANVDLSTSEALFL 150

                         170
                  ....*....|....*...
gi 1707052555 671 FRQLKGRESQIRIILNKA 688
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
 490-522 6.17e-10

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: 54.71  E-value: 6.17e-10
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1707052555 490 RLRKIYHTSIKPLEQSYKYNELRQHEITDGEIT 522
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 271-483 3.67e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 51.15  E-value: 3.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  271 DPHAVSDMASSEVGAEEDAEdskAEVDAETGEEAEDQGEPRPSLEAGSARE--ASEKSEDTQSSEVRETEGQASGMSEED 348
Cdd:TIGR00927  637 EAEHTGERTGEEGERPTEAE---GENGEESGGEAEQEGETETKGENESEGEipAERKGEQEGEGEIEAKEADHKGETEAE 713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  349 LAEASSEEEGGEEDGRENGGLPSKEESGEDSGDG-ASSEEEGSTSGEAAEPQKTPRATGHEEEG-------AQLDVE-DL 419
Cdd:TIGR00927  714 EVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGeAEGKHEVETEGDRKETEHEGETEAEGKEDedegeiqAGEDGEmKG 793

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707052555  420 NTGSEGVKTQDTEAEASEERQQGRGNPVIAHQEEAEDVSEEAPMRDRSHIEKTlmlNEDKPADD 483
Cdd:TIGR00927  794 DEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAK---QDEKGVDG 854
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 76-309 7.52e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.98  E-value: 7.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  76 AESFEQPPAGAPSTANGQGSESEASlSNSSAAESAPPGDVEGPGEEEEGPHAAGTLPPGGAEGPEERPEFSSGEEAGQEE 155
Cdd:PRK07764  594 AAGGEGPPAPASSGPPEEAARPAAP-AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAK 672

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 156 AGVGLPTEGAANMEAEAQEELQGRlgdgpmeeaaagaaepVAPQSTEGEEAEGEGSIGSDHQSTELDGAQDAIPAGEDSD 235
Cdd:PRK07764  673 AGGAAPAAPPPAPAPAAPAAPAGA----------------APAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAAD 736

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707052555 236 ADVAAEAREEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSDMASSEVGAEEDAEdskaEVDAETGEEAEDQGE 309
Cdd:PRK07764  737 DPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAP----SMDDEDRRDAEEVAM 806
PHA03169 PHA03169
hypothetical protein; Provisional
 260-462 1.27e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.81  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 260 AAPPGPDHQPTDPhavsdmassEVGAEEDAEDSKAEVDAETGEEaEDQGEPRPSLEAGSAREASEKSEDTQSSEVRETEG 339
Cdd:PHA03169   44 AKPAPPAPTTSGP---------QVRAVAEQGHRQTESDTETAEE-SRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 340 QASGMSEEDLAEASSEEEGGEEDGRENGGLPSKEESGEDSGDGASSEEEGS-----TSGEAAEPQKTPRATGHEEEGAQL 414
Cdd:PHA03169  114 LASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSsflqpSHEDSPEEPEPPTSEPEPDSPGPP 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1707052555 415 DVEDLNTGSEGVKTQDTEAEASEERQQGRGNP----VIAHQEEAEDVSEEAP 462
Cdd:PHA03169  194 QSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPntqqAVEHEDEPTEPEREGP 245
YeeP COG3596
Predicted GTPase [General function prediction only];
481-689 1.60e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.84  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 481 ADDYSAVLQRLRKIYHTSIKPLEQsykynELRQHEITDGEITskpmVLFLGPWSVGKSTMINYLLGLEDTRyqlyTGA-E 559
Cdd:COG3596     5 VSSLTERLEALKRLPQVLRELLAE-----ALERLLVELPPPV----IALVGKTGAGKSSLINALFGAEVAE----VGVgR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 560 PTTSEFTVlmhgpklktiegivmaadsarsfsplekfgqnflekligIEVPHKLLERVTFVDTPGI--IENRKQQERGYp 637
Cdd:COG3596    72 PCTREIQR---------------------------------------YRLESDGLPGLVLLDTPGLgeVNERDREYREL- 111

