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Conserved domains on  [gi|767966632|ref|XP_011518698|]
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myotubularin-related protein 13 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SBF2 pfam12335
Myotubularin protein; This domain family is found in eukaryotes, and is approximately 220 ...
530-754 8.26e-148

Myotubularin protein; This domain family is found in eukaryotes, and is approximately 220 amino acids in length. The family is found in association with pfam02141, pfam03456, pfam03455. This family is the middle region of SBF2, a member of the myotubularin family. Myotubularin-related proteins have been suggested to work in phosphoinositide-mediated signalling events that may also convey control of myelination. Mutations of SBF2 are implicated in Charcot-Marie-Tooth disease.


:

Pssm-ID: 463536  Cd Length: 227  Bit Score: 442.52  E-value: 8.26e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   530 GPPVVSIMDKVTTVF-NSAQRLEVVRNCISFIFENKILETEKTLPAALRALKGKAARQCLTDELGLHVQQNRAILDHQQF 608
Cdd:pfam12335    1 GPPVVSIVDKRGNVFsNSARRLEVLRNCISFIFENKISEARKSLPAVLRALKGKAARLALCEELNQHVQQNRAVLDHQQF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   609 DYIIRMMNCTLQDCSSLEEYNIAAALLPLTSAFYRKLAPGVSQFAYTCVQDHPIWTNQQFWETTFYNAVQEQVRSLYLSA 688
Cdd:pfam12335   81 DLVVRLMNCALQDCSSMDEYGVAAALLPLSTAFCRKLCTGVIQFAYTCVQDHPVWKNQQFWEAAFYQDVQKQIRALYLPS 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966632   689 KEDNHAPHLKQK-DKLPDDHYQEKTAMDLAAEQLRLWPTLSKSTQQELVQHEESTVFSQAIHFANLM 754
Cdd:pfam12335  161 DEKNPHISAQGKnTASLASHAEEPSALEIAAEQMRLWPTLSKEKQQELVKSEESTVYSQAIHYANRM 227
DENN pfam02141
DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a ...
116-298 3.48e-67

DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a domain which occurs in several proteins involved in Rab- mediated processes or regulation of MAPK signalling pathways.


:

Pssm-ID: 460461  Cd Length: 186  Bit Score: 223.99  E-value: 3.48e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   116 FAPKSLVLVSRLYYPEIFRACLGLIYTVYVDSLN-VSLESLIANLCAC-LVPAAGGSQKLFSLGAGDRQLIQTPLHDSLP 193
Cdd:pfam02141    1 RIPKAYCIISRLPFFNLFKKFLDELYRRRTISPLpNPIERFIANLLYEvPFPPPGRTQKLKPLGGTEPILLQRPEDSELP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   194 ITGTSVALLFQQLGIQNVLSLFCAVLTENKVLFHSASFQRLSDACRALESLMFPLKYSYPYIPILPAQLLEVLSSPTPFI 273
Cdd:pfam02141   81 LEGVDLHLLFRCLSPENILQLFEAALLERRIIFLSSDLARLTLVAEAVVALLYPFVWQHIYIPVLPASLLDVLSAPTPFI 160
                          170       180
                   ....*....|....*....|....*.
gi 767966632   274 IGVHS-VFKTDVHELLDVIIADLDGG 298
Cdd:pfam02141  161 IGVHSrYFDLLEDPLDDVVLVDLDTG 186
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
882-1000 1.87e-57

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13339:

Pssm-ID: 473070  Cd Length: 119  Bit Score: 193.65  E-value: 1.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632  882 EEIVCEGLRVLLDPDGREEATGGLLGGPQLLPAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQNQ 961
Cdd:cd13339     1 EEFVCEGLRVLLDPDGREEATGGLLGGPHILPAEGALFLTTYRIIFKGTPHDQLVGEQTVIRSFPIASITKEKKITIQNQ 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767966632  962 LQQNMQEGLQITSASFQLIKVAFDEEVSPEVVEIFKKQL 1000
Cdd:cd13339    81 LQQNMQEGLQITSASFQLIKVAFDEEVSPEVVEIFKKQL 119
uDENN smart00800
Domain always found upstream of DENN domain, found in a variety of signalling proteins; The ...
1-86 7.81e-31

