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Conserved domains on  [gi|195927015|ref|NP_004901|]
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membrane-associated phosphatidylinositol transfer protein 1 isoform a [Homo sapiens]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC_PITPNM1-2_like cd08889
Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); ...
 1-257 0e+00

Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); This subgroup includes an N-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class II phosphatidylinositol transfer protein (PITPs), PITPNM1/PITPalphaI/Nir2 (PYK2 N-terminal domain-interacting receptor2) and PITPNM2/PITPalphaII/Nir3), Drosophila RdgB, and related proteins. These are membrane associated multidomain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Ablation of the mouse gene encoding PITPNM1 results in early embryonic death. PITPNM1 is localized chiefly to the Golgi apparatus, and under certain conditions translocates to the lipid droplets. Targeting to the latter is dependent on a specific threonine residue within the SRPBCC domain. PITPNM1 plays a part in Golgi-mediated transport. It regulates diacylglycerol (DAG) production at the trans-Golgi network (TGN) via the CDP-choline pathway. Drosophila RdgB, the founding member of the PITP family, is implicated in the visual and olfactory transduction. RdgB is required for maintenance of ultra structure in photoreceptors and for sensory transduction. The mouse PITPNM1 gene rescues the phenotype of Drosophila rdgB mutant flies. In addition to the SRPBCC domain, PITPNM1 and -2 contain a Rho-inhibitory domain (Rid), six hydrophobic stretches, a DDHD calcium binding region, and a C-terminal tyrosine kinase Pyk2-binding / HAD-like phosphohydrolase domain. PITPNM1 has a role in regulating cell morphogenesis through its Rho inhibitory domain (Rid). This SRPBCC_PITPNM1-2_like domain model includes the first 52 residues of the 224 residues Rid (Rho-inhibitory domain).


:

Pssm-ID: 176898  Cd Length: 260  Bit Score: 573.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015    1 MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKA 80
Cdd:cd08889     1 MLIKEYRIPLPMSVEEYRIAQLYMIQKKSREESKGEGSGVEILENRPYTDGPGGSGQYTHKIYHIGSHIPGWFRAILPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   81 ALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPR 160
Cdd:cd08889    81 ALRVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDFIDIVKDPVPGSDYKAEEDPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  161 LYHSVKTGRGPLSDDWARTA---AQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELS 237
Cdd:cd08889   161 LYVSEKTGRGPLSDDWIEEYkdpPGKGPIMCAYKLCKVEFRYWGMQTKIERFIHDVALRKVMLRAHRQAWCWQDEWYGLT 240

                         250       260
                  ....*....|....*....|
gi 195927015  238 MADIRALEEETARMLAQRMA 257
Cdd:cd08889   241 MEDIRKLEEETQLALAQKMA 260
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 1023-1154 1.45e-48

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


:

Pssm-ID: 197870  Cd Length: 157  Bit Score: 169.76  E-value: 1.45e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   1023 VVFS-IDGSFTAS------VSIMGSDpKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQ-----HNFPHGVV 1090
Cdd:smart00775    1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQikqdgHNLPHGPV 79

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195927015   1091 SFCDG----------LTHDPLRQKAMFLQSLVQEVE---LNIVAGYGS-PKDVAVYAALGLSPSQTYIVGRAVRKLQA 1154
Cdd:smart00775   80 LLSPDrlfaalhrevISKKPEVFKIACLRDIKNLFPpqgNPFYAGFGNrITDVISYSAVGIPPSRIFTINPKGEVHQE 157
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
 686-879 6.75e-41

DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that may form a metal binding site. The domain is named after these four residues. This pattern of conservation of metal binding residues is often seen in phosphoesterase domains. This domain is found in retinal degeneration B proteins, as well as a family of probable phospholipases. It has been shown that this domain is found in a longer C terminal region that binds to PYK2 tyrosine kinase. These proteins have been called N-terminal domain-interacting receptor (Nir1, Nir2 and Nir3). This suggests that this region is involved in functionally important interactions in other members of this family.


