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Conserved domains on  [gi|24308237|ref|NP_065896|]
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membrane-associated phosphatidylinositol transfer protein 2 isoform 1 [Homo sapiens]

Protein Classification

SRPBCC_PITPNM1-2_like and LNS2 domain-containing protein( domain architecture ID 10172326)

protein containing domains SRPBCC_PITPNM1-2_like, DDHD, and LNS2

Graphical summary

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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); ...
 1-258 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: 582.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    1 MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETYGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKA 80
Cdd:cd08889    1 MLIKEYRIPLPMSVEEYRIAQLYMIQKKSREESKGEGSGVEILENRPYTDGPGGSGQYTHKIYHIGSHIPGWFRAILPKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237   81 ALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPK 160
Cdd:cd08889   81 ALRVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDFIDIVKDPVPGSDYKAEEDPK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237  161 LFQSTKTQRGPLSENWIEEYK--KQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLS 238
Cdd:cd08889  161 LYVSEKTGRGPLSDDWIEEYKdpPGKGPIMCAYKLCKVEFRYWGMQTKIERFIHDVALRKVMLRAHRQAWCWQDEWYGLT 240

                        250       260
                 ....*....|....*....|
gi 24308237  239 MENIRELEKEAQLMLSRKMA 258
Cdd:cd08889  241 MEDIRKLEEETQLALAQKMA 260
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
 715-962 1.37e-55

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: 193.42  E-value: 1.37e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    715 FDFEITDLFLFGCPLGLVLALR-KTVIP--ALDVFQLRPACQQVYNLFHPADPSASRLEPLLERRFHALPPFSVPRYQRY 791
Cdd:pfam02862    1 LDFEVENFFLLGSPLGLFLALRgAQIAGrsRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    792 P-----LGDGCSTLLADVLQTHNA------------AFQEHGAPSSPGTAPASRGFRRASEISIASQVSGMAESYTASSI 854
Cdd:pfam02862   81 GlrhleLGEGLTRIGAAVGQSVSGlwsslssgaslnRSLGLSDESSASSADSEQSHERSSEASSASESSLQAQSSSAPSS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    855 AqkapdalshtpsvrrlsllalpAPSPTTPGPHPPARKASPGLERAPGLPELDIGEVAAKWWGqkRIDYALYcPDALTA- 933
Cdd:pfam02862  161 T----------------------SSSNGIKEIEETELDWSESERKADKLEREEAKVRALNPNG--RIDYVLQ-EGALESq 215

                          250       260       270
                   ....*....|....*....|....*....|
gi 24308237    934 -FPTVALphlfHASYWESTDVVSFLLRQVM 962
Cdd:pfam02862  216 yLSALTS----HLSYWESEDVALFLLRQLL 241
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 1108-1239 9.80e-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: 167.45  E-value: 9.80e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    1108 VVFS-IDGSFAAS------VSIMGSDpKVRAGAVDVVRHWQDLGYLIIYVTGRPDMQKQRVVAWLAQ-----HNFPHGVV 1175
Cdd:smart00775    1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQikqdgHNLPHGPV 79

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24308237    1176 SFCDG----------LVHDPLRHKANFLKLLISEL---HLRVHAAYGS-TKDVAVYSAISLSPMQIYIVGRPTKKLQQ 1239
Cdd:smart00775   80 LLSPDrlfaalhrevISKKPEVFKIACLRDIKNLFppqGNPFYAGFGNrITDVISYSAVGIPPSRIFTINPKGEVHQE 157
 
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); ...
 1-258 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: 582.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    1 MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETYGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKA 80
Cdd:cd08889    1 MLIKEYRIPLPMSVEEYRIAQLYMIQKKSREESKGEGSGVEILENRPYTDGPGGSGQYTHKIYHIGSHIPGWFRAILPKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237   81 ALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPK 160
Cdd:cd08889   81 ALRVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDFIDIVKDPVPGSDYKAEEDPK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237  161 LFQSTKTQRGPLSENWIEEYK--KQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLS 238
Cdd:cd08889  161 LYVSEKTGRGPLSDDWIEEYKdpPGKGPIMCAYKLCKVEFRYWGMQTKIERFIHDVALRKVMLRAHRQAWCWQDEWYGLT 240

                        250       260
                 ....*....|....*....|
gi 24308237  239 MENIRELEKEAQLMLSRKMA 258
Cdd:cd08889  241 MEDIRKLEEETQLALAQKMA 260
IP_trans pfam02121
Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family ...
 1-250 4.62e-143

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: 434.69  E-value: 4.62e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237      1 MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETyGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKA 80
Cdd:pfam02121    1 MLIKEYRIPLPLTVEEYQIAQLYMVAKKSKEET-GGGEGVEVLENEPYEDGEGGKGQYTHKIYHLASKLPSWIRALLPKG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237     81 ALRVVEESWNAYPYTRTRFTCPFV-EKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDP 159
Cdd:pfam02121   80 ALYVEEKAWNAYPYTKTVYTCPFMkEKFSITIETVHKPDNGTQENVLNLSSEELAKREVVVIDIANDKVSSKDYKEEEDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    160 KLFQSTKTQRGPLSENWIEEYKkqvfPIMCAYKLCKVEFRYWGMQSKIERFIHdTGLRRVMVRAHRQAWCWQDEWYGLSM 239
Cdd:pfam02121  160 TLFKSEKTGRGPLKEGWKKSTS----PIMCAYKLVTVEFKWWGLQTRVESFIH-KALRDIFLKFHRQAFCWIDEWYGMTM 234