Domain always found upstream of DENN domain, found in a variety of signalling proteins; The uDENN domain is part of the tripartite DENN domain. It is always found upstream of the DENN domain itself, which is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


:

Pssm-ID: 214824  Cd Length: 89  Bit Score: 116.67  E-value: 7.81e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632      1 MARLADYFIVVGYDHEKPGSGEG-LGKIIQRFPQKDWDDTPFPQGIELFCQPGGWQL--SRERKQPTFFVVVLTDIDSDR 77
Cdd:smart00800    1 PSRLFDYFVVVGLDSDTGPLGRSyKPEILQRYPEKDFEDFPLPDSIPLFCFPEGLDFvtQTSSKDPQFFSFVLTDIDGSR 80

                    ....*....
gi 767966632     78 HYCSCLTFY 86
Cdd:smart00800   81 RYGFCLRFY 89
dDENN smart00801
Domain always found downstream of DENN domain, found in a variety of signalling proteins; The ...
352-420 5.61e-19

Domain always found downstream of DENN domain, found in a variety of signalling proteins; The dDENN domain is part of the tripartite DENN domain. It is always found downstream of the DENN domain itself, which is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


:

Pssm-ID: 129037  Cd Length: 69  Bit Score: 81.95  E-value: 5.61e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966632    352 DKEVRAVFLRLFAQLFQGYRSCLQLIRIHAEPVIHFHKTAFLGQRGLVENDFLTKVLSGMAFAGFVSER 420
Cdd:smart00801    1 NDEIREAFLRFFVNLFGGYRNFLRELRKEPGPVITFDKESFLKSRPSSERPFLSKFLETQMFSQFIEER 69
 
Name Accession Description Interval E-value
SBF2 pfam12335
Myotubularin protein; This domain family is found in eukaryotes, and is approximately 220 ...
530-754 8.26e-148

Myotubularin protein; This domain family is found in eukaryotes, and is approximately 220 amino acids in length. The family is found in association with pfam02141, pfam03456, pfam03455. This family is the middle region of SBF2, a member of the myotubularin family. Myotubularin-related proteins have been suggested to work in phosphoinositide-mediated signalling events that may also convey control of myelination. Mutations of SBF2 are implicated in Charcot-Marie-Tooth disease.


Pssm-ID: 463536  Cd Length: 227  Bit Score: 442.52  E-value: 8.26e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   530 GPPVVSIMDKVTTVF-NSAQRLEVVRNCISFIFENKILETEKTLPAALRALKGKAARQCLTDELGLHVQQNRAILDHQQF 608
Cdd:pfam12335    1 GPPVVSIVDKRGNVFsNSARRLEVLRNCISFIFENKISEARKSLPAVLRALKGKAARLALCEELNQHVQQNRAVLDHQQF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   609 DYIIRMMNCTLQDCSSLEEYNIAAALLPLTSAFYRKLAPGVSQFAYTCVQDHPIWTNQQFWETTFYNAVQEQVRSLYLSA 688
Cdd:pfam12335   81 DLVVRLMNCALQDCSSMDEYGVAAALLPLSTAFCRKLCTGVIQFAYTCVQDHPVWKNQQFWEAAFYQDVQKQIRALYLPS 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966632   689 KEDNHAPHLKQK-DKLPDDHYQEKTAMDLAAEQLRLWPTLSKSTQQELVQHEESTVFSQAIHFANLM 754
Cdd:pfam12335  161 DEKNPHISAQGKnTASLASHAEEPSALEIAAEQMRLWPTLSKEKQQELVKSEESTVYSQAIHYANRM 227
DENN pfam02141
DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a ...
116-298 3.48e-67

DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a domain which occurs in several proteins involved in Rab- mediated processes or regulation of MAPK signalling pathways.