:

Pssm-ID: 460725  Cd Length: 241  Bit Score: 151.05  E-value: 6.75e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   686 LDFKVSGFFLFGSPLGLVLALRKtVMPALEAAQ----MRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLTVPRYQK 761
Cdd:pfam02862    1 LDFEVENFFLLGSPLGLFLALRG-AQIAGRSRSdhiyGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   762 FP---------------------------------------LGDGSSLLLADTLQTH------SSLFLEELEMLVPSTPT 796
Cdd:pfam02862   80 RGlrhlelgegltrigaavgqsvsglwsslssgaslnrslgLSDESSASSADSEQSHersseaSSASESSLQAQSSSAPS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   797 STSGAFWKGSELATDPPAQPAAP----STTSEVVKILERWWGtkRIDYSLYcPEALTA--FPTVTLphlfHASYWESADV 870
Cdd:pfam02862  160 STSSSNGIKEIEETELDWSESERkadkLEREEAKVRALNPNG--RIDYVLQ-EGALESqyLSALTS----HLSYWESEDV 232


                   ....*....
gi 195927015   871 VAFILRQVI 879
Cdd:pfam02862  233 ALFLLRQLL 241
SAV_2336_NTERM super family cl49223
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 606-707 8.16e-03

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


The actual alignment was detected with superfamily member NF041121:

Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 40.37  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  606 VRDPLADGVEGLGRGSPEPSALPPQRIPSDMASPEPEGSQNSLQAAPATTSSWEPRRAStafcPPAASSEAPDGPSSTAR 685
Cdd:NF041121   13 AQMGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLA----PPPPPPPGPAGAAPGAA 88

                          90       100
                  ....*....|....*....|..
gi 195927015  686 LDFKVSGFFLFGSPLGLVLALR 707
Cdd:NF041121   89 LPVRVPAPPALPNPLELARALR 110
 
Name Accession Description Interval E-value
SRPBCC_PITPNM1-2_like cd08889
Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); ...
 1-257 0e+00

Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); This subgroup includes an N-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class II phosphatidylinositol transfer protein (PITPs), PITPNM1/PITPalphaI/Nir2 (PYK2 N-terminal domain-interacting receptor2) and PITPNM2/PITPalphaII/Nir3), Drosophila RdgB, and related proteins. These are membrane associated multidomain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Ablation of the mouse gene encoding PITPNM1 results in early embryonic death. PITPNM1 is localized chiefly to the Golgi apparatus, and under certain conditions translocates to the lipid droplets. Targeting to the latter is dependent on a specific threonine residue within the SRPBCC domain. PITPNM1 plays a part in Golgi-mediated transport. It regulates diacylglycerol (DAG) production at the trans-Golgi network (TGN) via the CDP-choline pathway. Drosophila RdgB, the founding member of the PITP family, is implicated in the visual and olfactory transduction. RdgB is required for maintenance of ultra structure in photoreceptors and for sensory transduction. The mouse PITPNM1 gene rescues the phenotype of Drosophila rdgB mutant flies. In addition to the SRPBCC domain, PITPNM1 and -2 contain a Rho-inhibitory domain (Rid), six hydrophobic stretches, a DDHD calcium binding region, and a C-terminal tyrosine kinase Pyk2-binding / HAD-like phosphohydrolase domain. PITPNM1 has a role in regulating cell morphogenesis through its Rho inhibitory domain (Rid). This SRPBCC_PITPNM1-2_like domain model includes the first 52 residues of the 224 residues Rid (Rho-inhibitory domain).