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1707052555 638 fndvcQWFIDRADLIFVVFDPTKLDVGLELEMLfRQLKGRESQIRII--LNKAD 689
Cdd:COG3596   112 -----RELLPEADLILWVVKADDRALATDEEFL-QALRAQYPDPPVLvvLTQVD 159
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 42-321 6.98e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 46.91  E-value: 6.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555   42 SAGDASLEEKERALYADAapgdknlllhyPDGREAESFEQPPAGAPSTANgqgSESEASLSNSSAAESAPPGDVEGPGEE 121
Cdd:TIGR00927  640 HTGERTGEEGERPTEAEG-----------ENGEESGGEAEQEGETETKGE---NESEGEIPAERKGEQEGEGEIEAKEAD 705

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  122 EEGPHAAGTLPPGG---AEGPEERPEFSSGEEAGQEEagvglpTEGAANMEAEAQEELQGRLGDGPMEEAAAGAAEPVAP 198
Cdd:TIGR00927  706 HKGETEAEEVEHEGeteAEGTEDEGEIETGEEGEEVE------DEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDED 779

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  199 Q-STEGEEAEGEGSIGSDHQSTELDGAQDAIPAGEDSDADVAAEAREEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSD 277
Cdd:TIGR00927  780 EgEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSD 859

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1707052555  278 MASSEVGAEEDAEDSKAEVDAETGEEAEDQGEPRPSLEAGSARE 321
Cdd:TIGR00927  860 GGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQ 903
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
 277-354 5.38e-04

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 43.63  E-value: 5.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707052555 277 DMASSEVGAEEDAEDSKAEVDAETGEEAEDQGEPRPSLEAGSAREASEKSEDTQSS-EVRETEGQASGMSEEDLAEASS 354
Cdd:COG4547   206 DLAEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAEEgESEAAEAESDEMAEEAEGEDSE 284
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 213-462 1.90e-03

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: 42.20  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 213 GSDHQSTELDGAQDAIPAGEDSDADVAAEAREEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSDMAS------------ 280
Cdd:NF033609  613 ASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdsdsdsdsds 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 281 -----SEVGAEEDAE-DSKAEVDAETGEEAEDQGEPRPSLEAGSAREA-------SEKSEDTQSSEVRETEGQASGMSEE 347
Cdd:NF033609  693 dsdsdSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdsdsdSDSDSDSDSDSDSDSDSDSDSDSDS 772

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 348 DLAEASSEEEGGEEDGRENGGLPSKEESGEDSGDGASSEEEGSTSGEAAEPQKTPRATGHEEEGAQLDVEDLNTGSEGVK 427
Cdd:NF033609  773 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 852

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1707052555 428 TQDTEAEASEERQQGRGNPVI-----------AHQEEAEDVSEEAP 462
Cdd:NF033609  853 DSDSESDSNSDSESGSNNNVVppnspkngtnaSNKNEAKDSKEPLP 898
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 229-438 5.58e-03

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: 40.66  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 229 PAGEDSDADVAAEAREEAEDQPEDHSLPSEDAAPPGPDH-QPTDPHAVSDMAS-SEVGAEED-AEDSKAEVDAET---GE 302
Cdd:NF033609  556 PIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSaSDSDSASDSDSASdSDSASDSDsASDSDSASDSDSasdSD 635

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 303 EAEDQGEPRPSLEAGSAREASEKSEDTQSSEVRETEGQASGMSEEDLAEASSEEEGGEEDGRENGGLPSKEESGEDSGDG 382
Cdd:NF033609  636 SASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 715

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1707052555 383 ASSEEEGSTSGEAAEPQKTPRATGHEEEGAQLDVEDLNTGSEGVKTQDTEAEASEE 438
Cdd:NF033609  716 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 771
era PRK00089
GTPase Era; Reviewed
 526-694 6.71e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 39.65  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 526 MVLFLGPWSVGKSTMINYLLGlED----------TRyqlytgaepttseftvlmhgpklKTIEGIVMAADSarsfsplek 595
Cdd:PRK00089    7 FVAIVGRPNVGKSTLLNALVG-QKisivspkpqtTR-----------------------HRIRGIVTEDDA--------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 596 fgQnflekLIgievphkllervtFVDTPGIIENRKQQERGypFNDVCQWFIDRADLIFVVFDPTKlDVGLELEMLFRQLK 675
Cdd:PRK00089   54 --Q-----II-------------FVDTPGIHKPKRALNRA--MNKAAWSSLKDVDLVLFVVDADE-KIGPGDEFILEKLK 110

