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Conserved domains on  [gi|28575000|ref|NP_788450|]
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stem cell tumor, isoform B [Drosophila melanogaster]

Protein Classification

rhomboid family intramembrane serine protease( domain architecture ID 12145414)

rhomboid family intramembrane serine protease is a membrane-bound protein that catalyzes regulated intramembrane proteolysis, resulting in the release of functional polypeptides from their membrane anchor; contains an EF-hand calcium binding domain

CATH:  1.20.1540.10
EC:  3.4.21.-
Gene Ontology:  GO:0004252|GO:0005509
MEROPS:  S54
SCOP:  4000471

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
262-428 2.65e-40

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


:

Pssm-ID: 426384  Cd Length: 147  Bit Score: 141.98  E-value: 2.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000   262 PDKRHEIWRFLFYMVLHAGWLHLGFNVAVQLVFGLPLEMVHGSTRIACIYFSGVLAGSLGTSIFDPD-VFLVGASGGVYA 340
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLsTPSVGASGAIFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000   341 LLAAHLANVLLNYHQMRYGVIKLLHILVFVSFDFGFAIYARYagdelqlgssseflaidqaetagAVSYVAHLAGAIAGL 420
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLLPGN-----------------------GVSNLAHLGGLLVGL 137

                  ....*...
gi 28575000   421 TIGLLVLK 428
Cdd:pfam01694 138 LLGFILLR 145
EF-hand_7 pfam13499
EF-hand domain pair;
87-157 7.77e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 7.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28575000    87 RDKWKLLFDMFDPEGFGEISVEEFLEALKSPEFLSQVPMNKRELLLERAKKaklpTGPGYVTFQDFVNVMS 157
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVEELFKEFDL----DKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
262-428 2.65e-40

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 141.98  E-value: 2.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000   262 PDKRHEIWRFLFYMVLHAGWLHLGFNVAVQLVFGLPLEMVHGSTRIACIYFSGVLAGSLGTSIFDPD-VFLVGASGGVYA 340
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLsTPSVGASGAIFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000   341 LLAAHLANVLLNYHQMRYGVIKLLHILVFVSFDFGFAIYARYagdelqlgssseflaidqaetagAVSYVAHLAGAIAGL 420
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLLPGN-----------------------GVSNLAHLGGLLVGL 137

                  ....*...
gi 28575000   421 TIGLLVLK 428
Cdd:pfam01694 138 LLGFILLR 145
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
257-428 1.13e-23

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 98.01  E-value: 1.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000 257 MFIYRPDKRHEIWRFLFYMVLHAGWLHLGFNVAVQLVFGLPLEMVHGSTRIACIYFSGVLAGSLGTSIFDP--DVFLVGA 334
Cdd:COG0705  32 ALVPARLLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPLLERRLGSKRFLLLYLLSGLGGGLLQLLFSPgsGYPLVGA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000 335 SGGVYALLAAHLANVLLNYHQMRYGVIKLLH-ILVFVSFDFGFAIYaryagdelqlgssseflaidqaeTAGAVSYVAHL 413
Cdd:COG0705 112 SGAIFGLLGALLVLGPRRRVLLLFIPIPALLfLLVWLLLGLLFGLL-----------------------GGGGIAWEAHL 168
                       170
                ....*....|....*
gi 28575000 414 AGAIAGLTIGLLVLK 428
Cdd:COG0705 169 GGLLAGLLLALLLRK 183
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
201-456 4.01e-14

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 72.58  E-value: 4.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000  201 EILPEERDRKYYADRYTCCP------------PPF----FIILVTLVELGFFVYhSVVTGEAAPRgpIPSDSMFI----- 259
Cdd:PTZ00101  16 ENTPFNRAEKYYQSQSSFIQrskpidvlnlifPHFtwksFIMAISIIQIIVFII-SVSIKPADFL--TPSDSLLVtlgan 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000  260 YRPD-KRHEIWRFLFYMVLHAGWLHLGFNVAVQLVFGLPLEMVHGSTRIACIYFSGVLAGSLGTSIFDPDVFLVGASGGV 338
Cdd:PTZ00101  93 VASRiKQGEIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVKIIILYFLTGIYGNILSSSVTYCPIKVGASTSG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000  339 YALLAAHLANVLLNYHQMRYGVIKLLHILVFVSFDFGFaiYARYAGdelqlgssseflaidqaetaGAVSYVAHLAGAIA 418
Cdd:PTZ00101 173 MGLLGIVTSELILLWHVIRHRERVVFNIIFFSLISFFY--YFTFNG--------------------SNIDHVGHLGGLLS 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 28575000  419 GLTIGLLvlksFEQKLHEQLLW--WIALGTYLALVVFAIA 456
Cdd:PTZ00101 231 GISMGIL----YNSQMENKPSWydHMKMASYACLALLAIV 266
rhom_GG_sort TIGR03902
rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like ...
267-424 2.58e-10

rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like intramembrane serine protease. Its species distribution closely matches model TIGR03501, GlyGly-CTERM, which describes a protein targeting domain analogous to LPXTG and PEP-CTERM. In a number of species (Ralstonia eutropha ,R. metallidurans, R. solanacearum, Marinobacter aquaeolei, etc) with just one GlyGly-CTERM protein (i.e., a dedicated system), the rhombosortase and GlyGly-CTERM genes are adjacent.