Pssm-ID: 176898  Cd Length: 260  Bit Score: 573.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015    1 MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKA 80
Cdd:cd08889     1 MLIKEYRIPLPMSVEEYRIAQLYMIQKKSREESKGEGSGVEILENRPYTDGPGGSGQYTHKIYHIGSHIPGWFRAILPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   81 ALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPR 160
Cdd:cd08889    81 ALRVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDFIDIVKDPVPGSDYKAEEDPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  161 LYHSVKTGRGPLSDDWARTA---AQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELS 237
Cdd:cd08889   161 LYVSEKTGRGPLSDDWIEEYkdpPGKGPIMCAYKLCKVEFRYWGMQTKIERFIHDVALRKVMLRAHRQAWCWQDEWYGLT 240

                         250       260
                  ....*....|....*....|
gi 195927015  238 MADIRALEEETARMLAQRMA 257
Cdd:cd08889   241 MEDIRKLEEETQLALAQKMA 260
IP_trans pfam02121
Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family ...
 1-248 5.72e-141

Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family (found in pfam00650), this family can bind/exchange one molecule of phosphatidylinositol (PI) or phosphatidylcholine (PC) and thus aids their transfer between different membrane compartments. There are three sub-families - all share an N-terminal PITP-like domain, whose sequence is highly conserved. It is described as consisting of three regions. The N-terminal region is thought to bind the lipid and contains two helices and an eight-stranded, mostly antiparallel beta-sheet. An intervening loop region, which is thought to play a role in protein-protein interactions, separates this from the C-terminal region, which exhibits the greatest sequence variation and may be involved in membrane binding. PITP alpha has a 16-fold greater affinity for PI than PC. Together with PITP beta, it is expressed ubiquitously in all tissues.


Pssm-ID: 460452  Cd Length: 245  Bit Score: 426.99  E-value: 5.72e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015     1 MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESsGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKA 80
Cdd:pfam02121    1 MLIKEYRIPLPLTVEEYQIAQLYMVAKKSKEET-GGGEGVEVLENEPYEDGEGGKGQYTHKIYHLASKLPSWIRALLPKG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015    81 ALQVEEESWNAYPYTRTRYTCPFV-EKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDP 159
Cdd:pfam02121   80 ALYVEEKAWNAYPYTKTVYTCPFMkEKFSITIETVHKPDNGTQENVLNLSSEELAKREVVVIDIANDKVSSKDYKEEEDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   160 RLYHSVKTGRGPLSDDWARTaaqTGPLMCAYKLCKVEFRYWGMQAKIEQFIHdVGLRRVMLRAHRQAWCWQDEWTELSMA 239
Cdd:pfam02121  160 TLFKSEKTGRGPLKEGWKKS---TSPIMCAYKLVTVEFKWWGLQTRVESFIH-KALRDIFLKFHRQAFCWIDEWYGMTME 235


                   ....*....
gi 195927015   240 DIRALEEET 248
Cdd:pfam02121  236 DIRELEEET 244
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 1023-1154 1.45e-48

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 197870  Cd Length: 157  Bit Score: 169.76  E-value: 1.45e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   1023 VVFS-IDGSFTAS------VSIMGSDpKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQ-----HNFPHGVV 1090
Cdd:smart00775    1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQikqdgHNLPHGPV 79

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195927015   1091 SFCDG----------LTHDPLRQKAMFLQSLVQEVE---LNIVAGYGS-PKDVAVYAALGLSPSQTYIVGRAVRKLQA 1154
Cdd:smart00775   80 LLSPDrlfaalhrevISKKPEVFKIACLRDIKNLFPpqgNPFYAGFGNrITDVISYSAVGIPPSRIFTINPKGEVHQE 157
SMP2 COG5083
Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid ...
 919-1146 2.09e-44

Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid maintenance [Lipid transport and metabolism];