Pssm-ID: 460461  Cd Length: 186  Bit Score: 223.99  E-value: 3.48e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   116 FAPKSLVLVSRLYYPEIFRACLGLIYTVYVDSLN-VSLESLIANLCAC-LVPAAGGSQKLFSLGAGDRQLIQTPLHDSLP 193
Cdd:pfam02141    1 RIPKAYCIISRLPFFNLFKKFLDELYRRRTISPLpNPIERFIANLLYEvPFPPPGRTQKLKPLGGTEPILLQRPEDSELP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   194 ITGTSVALLFQQLGIQNVLSLFCAVLTENKVLFHSASFQRLSDACRALESLMFPLKYSYPYIPILPAQLLEVLSSPTPFI 273
Cdd:pfam02141   81 LEGVDLHLLFRCLSPENILQLFEAALLERRIIFLSSDLARLTLVAEAVVALLYPFVWQHIYIPVLPASLLDVLSAPTPFI 160
                          170       180
                   ....*....|....*....|....*.
gi 767966632   274 IGVHS-VFKTDVHELLDVIIADLDGG 298
Cdd:pfam02141  161 IGVHSrYFDLLEDPLDDVVLVDLDTG 186
DENN smart00799
Domain found in a variety of signalling proteins, always encircled by uDENN and dDENN; The ...
117-298 3.90e-64

Domain found in a variety of signalling proteins, always encircled by uDENN and dDENN; The DENN domain is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


Pssm-ID: 214823  Cd Length: 183  Bit Score: 215.14  E-value: 3.90e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632    117 APKSLVLVSRLYYPEIFRACLGLIYTVYVDSLNVSLEsLIANLCACLVPAAGGSQKLFSLGAGDRQLIQTPLHDSLPITG 196
Cdd:smart00799    1 APKCICILSRLPFFELFRKILNELYRLLPSSSNLPLE-LLISLLLYPVPPPGGSLVLVSLGPGDLIELQRPLDSSLPLID 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632    197 TSVALLFQQLGIQNVLSLFCAVLTENKVLFHSASFQRLSDACRALESLMFPLKYSYPYIPILPAQLLEVLSSPTPFIIGV 276
Cdd:smart00799   80 FSLHELFECLGVENILQLFAALLLERRIIFTSSNLSTLSAVIEALLALLYPFVWQHIYIPILPASLLDVLSAPTPFIIGV 159
                           170       180
                    ....*....|....*....|....
gi 767966632    277 HSVFKTDVHELL--DVIIADLDGG 298
Cdd:smart00799  160 HSSYFEEVKELPdeDVVVVDLDTG 183
PH-GRAM_MTMR13 cd13339
Myotubularian (MTM) related 13 protein Pleckstrin Homology-Glucosyltransferases, Rab-like ...
882-1000 1.87e-57

Myotubularian (MTM) related 13 protein Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR13 (also called SBF2/SET binding factor 2) is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Leu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR13 has high sequence similarity to MTMR5 and has recently been shown to be a second gene mutated in type 4B Charcot-Marie-Tooth syndrome. Both MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 275416  Cd Length: 119  Bit Score: 193.65  E-value: 1.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632  882 EEIVCEGLRVLLDPDGREEATGGLLGGPQLLPAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQNQ 961
Cdd:cd13339     1 EEFVCEGLRVLLDPDGREEATGGLLGGPHILPAEGALFLTTYRIIFKGTPHDQLVGEQTVIRSFPIASITKEKKITIQNQ 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767966632  962 LQQNMQEGLQITSASFQLIKVAFDEEVSPEVVEIFKKQL 1000
Cdd:cd13339    81 LQQNMQEGLQITSASFQLIKVAFDEEVSPEVVEIFKKQL 119
uDENN smart00800
Domain always found upstream of DENN domain, found in a variety of signalling proteins; The ...
1-86 7.81e-31