                         170
                  ....*....|....*....
gi 1707052555 676 GRESQIRIILNKADNLATQ 694
Cdd:PRK00089  111 KVKTPVILVLNKIDLVKDK 129
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 213-438 9.95e-03

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: 39.89  E-value: 9.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 213 GSDHQS-TELDGAQDAIPAgEDSDADVAAEAREEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSDMASSEVGAEEDAED 291
Cdd:NF033609  583 GSDSTSdSGSDSASDSDSA-SDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSD 661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 292 SKAEVDAETGEEAEDQGEPRPSLEAGSAREA-----SEKSEDTQSSEVRETEGQASGMSEEDLAEASSEEEGGEEDGREN 366
Cdd:NF033609  662 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 741

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1707052555 367 GGLPSKEESGEDSGDGASSEEEGSTSGEAAEPQKTPRATGHEEEGAQLDVEDLNTGSEGVKTQDTEAEASEE 438
Cdd:NF033609  742 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 813
 
Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 526-767 4.55e-152

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: 447.11  E-value: 4.55e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 526 MVLFLGPWSVGKSTMINYLLGLEDTryQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMAADSARSFSPLEKFGQNFLEKLI 605
Cdd:cd09913     1 MVLFLGQYSTGKSTFINYLLGQDYP--GLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 606 GIEVPHKLLERVTFVDTPGIIENRKQ-QERGYPFNDVCQWFIDRADLIFVVFDPTKLDVGLELEMLFRQLKGRESQIRII 684
Cdd:cd09913    79 GSTLPHPLLESVTIVDTPGILSGEKQrQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 685 LNKADNLATQMLMRVYGALFWSLAPLINVTEPPRVYVSSFWPQDYKPDTHRDLFLKEEISLLEDLNQVIENRLENKIAFI 764
Cdd:cd09913   159 LNKADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDL 238


                  ...
gi 1707052555 765 RQH 767
Cdd:cd09913   239 IKR 241
Dynamin_N pfam00350
Dynamin family;
527-688 3.60e-15

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 74.19  E-value: 3.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 527 VLFLGPWSVGKSTMINYLLGLEdtryQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMA--ADSARSFSPLEKFGQNF---- 600
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRD----ILPRGPGPTTRRPTVLRLGESPGASEGAVKVeyKDGEKKFEDFSELREEIeket 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 601 ----------LEKLIGIEVPHKLLERVTFVDTPGIIENRKQQErgypfnDVCQWFIDRADLIFVVFDPTKLDVGLELEML 670
Cdd:pfam00350  77 ekiagtgkgiSSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ------ELTKEYIKPADIILAVTPANVDLSTSEALFL 150

                         170
                  ....*....|....*...
gi 1707052555 671 FRQLKGRESQIRIILNKA 688
Cdd:pfam00350 151 AREVDPNGKRTIGVLTKA 168
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
 490-522 6.17e-10

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: 54.71  E-value: 6.17e-10
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1707052555 490 RLRKIYHTSIKPLEQSYKYNELRQHEITDGEIT 522
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 527-757 6.53e-10

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. 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 mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 59.10  E-value: 6.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 527 VLFLGPWSVGKSTMINYLLGLEdtryQLYTGAEPTTSEFTVLMHGpklktiegivmaadsarsfsplekfgqnfleklig 606
Cdd:cd09912     3 LAVVGEFSAGKSTLLNALLGEE----VLPTGVTPTTAVITVLRYG----------------------------------- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 607 ievphkLLERVTFVDTPGIIENRKQQErgypfnDVCQWFIDRADLIFVVFD---PTKLDvglELEmLFRQLKGRE-SQIR 682
Cdd:cd09912    44 ------LLKGVVLVDTPGLNSTIEHHT------EITESFLPRADAVIFVLSadqPLTES---ERE-FLKEILKWSgKKIF 107