Pssm-ID: 444053  Cd Length: 353  Bit Score: 165.02  E-value: 2.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  919 NHRASDTVVCEGRPQVLSGRFMYGPLDVVTLTGEKVDVYImTQPLSGKWIHFGTEVTNSSGRLTFPVPPERAlgiGVYPV 998
Cdd:COG5083    88 YHMGHDEIVAAGDTQTIVGKFDYGAVFHKDLEDEDVHVYI-YGTGMPDWEYLGSYRTDSDGKIYVPVPAAQE---GRYRV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  999 RMVVRGDHTYAECCLTVVARGTEAVVFSIDGSFTASVSIMGSD------PKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQ 1072
Cdd:COG5083   164 RMVVAGDLSSADLFVSVVPPGRKTVVFDIDGTLTLNDFEGVGDylggetADAHPYAAEVVQAYADKGYRPIYVTGRPYWL 243

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 195927015 1073 KHRVVAWLSQHNFPHGVVSFCDGLTH----DPLRQKAMFLQSLvQEVELNIVAGYG-SPKDVAVYAALGLSPSQTYIVG 1146
Cdd:COG5083   244 AKDTREWLDTQGLPPGILHTTPSATGpigpDTARYKTAEIQLL-IDDGLNIVRAYGnAATDAEAYANAGIPKSETYIIG 321
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
 686-879 6.75e-41

DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that may form a metal binding site. The domain is named after these four residues. This pattern of conservation of metal binding residues is often seen in phosphoesterase domains. This domain is found in retinal degeneration B proteins, as well as a family of probable phospholipases. It has been shown that this domain is found in a longer C terminal region that binds to PYK2 tyrosine kinase. These proteins have been called N-terminal domain-interacting receptor (Nir1, Nir2 and Nir3). This suggests that this region is involved in functionally important interactions in other members of this family.


Pssm-ID: 460725  Cd Length: 241  Bit Score: 151.05  E-value: 6.75e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   686 LDFKVSGFFLFGSPLGLVLALRKtVMPALEAAQ----MRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLTVPRYQK 761
Cdd:pfam02862    1 LDFEVENFFLLGSPLGLFLALRG-AQIAGRSRSdhiyGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   762 FP---------------------------------------LGDGSSLLLADTLQTH------SSLFLEELEMLVPSTPT 796
Cdd:pfam02862   80 RGlrhlelgegltrigaavgqsvsglwsslssgaslnrslgLSDESSASSADSEQSHersseaSSASESSLQAQSSSAPS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   797 STSGAFWKGSELATDPPAQPAAP----STTSEVVKILERWWGtkRIDYSLYcPEALTA--FPTVTLphlfHASYWESADV 870
Cdd:pfam02862  160 STSSSNGIKEIEETELDWSESERkadkLEREEAKVRALNPNG--RIDYVLQ-EGALESqyLSALTS----HLSYWESEDV 232


                   ....*....
gi 195927015   871 VAFILRQVI 879
Cdd:pfam02862  233 ALFLLRQLL 241
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 606-707 8.16e-03

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 40.37  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  606 VRDPLADGVEGLGRGSPEPSALPPQRIPSDMASPEPEGSQNSLQAAPATTSSWEPRRAStafcPPAASSEAPDGPSSTAR 685
Cdd:NF041121   13 AQMGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLA----PPPPPPPGPAGAAPGAA 88

                          90       100
                  ....*....|....*....|..
gi 195927015  686 LDFKVSGFFLFGSPLGLVLALR 707
Cdd:NF041121   89 LPVRVPAPPALPNPLELARALR 110
 
Name Accession Description Interval E-value
SRPBCC_PITPNM1-2_like cd08889
Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); ...
 1-257 0e+00

Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); This subgroup includes an N-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class II phosphatidylinositol transfer protein (PITPs), PITPNM1/PITPalphaI/Nir2 (PYK2 N-terminal domain-interacting receptor2) and PITPNM2/PITPalphaII/Nir3), Drosophila RdgB, and related proteins. These are membrane associated multidomain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Ablation of the mouse gene encoding PITPNM1 results in early embryonic death. PITPNM1 is localized chiefly to the Golgi apparatus, and under certain conditions translocates to the lipid droplets. Targeting to the latter is dependent on a specific threonine residue within the SRPBCC domain. PITPNM1 plays a part in Golgi-mediated transport. It regulates diacylglycerol (DAG) production at the trans-Golgi network (TGN) via the CDP-choline pathway. Drosophila RdgB, the founding member of the PITP family, is implicated in the visual and olfactory transduction. RdgB is required for maintenance of ultra structure in photoreceptors and for sensory transduction. The mouse PITPNM1 gene rescues the phenotype of Drosophila rdgB mutant flies. In addition to the SRPBCC domain, PITPNM1 and -2 contain a Rho-inhibitory domain (Rid), six hydrophobic stretches, a DDHD calcium binding region, and a C-terminal tyrosine kinase Pyk2-binding / HAD-like phosphohydrolase domain. PITPNM1 has a role in regulating cell morphogenesis through its Rho inhibitory domain (Rid). This SRPBCC_PITPNM1-2_like domain model includes the first 52 residues of the 224 residues Rid (Rho-inhibitory domain).


Pssm-ID: 176898  Cd Length: 260  Bit Score: 573.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015    1 MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKA 80
Cdd:cd08889     1 MLIKEYRIPLPMSVEEYRIAQLYMIQKKSREESKGEGSGVEILENRPYTDGPGGSGQYTHKIYHIGSHIPGWFRAILPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   81 ALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPR 160
Cdd:cd08889    81 ALRVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDFIDIVKDPVPGSDYKAEEDPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  161 LYHSVKTGRGPLSDDWARTA---AQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELS 237
Cdd:cd08889   161 LYVSEKTGRGPLSDDWIEEYkdpPGKGPIMCAYKLCKVEFRYWGMQTKIERFIHDVALRKVMLRAHRQAWCWQDEWYGLT 240

                         250       260
                  ....*....|....*....|
gi 195927015  238 MADIRALEEETARMLAQRMA 257
Cdd:cd08889   241 MEDIRKLEEETQLALAQKMA 260
SRPBCC_PITP cd07815
Lipid-binding SRPBCC domain of Class I and Class II Phosphatidylinositol Transfer Proteins; ...
 2-256 1.22e-147

Lipid-binding SRPBCC domain of Class I and Class II Phosphatidylinositol Transfer Proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of the phosphatidylinositol transfer protein (PITP) family of lipid transfer proteins. This family of proteins includes Class 1 PITPs (PITPNA/PITPalpha and PITPNB/PITPbeta, Drosophila vibrator and related proteins), Class IIA PITPs (PITPNM1/PITPalphaI/Nir2, PITPNM2/PITPalphaII/Nir3, Drosophila RdgB, and related proteins), and Class IIB PITPs (PITPNC1/RdgBbeta and related proteins). The PITP family belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Class III PITPs, exemplified by the Sec14p family, are found in yeast and plants but are unrelated in sequence and structure to Class I and II PITPs and belong to a different superfamily.


Pssm-ID: 176857  Cd Length: 251  Bit Score: 444.85  E-value: 1.22e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015    2 LIKEYHILLPMSLDEYQVAQLYMIQKKSREESsGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKAA 81
Cdd:cd07815     1 LIKEFRIVLPLTVEEYQIGQLYMVAKASKEET-GSGEGVEVLKNEPYEDENGGKGQYTHKIYHLGSKLPSWLRALAPKSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   82 LQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRL 161
Cdd:cd07815    80 LTIEEKSWNAYPYCKTVYSCPFFEKFSISIESMHKPDLGTQENAHNLSAEQLAQRKVVVIDIANDSVASKDYKPEEDPKL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  162 YHSVKTGRGPLSDDWARTaaqTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGlRRVMLRAHRQAWCWQDEWTELSMADI 241
Cdd:cd07815   160 FKSKKTGRGPLRKGWRKS---TKPIMCAYKLVTVDFPYWGLQNKVENFIQKVE-RDVFLNYHRQAFCWIDEWFDLTMEDI 235