Domain always found upstream of DENN domain, found in a variety of signalling proteins; The uDENN domain is part of the tripartite DENN domain. It is always found upstream of the DENN domain itself, which is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


Pssm-ID: 214824  Cd Length: 89  Bit Score: 116.67  E-value: 7.81e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632      1 MARLADYFIVVGYDHEKPGSGEG-LGKIIQRFPQKDWDDTPFPQGIELFCQPGGWQL--SRERKQPTFFVVVLTDIDSDR 77
Cdd:smart00800    1 PSRLFDYFVVVGLDSDTGPLGRSyKPEILQRYPEKDFEDFPLPDSIPLFCFPEGLDFvtQTSSKDPQFFSFVLTDIDGSR 80

                    ....*....
gi 767966632     78 HYCSCLTFY 86
Cdd:smart00800   81 RYGFCLRFY 89
uDENN pfam03456
uDENN domain; This region is always found associated with pfam02141. It is predicted to form ...
25-84 2.03e-23

uDENN domain; This region is always found associated with pfam02141. It is predicted to form an all beta domain.


Pssm-ID: 460926  Cd Length: 59  Bit Score: 94.21  E-value: 2.03e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632    25 GKIIQRFPQKDWDDTPFPQGIELFCQPGGWQLSRERKqPTFFVVVLTDIDSDRHYCSCLT 84
Cdd:pfam03456    1 PEVLDRYPEDDWSDPPLPDGIPMFCFPEGLETLSSRE-PTFFSFVLTDEDGSRLYGACLT 59
dDENN smart00801
Domain always found downstream of DENN domain, found in a variety of signalling proteins; The ...
352-420 5.61e-19

Domain always found downstream of DENN domain, found in a variety of signalling proteins; The dDENN domain is part of the tripartite DENN domain. It is always found downstream of the DENN domain itself, which is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


Pssm-ID: 129037  Cd Length: 69  Bit Score: 81.95  E-value: 5.61e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966632    352 DKEVRAVFLRLFAQLFQGYRSCLQLIRIHAEPVIHFHKTAFLGQRGLVENDFLTKVLSGMAFAGFVSER 420
Cdd:smart00801    1 NDEIREAFLRFFVNLFGGYRNFLRELRKEPGPVITFDKESFLKSRPSSERPFLSKFLETQMFSQFIEER 69
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
879-957 4.08e-05

domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 42.20  E-value: 4.08e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966632    879 LPGEEIVCEGLRVLLDPDGReeatggllggpqllpAEGALFLTTYRILFRGTPHDQLvgeqtVVRSFPIASITKEKKIT 957
Cdd:smart00568    2 LPEEEKLIADYSCYLSRTGP---------------VQGRLYISNYRLCFRSNLPGKL-----TKVVIPLADITRIEKST 60
dDENN pfam03455
dDENN domain; This region is always found associated with pfam02141. It is predicted to form a ...
387-433 5.32e-05

dDENN domain; This region is always found associated with pfam02141. It is predicted to form a globular domain. Although not statistically supported it has been suggested that this domain may be similar to members of the Rho/Rac/Cdc42 GEF family. This N-terminal region of DENN folds into a longin module, consisting of a central antiparallel beta-sheet layered between helix H1 and helices H2 and H3 (strands S1-S5). Rab35 interacts with dDENN via residues in helix 1 and in the loop S3-S4.