Pssm-ID: 274845  Cd Length: 154  Bit Score: 58.74  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000   267 EIWRFLFYMVLHAGWLHLGFNVAVQLVFGLPLEMVHGSTRIACIYFSGVLAGSLGTSIFDPDV-FLVGASGGVYALLAAH 345
Cdd:TIGR03902  15 EWWRLLTGHFVHLNWWHLLMNLAGLLLLWALFGRHLRARRLLLLLLLLSLLISLGLLLFLPSLqWYVGLSGVLHGLFAWG 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28575000   346 LanvllnYHQMRYGviKLLHILVFVsfdfgfAIYARYAGDELQLGSSSEflaidQAETAGAVSYVAHLAGAIAGLTIGL 424
Cdd:TIGR03902  95 A------LRDIRYG--RRSGWLLLL------GVIAKLAWEQLFGASAFT-----AALIGAPVATEAHLAGAISGLLIAL 154
EF-hand_7 pfam13499
EF-hand domain pair;
87-157 7.77e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 7.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28575000    87 RDKWKLLFDMFDPEGFGEISVEEFLEALKSPEFLSQVPMNKRELLLERAKKaklpTGPGYVTFQDFVNVMS 157
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVEELFKEFDL----DKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
75-115 1.93e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 36.76  E-value: 1.93e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 28575000  75 DFDE-----AELRRELLRDKWKLLFDMFDPEGFGEISVEEFLEALK 115
Cdd:cd00051  18 SADElkaalKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00183 PTZ00183
centrin; Provisional
66-159 3.03e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.52  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000   66 DTEHTSLNSDfDEAELRREllrdkwkllFDMFDPEGFGEISVEEFLEALKSPEFLSQVPMNKReLLLERAKKaklptGPG 145
Cdd:PTZ00183   5 RSERPGLTED-QKKEIREA---------FDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQ-MIADVDKD-----GSG 68
                         90
                 ....*....|....
gi 28575000  146 YVTFQDFVNVMSGK 159
Cdd:PTZ00183  69 KIDFEEFLDIMTKK 82
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
262-428 2.65e-40

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 141.98  E-value: 2.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000   262 PDKRHEIWRFLFYMVLHAGWLHLGFNVAVQLVFGLPLEMVHGSTRIACIYFSGVLAGSLGTSIFDPD-VFLVGASGGVYA 340
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLsTPSVGASGAIFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000   341 LLAAHLANVLLNYHQMRYGVIKLLHILVFVSFDFGFAIYARYagdelqlgssseflaidqaetagAVSYVAHLAGAIAGL 420
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLLPGN-----------------------GVSNLAHLGGLLVGL 137

                  ....*...
gi 28575000   421 TIGLLVLK 428
Cdd:pfam01694 138 LLGFILLR 145
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
257-428 1.13e-23

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 98.01  E-value: 1.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000 257 MFIYRPDKRHEIWRFLFYMVLHAGWLHLGFNVAVQLVFGLPLEMVHGSTRIACIYFSGVLAGSLGTSIFDP--DVFLVGA 334
Cdd:COG0705  32 ALVPARLLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPLLERRLGSKRFLLLYLLSGLGGGLLQLLFSPgsGYPLVGA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000 335 SGGVYALLAAHLANVLLNYHQMRYGVIKLLH-ILVFVSFDFGFAIYaryagdelqlgssseflaidqaeTAGAVSYVAHL 413
Cdd:COG0705 112 SGAIFGLLGALLVLGPRRRVLLLFIPIPALLfLLVWLLLGLLFGLL-----------------------GGGGIAWEAHL 168
                       170
                ....*....|....*
gi 28575000 414 AGAIAGLTIGLLVLK 428
Cdd:COG0705 169 GGLLAGLLLALLLRK 183
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
201-456 4.01e-14