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707052555 683 IILNKADNLATQMLMRVYGALFWSLAPLINVTEPPRVY-VSSFWPQDYKPDTHRDLFLKEEISLLEDLnqvIENRL 757
Cdd:cd09912   108 FVLNKIDLLSEEELEEVLEYSREELGVLELGGGEPRIFpVSAKEALEARLQGDEELLEQSGFEELEEH---LEEFL 180
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 528-715 2.18e-09

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: 57.08  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 528 LFLGPWSVGKSTMINYLLGLEdtrYQLYTGAEPTTSEFTVLMHGPklktiegivmaadsarsfsplekfgqnflekligi 607
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGE---VGEVSDVPGTTRDPDVYVKEL----------------------------------- 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 608 evpHKLLERVTFVDTPGIIENRKQQERgypfnDVCQWFIDRADLIFVVFDPTKLDVGLELEML-FRQLKGRESQIRIILN 686
Cdd:cd00882    43 ---DKGKVKLVLVDTPGLDEFGGLGRE-----ELARLLLRGADLILLVVDSTDRESEEDAKLLiLRRLRKEGIPIILVGN 114

                         170       180
                  ....*....|....*....|....*....
gi 1707052555 687 KADNLATQMLMRVYGALFWSLAPLINVTE 715
Cdd:cd00882   115 KIDLLEEREVEELLRLEELAKILGVPVFE 143
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 529-691 3.53e-07

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 50.71  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 529 FLGPWSVGKSTMINYLLGledtRYQLYTGAEP-TTSEftvlmhgPKLKtiegivmaadsarsfsplekfgqnflekligi 607
Cdd:cd00880     2 IFGRPNVGKSSLLNALLG----QNVGIVSPIPgTTRD-------PVRK-------------------------------- 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 608 EVPHKLLERVTFVDTPGIIENRkqqERGYPFNDVCQWFIDRADLIFVVFDPTKLDVglELEMLFRQLKGRESQIRIILNK 687
Cdd:cd00880    39 EWELLPLGPVVLIDTPGLDEEG---GLGRERVEEARQVADRADLVLLVVDSDLTPV--EEEAKLGLLRERGKPVLLVLNK 113


                  ....
gi 1707052555 688 ADNL 691
Cdd:cd00880   114 IDLV 117
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 527-687 2.43e-06

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 47.23  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 527 VLFLGPWSVGKSTMINYLLGLEdtryqLYTGAEP-TTseftvlmhgpkLKTIEGIVMAADsarsfsplekfgqnflekli 605
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAK-----AIVSDYPgTT-----------RDPNEGRLELKG-------------------- 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 606 gievphkllERVTFVDTPGIIENRKQQE-RGYPFNDvcqwfIDRADLIFVVFDPTKlDVGLELEMLFRQLKGRESQIRII 684
Cdd:pfam01926  46 ---------KQIILVDTPGLIEGASEGEgLGRAFLA-----IIEADLILFVVDSEE-GITPLDEELLELLRENKKPIILV 110


                  ...
gi 1707052555 685 LNK 687
Cdd:pfam01926 111 LNK 113
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 271-483 3.67e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 51.15  E-value: 3.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  271 DPHAVSDMASSEVGAEEDAEdskAEVDAETGEEAEDQGEPRPSLEAGSARE--ASEKSEDTQSSEVRETEGQASGMSEED 348
Cdd:TIGR00927  637 EAEHTGERTGEEGERPTEAE---GENGEESGGEAEQEGETETKGENESEGEipAERKGEQEGEGEIEAKEADHKGETEAE 713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  349 LAEASSEEEGGEEDGRENGGLPSKEESGEDSGDG-ASSEEEGSTSGEAAEPQKTPRATGHEEEG-------AQLDVE-DL 419
Cdd:TIGR00927  714 EVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGeAEGKHEVETEGDRKETEHEGETEAEGKEDedegeiqAGEDGEmKG 793

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707052555  420 NTGSEGVKTQDTEAEASEERQQGRGNPVIAHQEEAEDVSEEAPMRDRSHIEKTlmlNEDKPADD 483
Cdd:TIGR00927  794 DEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAK---QDEKGVDG 854
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 76-309 7.52e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.98  E-value: 7.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  76 AESFEQPPAGAPSTANGQGSESEASlSNSSAAESAPPGDVEGPGEEEEGPHAAGTLPPGGAEGPEERPEFSSGEEAGQEE 155
Cdd:PRK07764  594 AAGGEGPPAPASSGPPEEAARPAAP-AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAK 672