                         250
                  ....*....|....*
gi 195927015  242 RALEEETARMLAQRM 256
Cdd:cd07815   236 REFEEETKELLDAKR 250
IP_trans pfam02121
Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family ...
 1-248 5.72e-141

Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family (found in pfam00650), this family can bind/exchange one molecule of phosphatidylinositol (PI) or phosphatidylcholine (PC) and thus aids their transfer between different membrane compartments. There are three sub-families - all share an N-terminal PITP-like domain, whose sequence is highly conserved. It is described as consisting of three regions. The N-terminal region is thought to bind the lipid and contains two helices and an eight-stranded, mostly antiparallel beta-sheet. An intervening loop region, which is thought to play a role in protein-protein interactions, separates this from the C-terminal region, which exhibits the greatest sequence variation and may be involved in membrane binding. PITP alpha has a 16-fold greater affinity for PI than PC. Together with PITP beta, it is expressed ubiquitously in all tissues.


Pssm-ID: 460452  Cd Length: 245  Bit Score: 426.99  E-value: 5.72e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015     1 MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESsGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKA 80
Cdd:pfam02121    1 MLIKEYRIPLPLTVEEYQIAQLYMVAKKSKEET-GGGEGVEVLENEPYEDGEGGKGQYTHKIYHLASKLPSWIRALLPKG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015    81 ALQVEEESWNAYPYTRTRYTCPFV-EKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDP 159
Cdd:pfam02121   80 ALYVEEKAWNAYPYTKTVYTCPFMkEKFSITIETVHKPDNGTQENVLNLSSEELAKREVVVIDIANDKVSSKDYKEEEDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   160 RLYHSVKTGRGPLSDDWARTaaqTGPLMCAYKLCKVEFRYWGMQAKIEQFIHdVGLRRVMLRAHRQAWCWQDEWTELSMA 239
Cdd:pfam02121  160 TLFKSEKTGRGPLKEGWKKS---TSPIMCAYKLVTVEFKWWGLQTRVESFIH-KALRDIFLKFHRQAFCWIDEWYGMTME 235


                   ....*....
gi 195927015   240 DIRALEEET 248
Cdd:pfam02121  236 DIRELEEET 244
SRPBCC_PITPNA-B_like cd08888
Lipid-binding SRPBCC domain of mammalian PITPNA, -B, and related proteins (Class I PITPs); ...
 2-252 9.64e-103

Lipid-binding SRPBCC domain of mammalian PITPNA, -B, and related proteins (Class I PITPs); This subgroup includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class 1 phosphatidylinositol transfer proteins (PITPs), PITPNA/PITPalpha and PITPNB/PITPbeta, Drosophila vibrator, and related proteins. These are single domain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. In addition, PITPNB transfers sphingomyelin in vitro, with a low affinity. PITPNA is found chiefly in the nucleus and cytoplasm; it is enriched in the brain and predominantly localized in the axons. A reduced expression of PITPNA contributes to the neurodegenerative phenotype of the mouse vibrator mutation. The role of PITPNA in vivo may be to provide PtdIns for localized PI3K-dependent signaling, thereby controlling the polarized extension of axonal processes. PITPNA homozygous null mice die soon after birth from complicated organ failure, including intestinal and hepatic steatosis, hypoglycemia, and spinocerebellar disease. PITPNB is associated with the Golgi and ER, and is highly expressed in the liver. Deletion of the PITPNB gene results in embryonic lethality. The PtdIns and PtdCho exchange activity of PITPNB is required for COPI-mediated retrograde transport from the Golgi to the ER. Drosophila vibrator localizes to the ER, and has an essential role in cytokinesis during mitosis and meiosis.