Pssm-ID: 460925  Cd Length: 48  Bit Score: 41.80  E-value: 5.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767966632   387 FHKTAFLGQRGLVENDFLTKVLSGMAFAGFVSERG-PPYRSCDLFDEL 433
Cdd:pfam03455    1 FDKEAFLKSLPSDSRPFLSQFLETQMFNEFIEERLeSSDPSIDLFDEE 48
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
914-1006 5.10e-04

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 40.81  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   914 AEGALFLTTYRILFRGTPHDQLvgeQTVVrsFPIASITKEKKITmqnQLQQNMQEGLQITSASFQliKVAFDEEVSPEVV 993
Cdd:pfam02893   30 VQGRLYLTNYRLCFRSLPKGWS---TKVV--IPLVDIEEIEKLK---GGANLFPNGIQVETGSND--KFSFAGFVTRDEA 99
                           90
                   ....*....|...
gi 767966632   994 EIFKKQLMKFRYP 1006
Cdd:pfam02893  100 IEFILALLKNAHP 112
 
Name Accession Description Interval E-value
SBF2 pfam12335
Myotubularin protein; This domain family is found in eukaryotes, and is approximately 220 ...
530-754 8.26e-148

Myotubularin protein; This domain family is found in eukaryotes, and is approximately 220 amino acids in length. The family is found in association with pfam02141, pfam03456, pfam03455. This family is the middle region of SBF2, a member of the myotubularin family. Myotubularin-related proteins have been suggested to work in phosphoinositide-mediated signalling events that may also convey control of myelination. Mutations of SBF2 are implicated in Charcot-Marie-Tooth disease.


Pssm-ID: 463536  Cd Length: 227  Bit Score: 442.52  E-value: 8.26e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   530 GPPVVSIMDKVTTVF-NSAQRLEVVRNCISFIFENKILETEKTLPAALRALKGKAARQCLTDELGLHVQQNRAILDHQQF 608
Cdd:pfam12335    1 GPPVVSIVDKRGNVFsNSARRLEVLRNCISFIFENKISEARKSLPAVLRALKGKAARLALCEELNQHVQQNRAVLDHQQF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   609 DYIIRMMNCTLQDCSSLEEYNIAAALLPLTSAFYRKLAPGVSQFAYTCVQDHPIWTNQQFWETTFYNAVQEQVRSLYLSA 688
Cdd:pfam12335   81 DLVVRLMNCALQDCSSMDEYGVAAALLPLSTAFCRKLCTGVIQFAYTCVQDHPVWKNQQFWEAAFYQDVQKQIRALYLPS 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966632   689 KEDNHAPHLKQK-DKLPDDHYQEKTAMDLAAEQLRLWPTLSKSTQQELVQHEESTVFSQAIHFANLM 754
Cdd:pfam12335  161 DEKNPHISAQGKnTASLASHAEEPSALEIAAEQMRLWPTLSKEKQQELVKSEESTVYSQAIHYANRM 227
DENN pfam02141
DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a ...
116-298 3.48e-67

DENN (AEX-3) domain; DENN (after differentially expressed in neoplastic vs normal cells) is a domain which occurs in several proteins involved in Rab- mediated processes or regulation of MAPK signalling pathways.


Pssm-ID: 460461  Cd Length: 186  Bit Score: 223.99  E-value: 3.48e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   116 FAPKSLVLVSRLYYPEIFRACLGLIYTVYVDSLN-VSLESLIANLCAC-LVPAAGGSQKLFSLGAGDRQLIQTPLHDSLP 193
Cdd:pfam02141    1 RIPKAYCIISRLPFFNLFKKFLDELYRRRTISPLpNPIERFIANLLYEvPFPPPGRTQKLKPLGGTEPILLQRPEDSELP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   194 ITGTSVALLFQQLGIQNVLSLFCAVLTENKVLFHSASFQRLSDACRALESLMFPLKYSYPYIPILPAQLLEVLSSPTPFI 273
Cdd:pfam02141   81 LEGVDLHLLFRCLSPENILQLFEAALLERRIIFLSSDLARLTLVAEAVVALLYPFVWQHIYIPVLPASLLDVLSAPTPFI 160
                          170       180
                   ....*....|....*....|....*.
gi 767966632   274 IGVHS-VFKTDVHELLDVIIADLDGG 298
Cdd:pfam02141  161 IGVHSrYFDLLEDPLDDVVLVDLDTG 186
DENN smart00799
Domain found in a variety of signalling proteins, always encircled by uDENN and dDENN; The ...
117-298 3.90e-64