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 72.58  E-value: 4.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000  201 EILPEERDRKYYADRYTCCP------------PPF----FIILVTLVELGFFVYhSVVTGEAAPRgpIPSDSMFI----- 259
Cdd:PTZ00101  16 ENTPFNRAEKYYQSQSSFIQrskpidvlnlifPHFtwksFIMAISIIQIIVFII-SVSIKPADFL--TPSDSLLVtlgan 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000  260 YRPD-KRHEIWRFLFYMVLHAGWLHLGFNVAVQLVFGLPLEMVHGSTRIACIYFSGVLAGSLGTSIFDPDVFLVGASGGV 338
Cdd:PTZ00101  93 VASRiKQGEIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVKIIILYFLTGIYGNILSSSVTYCPIKVGASTSG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000  339 YALLAAHLANVLLNYHQMRYGVIKLLHILVFVSFDFGFaiYARYAGdelqlgssseflaidqaetaGAVSYVAHLAGAIA 418
Cdd:PTZ00101 173 MGLLGIVTSELILLWHVIRHRERVVFNIIFFSLISFFY--YFTFNG--------------------SNIDHVGHLGGLLS 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 28575000  419 GLTIGLLvlksFEQKLHEQLLW--WIALGTYLALVVFAIA 456
Cdd:PTZ00101 231 GISMGIL----YNSQMENKPSWydHMKMASYACLALLAIV 266
rhom_GG_sort TIGR03902
rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like ...
267-424 2.58e-10

rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like intramembrane serine protease. Its species distribution closely matches model TIGR03501, GlyGly-CTERM, which describes a protein targeting domain analogous to LPXTG and PEP-CTERM. In a number of species (Ralstonia eutropha ,R. metallidurans, R. solanacearum, Marinobacter aquaeolei, etc) with just one GlyGly-CTERM protein (i.e., a dedicated system), the rhombosortase and GlyGly-CTERM genes are adjacent.


Pssm-ID: 274845  Cd Length: 154  Bit Score: 58.74  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000   267 EIWRFLFYMVLHAGWLHLGFNVAVQLVFGLPLEMVHGSTRIACIYFSGVLAGSLGTSIFDPDV-FLVGASGGVYALLAAH 345
Cdd:TIGR03902  15 EWWRLLTGHFVHLNWWHLLMNLAGLLLLWALFGRHLRARRLLLLLLLLSLLISLGLLLFLPSLqWYVGLSGVLHGLFAWG 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28575000   346 LanvllnYHQMRYGviKLLHILVFVsfdfgfAIYARYAGDELQLGSSSEflaidQAETAGAVSYVAHLAGAIAGLTIGL 424
Cdd:TIGR03902  95 A------LRDIRYG--RRSGWLLLL------GVIAKLAWEQLFGASAFT-----AALIGAPVATEAHLAGAISGLLIAL 154
EF-hand_7 pfam13499
EF-hand domain pair;
87-157 7.77e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 7.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28575000    87 RDKWKLLFDMFDPEGFGEISVEEFLEALKSPEFLSQVPMNKRELLLERAKKaklpTGPGYVTFQDFVNVMS 157
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVEELFKEFDL----DKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
75-115 1.93e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 36.76  E-value: 1.93e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 28575000  75 DFDE-----AELRRELLRDKWKLLFDMFDPEGFGEISVEEFLEALK 115
Cdd:cd00051  18 SADElkaalKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00183 PTZ00183
centrin; Provisional
66-159 3.03e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.52  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000   66 DTEHTSLNSDfDEAELRREllrdkwkllFDMFDPEGFGEISVEEFLEALKSPEFLSQVPMNKReLLLERAKKaklptGPG 145
Cdd:PTZ00183   5 RSERPGLTED-QKKEIREA---------FDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQ-MIADVDKD-----GSG 68
                         90
                 ....*....|....
gi 28575000  146 YVTFQDFVNVMSGK 159
Cdd:PTZ00183  69 KIDFEEFLDIMTKK 82
PRK10907 PRK10907
intramembrane serine protease GlpG; Provisional
260-342 3.86e-03

intramembrane serine protease GlpG; Provisional


Pssm-ID: 182828 [Multi-domain]  Cd Length: 276  Bit Score: 39.22  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28575000  260 YRPDKRHEIWRFLFYMVLHAGWLHLGFNVAVQLVFGLPLEMVHGSTRIACIYFSGVLAGSLGTSIFDpDVFLVGASGGVY 339
Cdd:PRK10907 127 FDPSLKFELWRYFTHALLHFSLLHILFNLLWWWYLGGAVEKRLGSGKLIVITLISALLSGWVQSKFS-GPWFGGLSGVVY 205

                 ...
gi 28575000  340 ALL 342
Cdd:PRK10907 206 ALM 208
EF-hand_7 pfam13499
EF-hand domain pair;
65-115 8.66e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.92  E-value: 8.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 28575000    65 YDTEHT-SLN-SDFDEA----ELRRELLRDKWKLLFDMFDPEGFGEISVEEFLEALK 115
Cdd:pfam13499  11 LDSDGDgYLDvEELKKLlrklEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
 
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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