Pssm-ID: 176897  Cd Length: 258  Bit Score: 325.93  E-value: 9.64e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015    2 LIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGeGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKAA 81
Cdd:cd08888     1 LIKEFRVILPLSVEEYQVGQLYSVAEASKNETGG-GEGIEVLVNEPYEKDDGEKGQYTHKIYHLQSKVPGFVRMLAPEGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   82 LQVEEESWNAYPYTRTRYTCPFV-EKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDA-VAPGEYKAEEDP 159
Cdd:cd08888    80 LEIHEKAWNAYPYCRTIITNEYMkEDFLIIIETWHKPDLGTQENVHNLDPEEWKEVEVVYIDIADRSqVDPKDYKADEDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  160 RLYHSVKTGRGPLSDDWAR--TAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHdVGLRRVMLRAHRQAWCWQDEWTELS 237
Cdd:cd08888   160 AKFQSEKTGRGPLGPNWKKelVNQKDCPIMCAYKLVTVEFKWWGLQNKVENFIQ-KQERRLFTNFHRQVFCWLDKWHGLT 238

                         250
                  ....*....|....*
gi 195927015  238 MADIRALEEETARML 252
Cdd:cd08888   239 MDDIRRMEDETKKEL 253
SRPBCC_PITPNC1_like cd08890
Lipid-binding SRPBCC domain of mammalian PITPNC1,and related proteins (Class IIB PITPs); This ...
 2-248 2.70e-84

Lipid-binding SRPBCC domain of mammalian PITPNC1,and related proteins (Class IIB PITPs); This subgroup includes the N-terminal SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain of mammalian Class IIB phosphatidylinositol transfer protein (PITP), PITPNC1/RdgBbeta, and related proteins. These are metazoan proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Mammalian PITPNC1 contains an amino-terminal SRPBCC PITP-like domain and a short carboxyl-terminal domain. It is a cytoplasmic protein, and is ubiquitously expressed. It can transfer phosphatidylinositol (PtdIns) in vitro with a similar ability to other PITPs.


Pssm-ID: 176899  Cd Length: 250  Bit Score: 275.14  E-value: 2.70e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015    2 LIKEYHILLPMSLDEYQVAQLYMIQKKSREESSgEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKAa 81
Cdd:cd08890     1 LLKEYRICMPLTVEEYRIGQLYMISRHSHEQSE-RGEGVEVVQNEPCEDPEHGNGQFTEKRVYLNSRLPSWARAVVPKI- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   82 LQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRL 161
Cdd:cd08890    79 FYVTEKAWNYYPYTITEYTCSFLPKFSIHIETKYEDNKGKSENCIFLSEAELSEREVCHLDIAYDEIPEKYYKEEEDPKY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  162 YHSVKTGRGPLSDDWARTAAqtgPLMCAYKLCKVEFRYWGMQAKIEQFIHDVgLRRVMLRAHRQAWCWQDEWTELSMADI 241
Cdd:cd08890   159 FKSEKTGRGPLKEGWRETHK---PIMCSYKLVTVKFEVWGLQTRVEQFVHKV-VRDILLLGHRQAFAWVDEWYDMTMDDV 234


                  ....*..
gi 195927015  242 RALEEET 248
Cdd:cd08890   235 REYERTI 241
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 1023-1154 1.45e-48

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 197870  Cd Length: 157  Bit Score: 169.76  E-value: 1.45e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   1023 VVFS-IDGSFTAS------VSIMGSDpKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQ-----HNFPHGVV 1090
Cdd:smart00775    1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQikqdgHNLPHGPV 79

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195927015   1091 SFCDG----------LTHDPLRQKAMFLQSLVQEVE---LNIVAGYGS-PKDVAVYAALGLSPSQTYIVGRAVRKLQA 1154
Cdd:smart00775   80 LLSPDrlfaalhrevISKKPEVFKIACLRDIKNLFPpqgNPFYAGFGNrITDVISYSAVGIPPSRIFTINPKGEVHQE 157
SMP2 COG5083
Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid ...
 919-1146 2.09e-44

Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid maintenance [Lipid transport and metabolism];