Domain found in a variety of signalling proteins, always encircled by uDENN and dDENN; The DENN domain is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


Pssm-ID: 214823  Cd Length: 183  Bit Score: 215.14  E-value: 3.90e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632    117 APKSLVLVSRLYYPEIFRACLGLIYTVYVDSLNVSLEsLIANLCACLVPAAGGSQKLFSLGAGDRQLIQTPLHDSLPITG 196
Cdd:smart00799    1 APKCICILSRLPFFELFRKILNELYRLLPSSSNLPLE-LLISLLLYPVPPPGGSLVLVSLGPGDLIELQRPLDSSLPLID 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632    197 TSVALLFQQLGIQNVLSLFCAVLTENKVLFHSASFQRLSDACRALESLMFPLKYSYPYIPILPAQLLEVLSSPTPFIIGV 276
Cdd:smart00799   80 FSLHELFECLGVENILQLFAALLLERRIIFTSSNLSTLSAVIEALLALLYPFVWQHIYIPILPASLLDVLSAPTPFIIGV 159
                           170       180
                    ....*....|....*....|....
gi 767966632    277 HSVFKTDVHELL--DVIIADLDGG 298
Cdd:smart00799  160 HSSYFEEVKELPdeDVVVVDLDTG 183
PH-GRAM_MTMR13 cd13339
Myotubularian (MTM) related 13 protein Pleckstrin Homology-Glucosyltransferases, Rab-like ...
882-1000 1.87e-57

Myotubularian (MTM) related 13 protein Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR13 (also called SBF2/SET binding factor 2) is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Leu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR13 has high sequence similarity to MTMR5 and has recently been shown to be a second gene mutated in type 4B Charcot-Marie-Tooth syndrome. Both MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 275416  Cd Length: 119  Bit Score: 193.65  E-value: 1.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632  882 EEIVCEGLRVLLDPDGREEATGGLLGGPQLLPAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQNQ 961
Cdd:cd13339     1 EEFVCEGLRVLLDPDGREEATGGLLGGPHILPAEGALFLTTYRIIFKGTPHDQLVGEQTVIRSFPIASITKEKKITIQNQ 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767966632  962 LQQNMQEGLQITSASFQLIKVAFDEEVSPEVVEIFKKQL 1000
Cdd:cd13339    81 LQQNMQEGLQITSASFQLIKVAFDEEVSPEVVEIFKKQL 119
PH-GRAM_MTMR5_MTMR13 cd13208
Myotubularian (MTM) related 5 and 13 proteins (MTMR5 and MTMR13) Pleckstrin ...
882-1000 1.09e-48

Myotubularian (MTM) related 5 and 13 proteins (MTMR5 and MTMR13) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR5 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It lacks several amino acids in the dsPTPase catalytic pocket which renders it catalytically inactive as a phosphatase. MTMR5 is the most well-studied inactive member of this family and has been implicated in cellular growth control and oncogenic transformation. MTMR13 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Leu residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR13 has high sequence similarity to MTMR5 and has recently been shown to be a second gene mutated in type 4B Charcot-Marie-Tooth syndrome. Both MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date. Although the majority of the sequences are MTMR 5 and 13, this cd also contains MTM5 nematode sequences.