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 156 AGVGLPTEGAANMEAEAQEELQGRlgdgpmeeaaagaaepVAPQSTEGEEAEGEGSIGSDHQSTELDGAQDAIPAGEDSD 235
Cdd:PRK07764  673 AGGAAPAAPPPAPAPAAPAAPAGA----------------APAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAAD 736

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707052555 236 ADVAAEAREEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSDMASSEVGAEEDAEdskaEVDAETGEEAEDQGE 309
Cdd:PRK07764  737 DPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAP----SMDDEDRRDAEEVAM 806
PHA03169 PHA03169
hypothetical protein; Provisional
 260-462 1.27e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.81  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 260 AAPPGPDHQPTDPhavsdmassEVGAEEDAEDSKAEVDAETGEEaEDQGEPRPSLEAGSAREASEKSEDTQSSEVRETEG 339
Cdd:PHA03169   44 AKPAPPAPTTSGP---------QVRAVAEQGHRQTESDTETAEE-SRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 340 QASGMSEEDLAEASSEEEGGEEDGRENGGLPSKEESGEDSGDGASSEEEGS-----TSGEAAEPQKTPRATGHEEEGAQL 414
Cdd:PHA03169  114 LASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSsflqpSHEDSPEEPEPPTSEPEPDSPGPP 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1707052555 415 DVEDLNTGSEGVKTQDTEAEASEERQQGRGNP----VIAHQEEAEDVSEEAP 462
Cdd:PHA03169  194 QSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPntqqAVEHEDEPTEPEREGP 245
YeeP COG3596
Predicted GTPase [General function prediction only];
481-689 1.60e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.84  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 481 ADDYSAVLQRLRKIYHTSIKPLEQsykynELRQHEITDGEITskpmVLFLGPWSVGKSTMINYLLGLEDTRyqlyTGA-E 559
Cdd:COG3596     5 VSSLTERLEALKRLPQVLRELLAE-----ALERLLVELPPPV----IALVGKTGAGKSSLINALFGAEVAE----VGVgR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 560 PTTSEFTVlmhgpklktiegivmaadsarsfsplekfgqnflekligIEVPHKLLERVTFVDTPGI--IENRKQQERGYp 637
Cdd:COG3596    72 PCTREIQR---------------------------------------YRLESDGLPGLVLLDTPGLgeVNERDREYREL- 111

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1707052555 638 fndvcQWFIDRADLIFVVFDPTKLDVGLELEMLfRQLKGRESQIRII--LNKAD 689
Cdd:COG3596   112 -----RELLPEADLILWVVKADDRALATDEEFL-QALRAQYPDPPVLvvLTQVD 159
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 249-417 3.82e-05

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 47.28  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 249 QPEDHSLPSEDAAPPGPDHQPTDPhavSDMASSEVGAEeDAEDSKAEVDAETGEEAEDQGEPRPSLEAGSAREASEKseD 328
Cdd:PRK13108  297 EREPAELAAAAVASAASAVGPVGP---GEPNQPDDVAE-AVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEA--D 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 329 TQSSEVRETEGQASGMSEEDLAEASSEEEGGEEDGRENGGLPSKEESGEDSGDGASSEEEGSTSGEAAepqktPRATGHE 408
Cdd:PRK13108  371 IEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPG-----DDPAEPD 445


                  ....*....
gi 1707052555 409 EEGAQLDVE 417
Cdd:PRK13108  446 GIRRQDDFS 454
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 42-321 6.98e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 46.91  E-value: 6.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555   42 SAGDASLEEKERALYADAapgdknlllhyPDGREAESFEQPPAGAPSTANgqgSESEASLSNSSAAESAPPGDVEGPGEE 121
Cdd:TIGR00927  640 HTGERTGEEGERPTEAEG-----------ENGEESGGEAEQEGETETKGE---NESEGEIPAERKGEQEGEGEIEAKEAD 705

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  122 EEGPHAAGTLPPGG---AEGPEERPEFSSGEEAGQEEagvglpTEGAANMEAEAQEELQGRLGDGPMEEAAAGAAEPVAP 198
Cdd:TIGR00927  706 HKGETEAEEVEHEGeteAEGTEDEGEIETGEEGEEVE------DEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDED 779