Pssm-ID: 444053  Cd Length: 353  Bit Score: 165.02  E-value: 2.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  919 NHRASDTVVCEGRPQVLSGRFMYGPLDVVTLTGEKVDVYImTQPLSGKWIHFGTEVTNSSGRLTFPVPPERAlgiGVYPV 998
Cdd:COG5083    88 YHMGHDEIVAAGDTQTIVGKFDYGAVFHKDLEDEDVHVYI-YGTGMPDWEYLGSYRTDSDGKIYVPVPAAQE---GRYRV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  999 RMVVRGDHTYAECCLTVVARGTEAVVFSIDGSFTASVSIMGSD------PKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQ 1072
Cdd:COG5083   164 RMVVAGDLSSADLFVSVVPPGRKTVVFDIDGTLTLNDFEGVGDylggetADAHPYAAEVVQAYADKGYRPIYVTGRPYWL 243

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 195927015 1073 KHRVVAWLSQHNFPHGVVSFCDGLTH----DPLRQKAMFLQSLvQEVELNIVAGYG-SPKDVAVYAALGLSPSQTYIVG 1146
Cdd:COG5083   244 AKDTREWLDTQGLPPGILHTTPSATGpigpDTARYKTAEIQLL-IDDGLNIVRAYGnAATDAEAYANAGIPKSETYIIG 321
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
 686-879 6.75e-41

DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that may form a metal binding site. The domain is named after these four residues. This pattern of conservation of metal binding residues is often seen in phosphoesterase domains. This domain is found in retinal degeneration B proteins, as well as a family of probable phospholipases. It has been shown that this domain is found in a longer C terminal region that binds to PYK2 tyrosine kinase. These proteins have been called N-terminal domain-interacting receptor (Nir1, Nir2 and Nir3). This suggests that this region is involved in functionally important interactions in other members of this family.


Pssm-ID: 460725  Cd Length: 241  Bit Score: 151.05  E-value: 6.75e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   686 LDFKVSGFFLFGSPLGLVLALRKtVMPALEAAQ----MRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLTVPRYQK 761
Cdd:pfam02862    1 LDFEVENFFLLGSPLGLFLALRG-AQIAGRSRSdhiyGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   762 FP---------------------------------------LGDGSSLLLADTLQTH------SSLFLEELEMLVPSTPT 796
Cdd:pfam02862   80 RGlrhlelgegltrigaavgqsvsglwsslssgaslnrslgLSDESSASSADSEQSHersseaSSASESSLQAQSSSAPS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015   797 STSGAFWKGSELATDPPAQPAAP----STTSEVVKILERWWGtkRIDYSLYcPEALTA--FPTVTLphlfHASYWESADV 870
Cdd:pfam02862  160 STSSSNGIKEIEETELDWSESERkadkLEREEAKVRALNPNG--RIDYVLQ-EGALESqyLSALTS----HLSYWESEDV 232


                   ....*....
gi 195927015   871 VAFILRQVI 879
Cdd:pfam02862  233 ALFLLRQLL 241
YqfW COG5663
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];
1031-1087 9.86e-05

Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];


Pssm-ID: 444382 [Multi-domain]  Cd Length: 187  Bit Score: 44.45  E-value: 9.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 195927015 1031 FTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIvYVTGRPDMQKHRVVAWLSQHNFPH 1087
Cdd:COG5663    55 FEENEEEIYTEAPPVPGAKEVLNKLKDQHELY-YITARPKHLEEVTENWLEKHGIPY 110
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 606-707 8.16e-03

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 40.37  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927015  606 VRDPLADGVEGLGRGSPEPSALPPQRIPSDMASPEPEGSQNSLQAAPATTSSWEPRRAStafcPPAASSEAPDGPSSTAR 685
Cdd:NF041121   13 AQMGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLA----PPPPPPPGPAGAAPGAA 88

                          90       100
                  ....*....|....*....|..
gi 195927015  686 LDFKVSGFFLFGSPLGLVLALR 707
Cdd:NF041121   89 LPVRVPAPPALPNPLELARALR 110
 
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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