Pssm-ID: 275396  Cd Length: 120  Bit Score: 168.69  E-value: 1.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632  882 EEIVCEGLRVLLDPDGREEATGGLLGGPQLLpAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQNQ 961
Cdd:cd13208     1 EELVMEGLRVYLLPDGREEGTGGNGGPNLLP-AEGALFLTNYRVIFKGTPCDPLACEQTVVRSFPIASLTKEKKIAVQKL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767966632  962 L--QQNMQEGLQITSASFQLIKVAFDEEVSPEVVEIFKKQL 1000
Cdd:cd13208    80 AhlDQKLQEGLQLRSATFQLIKVAFDEEVSSEKIEKFRKQL 120
PH-GRAM_MTMR5 cd13340
Myotubularian (MTM) related 5 protein (MTMR5) Pleckstrin Homology-Glucosyltransferases, ...
882-1000 1.71e-42

Myotubularian (MTM) related 5 protein (MTMR5) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR5 (also called SBF1/SET binding factor 1) is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It lacks several amino acids in the dsPTPase catalytic pocket which renders it catalytically inactive as a phosphatase. MTMR5 is the most well-studied inactive member of this family and has been implicated in cellular growth control and oncogenic transformation. MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 275417  Cd Length: 119  Bit Score: 150.78  E-value: 1.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632  882 EEIVCEGLRVLLDPDGREEATGGLLGGPQLLPAEGALFLTTYRILFRGTPHDQLVGEQTVVRSFPIASITKEKKITMQNQ 961
Cdd:cd13340     1 EECVMDGLRVYLLPDGREEASGGSLGGPPLLPAEGAIFLTTYRVIFKGTPTDPLVGEQVVVRSFPVASLTKEKRISVQAQ 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767966632  962 LQQNMQEGLQITSASFQLIKVAFDEEVSPEVVEIFKKQL 1000
Cdd:cd13340    81 MDQFLQEGLQLRSCTFQLLKIAFDEEVASDSAEVFRKHL 119
uDENN smart00800
Domain always found upstream of DENN domain, found in a variety of signalling proteins; The ...
1-86 7.81e-31

Domain always found upstream of DENN domain, found in a variety of signalling proteins; The uDENN domain is part of the tripartite DENN domain. It is always found upstream of the DENN domain itself, which is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


Pssm-ID: 214824  Cd Length: 89  Bit Score: 116.67  E-value: 7.81e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632      1 MARLADYFIVVGYDHEKPGSGEG-LGKIIQRFPQKDWDDTPFPQGIELFCQPGGWQL--SRERKQPTFFVVVLTDIDSDR 77
Cdd:smart00800    1 PSRLFDYFVVVGLDSDTGPLGRSyKPEILQRYPEKDFEDFPLPDSIPLFCFPEGLDFvtQTSSKDPQFFSFVLTDIDGSR 80

                    ....*....
gi 767966632     78 HYCSCLTFY 86
Cdd:smart00800   81 RYGFCLRFY 89
uDENN pfam03456
uDENN domain; This region is always found associated with pfam02141. It is predicted to form ...
25-84 2.03e-23

uDENN domain; This region is always found associated with pfam02141. It is predicted to form an all beta domain.


Pssm-ID: 460926  Cd Length: 59  Bit Score: 94.21  E-value: 2.03e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632    25 GKIIQRFPQKDWDDTPFPQGIELFCQPGGWQLSRERKqPTFFVVVLTDIDSDRHYCSCLT 84
Cdd:pfam03456    1 PEVLDRYPEDDWSDPPLPDGIPMFCFPEGLETLSSRE-PTFFSFVLTDEDGSRLYGACLT 59
dDENN smart00801
Domain always found downstream of DENN domain, found in a variety of signalling proteins; The ...
352-420 5.61e-19

Domain always found downstream of DENN domain, found in a variety of signalling proteins; The dDENN domain is part of the tripartite DENN domain. It is always found downstream of the DENN domain itself, which is found in a variety of signalling proteins involved in Rab-mediated processes or regulation of MAPKs signalling pathways. The DENN domain is always encircled on both sides by more divergent domains, called uDENN (for upstream DENN) and dDENN (for downstream DENN). The function of the DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity.