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  199 Q-STEGEEAEGEGSIGSDHQSTELDGAQDAIPAGEDSDADVAAEAREEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSD 277
Cdd:TIGR00927  780 EgEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSD 859

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1707052555  278 MASSEVGAEEDAEDSKAEVDAETGEEAEDQGEPRPSLEAGSARE 321
Cdd:TIGR00927  860 GGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQ 903
PHA03169 PHA03169
hypothetical protein; Provisional
 281-446 1.09e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.73  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 281 SEVGAEEDAEDSKAEVDAETGEEAEDQGEPRPSLEAGSAREASEKSEDTQSSEVRETEGQASGMSEEDLAEASSEEEGGE 360
Cdd:PHA03169   91 GPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPS 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 361 EDGRENGGLPSKEESGEDSGDGasseEEGSTSGEAAEPQKTPRATGHEEEGAQLDVEDLNTGSEGvktqDTEAEASEERQ 440
Cdd:PHA03169  171 HEDSPEEPEPPTSEPEPDSPGP----PQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAV----EHEDEPTEPER 242


                  ....*.
gi 1707052555 441 QGRGNP 446
Cdd:PHA03169  243 EGPPFP 248
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 609-689 1.20e-04

Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.


Pssm-ID: 206668 [Multi-domain]  Cd Length: 167  Bit Score: 43.54  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 609 VPHKLLERVTFVDTPGIIENRKQQE-RGYPFNDVcqwfIDRADLIFVVFDPTKLDVGL---ELEMLFRQLKGR-----ES 679
Cdd:cd01881    39 FEFGDGVDIQIIDLPGLLDGASEGRgLGEQILAH----LYRSDLILHVIDASEDCVGDpleDQKTLNEEVSGSflflkNK 114

                          90
                  ....*....|
gi 1707052555 680 QIRIILNKAD 689
Cdd:cd01881   115 PEMIVANKID 124
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 127-410 2.33e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 44.99  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  127 AAGTLPPGGAEGPEERPEFSSGEEAGQEEAGVGLPTEGAANMEAEAQEElqgrlGDGPMEEAAAGAAEPVAPQSTEGEEA 206
Cdd:TIGR00927  626 ALGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETE-----TKGENESEGEIPAERKGEQEGEGEIE 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  207 EGEGSIGSDHQSTELDGAQDAIPAGEDSDADVAAEAREEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSdmaSSEVGAE 286
Cdd:TIGR00927  701 AKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGET---EAEGKED 777

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  287 EDAEDSKAEVDAET--GEEAEDQGEPRPSLEAGSAREASEKSEDTQSSEVRETEGQASGMSEEDLAEASSEEeggeedgr 364
Cdd:TIGR00927  778 EDEGEIQAGEDGEMkgDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDE-------- 849

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1707052555  365 engglpsKEESGEDSGDGASSEEEGSTSGEAAEPQKTPRATGHEEE 410
Cdd:TIGR00927  850 -------KGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEE 888
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
509-689 3.11e-04

GTP-binding protein, GTP1/Obg family [General function prediction only];


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 44.05  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 509 NELRQ-HEItDGEItskPMVLFLGPWSVGKSTMINYLlgledtryqlyTGAEPTTSE--FTVlmhgpklKTIegivmaad 585
Cdd:COG1084   148 NKLRKlPDI-DPDL---PTIVVAGYPNVGKSSLVSKV-----------TSAKPEIASypFTT-------KGI-------- 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 586 sarsfsplekfgqnflekLIG-IEVPHkllERVTFVDTPGIIEnRKQQERgypfNDvcqwfIDR---------ADLIFVV 655
Cdd:COG1084   198 ------------------IVGhFERGH---GRYQVIDTPGLLD-RPLSER----NE-----IERqailalkhlADVILFL 246

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1707052555 656 FDPTKlDVGLELEM---LFRQLKGR-ESQIRIILNKAD 689
Cdd:COG1084   247 FDPSE-TCGYSLEEqlnLLEEIRSLfDVPVIVVINKID 283
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
 277-354 5.38e-04