Pssm-ID: 129037  Cd Length: 69  Bit Score: 81.95  E-value: 5.61e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966632    352 DKEVRAVFLRLFAQLFQGYRSCLQLIRIHAEPVIHFHKTAFLGQRGLVENDFLTKVLSGMAFAGFVSER 420
Cdd:smart00801    1 NDEIREAFLRFFVNLFGGYRNFLRELRKEPGPVITFDKESFLKSRPSSERPFLSKFLETQMFSQFIEER 69
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
915-1000 1.44e-05

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275393  Cd Length: 94  Bit Score: 44.68  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632  915 EGALFLTTYRILFrgtpHDQLVGEQTVVrSFPIASITKEKKITMQNQLQQnmqeGLQITSASFQLIKVAFDEEvsPEVVE 994
Cdd:cd10570    20 EGTLYLSTYRLIF----SSKADGDETKL-VIPLVDITDVEKIAGASFLPS----GLIITCKDFRTIKFSFDSE--DEAVK 88

                  ....*.
gi 767966632  995 IFKKQL 1000
Cdd:cd10570    89 VIARVL 94
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
879-957 4.08e-05

domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 42.20  E-value: 4.08e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966632    879 LPGEEIVCEGLRVLLDPDGReeatggllggpqllpAEGALFLTTYRILFRGTPHDQLvgeqtVVRSFPIASITKEKKIT 957
Cdd:smart00568    2 LPEEEKLIADYSCYLSRTGP---------------VQGRLYISNYRLCFRSNLPGKL-----TKVVIPLADITRIEKST 60
dDENN pfam03455
dDENN domain; This region is always found associated with pfam02141. It is predicted to form a ...
387-433 5.32e-05

dDENN domain; This region is always found associated with pfam02141. It is predicted to form a globular domain. Although not statistically supported it has been suggested that this domain may be similar to members of the Rho/Rac/Cdc42 GEF family. This N-terminal region of DENN folds into a longin module, consisting of a central antiparallel beta-sheet layered between helix H1 and helices H2 and H3 (strands S1-S5). Rab35 interacts with dDENN via residues in helix 1 and in the loop S3-S4.


Pssm-ID: 460925  Cd Length: 48  Bit Score: 41.80  E-value: 5.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767966632   387 FHKTAFLGQRGLVENDFLTKVLSGMAFAGFVSERG-PPYRSCDLFDEL 433
Cdd:pfam03455    1 FDKEAFLKSLPSDSRPFLSQFLETQMFNEFIEERLeSSDPSIDLFDEE 48
SPA pfam08616
Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque ...
208-302 3.25e-04

Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque of the spindle pole body. In Aspergillus nidulans the protein member is necessary for stabilization of the polarity axes during septation. and in S. cerevisiae it functions as a polarization-specific docking factor.


Pssm-ID: 400783  Cd Length: 113  Bit Score: 41.51  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   208 IQNVLSLFCAVLTENKVLF--HSASFQRLSDACRALESLMFPL-------KYSYPYIPIlpaQLLEVLSSPTPFIIGVHS 278
Cdd:pfam08616   12 TPPIILLINALLTSKRIIFlsYQRSAGEVSEFVLALCNLISGGfvlrgftNNSFPYVDL---SKLDALRKVPGYIAGVTN 88
                           90       100
                   ....*....|....*....|....
gi 767966632   279 VFKTDVHELLDVIIaDLDGGTIKI 302
Cdd:pfam08616   89 PIFENQDQWWDVLC-DLDSGSVKL 111
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
914-1006 5.10e-04

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 40.81  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966632   914 AEGALFLTTYRILFRGTPHDQLvgeQTVVrsFPIASITKEKKITmqnQLQQNMQEGLQITSASFQliKVAFDEEVSPEVV 993
Cdd:pfam02893   30 VQGRLYLTNYRLCFRSLPKGWS---TKVV--IPLVDIEEIEKLK---GGANLFPNGIQVETGSND--KFSFAGFVTRDEA 99
                           90
                   ....*....|...
gi 767966632   994 EIFKKQLMKFRYP 1006
Cdd:pfam02893  100 IEFILALLKNAHP 112
 
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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