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 43.63  E-value: 5.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707052555 277 DMASSEVGAEEDAEDSKAEVDAETGEEAEDQGEPRPSLEAGSAREASEKSEDTQSS-EVRETEGQASGMSEEDLAEASS 354
Cdd:COG4547   206 DLAEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAEEgESEAAEAESDEMAEEAEGEDSE 284
PTZ00121 PTZ00121
MAEBL; Provisional
 285-516 7.80e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 7.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  285 AEE--DAEDSKAEVDAETGEEAEDQGEPRPSLEAGSAREASEKSEDTQSSEVRETEGQASGMSEEDLAEASSEEEGGEED 362
Cdd:PTZ00121  1512 ADEakKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE 1591

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  363 GRENGGLPSKEESGEDSGDGASSEEEGSTSGE----AAEPQKTPRATGHEEEGAQLDVEDLNTGSEGVKTQdTEAEASEE 438
Cdd:PTZ00121  1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK-AAEEAKKA 1670

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707052555  439 RQQGRGNPVIAHQEEAEDVSEEAPMRDRSHIEKTlmlnedkpaddysavlQRLRKIYHTSIKPLEQSYKYNELRQHEI 516
Cdd:PTZ00121  1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA----------------EELKKKEAEEKKKAEELKKAEEENKIKA 1732
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 635-690 8.53e-04

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 41.88  E-value: 8.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1707052555 635 GYPFNDVCQWFIDRADLIFVVFDPT--KLDVGLELEMLFRQLKGRESQIRIILNKADN 690
Cdd:cd03111   122 GHFLDEVTLAVLEAADEILLVTQQDlpSLRNARRLLDSLRELEGSSDRLRLVLNRYDK 179
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 619-691 9.42e-04

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 40.91  E-value: 9.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707052555 619 FVDTPGIIENRKQqeRGYPFNDVCQWFIDRADLIFVVFDPTKlDVGLELEMLFRQLKGRESQIRIILNKADNL 691
Cdd:cd04163    55 FVDTPGIHKPKKK--LGERMVKAAWSALKDVDLVLFVVDASE-WIGEGDEFILELLKKSKTPVILVLNKIDLV 124
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 213-462 1.90e-03

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: 42.20  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 213 GSDHQSTELDGAQDAIPAGEDSDADVAAEAREEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSDMAS------------ 280
Cdd:NF033609  613 ASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdsdsdsdsds 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 281 -----SEVGAEEDAE-DSKAEVDAETGEEAEDQGEPRPSLEAGSAREA-------SEKSEDTQSSEVRETEGQASGMSEE 347
Cdd:NF033609  693 dsdsdSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdsdsdSDSDSDSDSDSDSDSDSDSDSDSDS 772

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 348 DLAEASSEEEGGEEDGRENGGLPSKEESGEDSGDGASSEEEGSTSGEAAEPQKTPRATGHEEEGAQLDVEDLNTGSEGVK 427
Cdd:NF033609  773 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 852

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1707052555 428 TQDTEAEASEERQQGRGNPVI-----------AHQEEAEDVSEEAP 462
Cdd:NF033609  853 DSDSESDSNSDSESGSNNNVVppnspkngtnaSNKNEAKDSKEPLP 898
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 274-483 2.59e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.52  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  274 AVSDMASSEVG-AEEDAEDSKAEVDAETGEEAE--DQGEPRPSLEAGSAREASEKSE-DTQSSEVRETEGQASGMSEEDL 349
Cdd:TIGR00927  626 ALGDLSKGDVAeAEHTGERTGEEGERPTEAEGEngEESGGEAEQEGETETKGENESEgEIPAERKGEQEGEGEIEAKEAD 705

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  350 AEASSEEEGGEEDGRENGGLPSKEESGEDSGDGASSEEEGSTSGEAAEPQktpratghEEEGAQldvedlntgSEGVKTQ 429
Cdd:TIGR00927  706 HKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEV--------ETEGDR---------KETEHEG 768

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1707052555  430 DTEAEASEERQQGRgnpvIAHQEEAEDVSEEAPMRDRSHIEKTLMLNEDKPADD 483
Cdd:TIGR00927  769 ETEAEGKEDEDEGE----IQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQ 818
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 229-438 5.58e-03

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: 40.66  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 229 PAGEDSDADVAAEAREEAEDQPEDHSLPSEDAAPPGPDH-QPTDPHAVSDMAS-SEVGAEED-AEDSKAEVDAET---GE 302
Cdd:NF033609  556 PIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSaSDSDSASDSDSASdSDSASDSDsASDSDSASDSDSasdSD 635

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 303 EAEDQGEPRPSLEAGSAREASEKSEDTQSSEVRETEGQASGMSEEDLAEASSEEEGGEEDGRENGGLPSKEESGEDSGDG 382
Cdd:NF033609  636 SASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 715

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1707052555 383 ASSEEEGSTSGEAAEPQKTPRATGHEEEGAQLDVEDLNTGSEGVKTQDTEAEASEE 438
Cdd:NF033609  716 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 771
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 617-689 5.87e-03

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 38.24  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 617 VTFVDTPGI------IEN---RKQQERgypfndvcqwfIDRADLIFVVFDPTKlDVGLELEMLFRQLKGResQIRIILNK 687
Cdd:cd04164    53 VRLIDTAGLretedeIEKigiERAREA-----------IEEADLVLLVVDASE-GLDEEDLEILELPAKK--PVIVVLNK 118


                  ..
gi 1707052555 688 AD 689
Cdd:cd04164   119 SD 120
era PRK00089
GTPase Era; Reviewed
 526-694 6.71e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 39.65  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 526 MVLFLGPWSVGKSTMINYLLGlED----------TRyqlytgaepttseftvlmhgpklKTIEGIVMAADSarsfsplek 595
Cdd:PRK00089    7 FVAIVGRPNVGKSTLLNALVG-QKisivspkpqtTR-----------------------HRIRGIVTEDDA--------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 596 fgQnflekLIgievphkllervtFVDTPGIIENRKQQERGypFNDVCQWFIDRADLIFVVFDPTKlDVGLELEMLFRQLK 675
Cdd:PRK00089   54 --Q-----II-------------FVDTPGIHKPKRALNRA--MNKAAWSSLKDVDLVLFVVDADE-KIGPGDEFILEKLK 110

                         170
                  ....*....|....*....
gi 1707052555 676 GRESQIRIILNKADNLATQ 694
Cdd:PRK00089  111 KVKTPVILVLNKIDLVKDK 129
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 207-463 6.94e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.36  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  207 EGEGsiGSDHQSTELDGAQDAIPAGEDSDadvaaeareEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSDMASSEVGAE 286
Cdd:TIGR00927  669 QEGE--TETKGENESEGEIPAERKGEQEG---------EGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  287 EDAEDSKAEVDAETGEEAEDQGEprpsleagsarEASEKSEDTQSSEVRETEGQASGMSEEDLAEASSEEEGGEEDGREN 366
Cdd:TIGR00927  738 GEEVEDEGEGEAEGKHEVETEGD-----------RKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGE 806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555  367 GGLPSKEESGEDSGDGASSEEEGSTSGEAAEPQKTPRATGHEEEGAqldveDLNTGSEGVKTQDTEAEASEERQQGRGNp 446
Cdd:TIGR00927  807 TEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGV-----DGGGGSDGGDSEEEEEEEEEEEEEEEEE- 880

                          250
                   ....*....|....*..
gi 1707052555  447 viaHQEEAEDVSEEAPM 463
Cdd:TIGR00927  881 ---EEEEEEEEENEEPL 894
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 213-438 9.95e-03

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: 39.89  E-value: 9.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 213 GSDHQS-TELDGAQDAIPAgEDSDADVAAEAREEAEDQPEDHSLPSEDAAPPGPDHQPTDPHAVSDMASSEVGAEEDAED 291
Cdd:NF033609  583 GSDSTSdSGSDSASDSDSA-SDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSD 661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707052555 292 SKAEVDAETGEEAEDQGEPRPSLEAGSAREA-----SEKSEDTQSSEVRETEGQASGMSEEDLAEASSEEEGGEEDGREN 366
Cdd:NF033609  662 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 741

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1707052555 367 GGLPSKEESGEDSGDGASSEEEGSTSGEAAEPQKTPRATGHEEEGAQLDVEDLNTGSEGVKTQDTEAEASEE 438
Cdd:NF033609  742 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 813
 
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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