                          250
                   ....*....|.
gi 24308237    240 ENIRELEKEAQ 250
Cdd:pfam02121  235 EDIRELEEETQ 245
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
 715-962 1.37e-55

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: 193.42  E-value: 1.37e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    715 FDFEITDLFLFGCPLGLVLALR-KTVIP--ALDVFQLRPACQQVYNLFHPADPSASRLEPLLERRFHALPPFSVPRYQRY 791
Cdd:pfam02862    1 LDFEVENFFLLGSPLGLFLALRgAQIAGrsRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    792 P-----LGDGCSTLLADVLQTHNA------------AFQEHGAPSSPGTAPASRGFRRASEISIASQVSGMAESYTASSI 854
Cdd:pfam02862   81 GlrhleLGEGLTRIGAAVGQSVSGlwsslssgaslnRSLGLSDESSASSADSEQSHERSSEASSASESSLQAQSSSAPSS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    855 AqkapdalshtpsvrrlsllalpAPSPTTPGPHPPARKASPGLERAPGLPELDIGEVAAKWWGqkRIDYALYcPDALTA- 933
Cdd:pfam02862  161 T----------------------SSSNGIKEIEETELDWSESERKADKLEREEAKVRALNPNG--RIDYVLQ-EGALESq 215

                          250       260       270
                   ....*....|....*....|....*....|
gi 24308237    934 -FPTVALphlfHASYWESTDVVSFLLRQVM 962
Cdd:pfam02862  216 yLSALTS----HLSYWESEDVALFLLRQLL 241
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 1108-1239 9.80e-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: 167.45  E-value: 9.80e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    1108 VVFS-IDGSFAAS------VSIMGSDpKVRAGAVDVVRHWQDLGYLIIYVTGRPDMQKQRVVAWLAQ-----HNFPHGVV 1175
Cdd:smart00775    1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQikqdgHNLPHGPV 79

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24308237    1176 SFCDG----------LVHDPLRHKANFLKLLISEL---HLRVHAAYGS-TKDVAVYSAISLSPMQIYIVGRPTKKLQQ 1239
Cdd:smart00775   80 LLSPDrlfaalhrevISKKPEVFKIACLRDIKNLFppqGNPFYAGFGNrITDVISYSAVGIPPSRIFTINPKGEVHQE 157
YqfW COG5663
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];
1116-1204 1.33e-05

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


Pssm-ID: 444382 [Multi-domain]  Cd Length: 187  Bit Score: 47.15  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237 1116 FAASVSIMGSDPKVRAGAVDVVRHWQDlGYLIIYVTGRPDMQKQRVVAWLAQHNFP-HGVVsfcdgLVHDplRHKANFLK 1194
Cdd:COG5663   55 FEENEEEIYTEAPPVPGAKEVLNKLKD-QHELYYITARPKHLEEVTENWLEKHGIPyDELI-----LLGS--HDKVEAAK 126

                         90
                 ....*....|
gi 24308237 1195 llisELHLRV 1204
Cdd:COG5663  127 ----ELGIDL 132
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 1108-1205 6.60e-03

C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319805  Cd Length: 145  Bit Score: 38.66  E-value: 6.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237 1108 VVFSIDGSFA-----------------ASVSIMGSDPKVRAGaVDVVRHWQDLGYLIIYVTGRPDMQKQRVVAWLAQHNF 1170
Cdd:cd07502    4 VIFDLDGTLAdtngrqpylerrprdwdAFFEAADHDPPNAPV-IELVKESALTGYEIVYLSGRPERYRRDTLRWLAKHGI 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 24308237 1171 PhgvvsfcDGLVH---DPLRHKANFLKLLISELHLRVH 1205
Cdd:cd07502   83 P-------DDALHmrgNADRRKDRRVKLEILRRLIRTR 113
 
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); ...
 1-258 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: 582.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    1 MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETYGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKA 80
Cdd:cd08889    1 MLIKEYRIPLPMSVEEYRIAQLYMIQKKSREESKGEGSGVEILENRPYTDGPGGSGQYTHKIYHIGSHIPGWFRAILPKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237   81 ALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPK 160
Cdd:cd08889   81 ALRVEEEAWNAYPYTRTRYTCPFVEKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDFIDIVKDPVPGSDYKAEEDPK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237  161 LFQSTKTQRGPLSENWIEEYK--KQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLS 238
Cdd:cd08889  161 LYVSEKTGRGPLSDDWIEEYKdpPGKGPIMCAYKLCKVEFRYWGMQTKIERFIHDVALRKVMLRAHRQAWCWQDEWYGLT 240

                        250       260
                 ....*....|....*....|
gi 24308237  239 MENIRELEKEAQLMLSRKMA 258
Cdd:cd08889  241 MEDIRKLEEETQLALAQKMA 260
IP_trans pfam02121
Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family ...
 1-250 4.62e-143

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: 434.69  E-value: 4.62e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237      1 MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETyGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKA 80
Cdd:pfam02121    1 MLIKEYRIPLPLTVEEYQIAQLYMVAKKSKEET-GGGEGVEVLENEPYEDGEGGKGQYTHKIYHLASKLPSWIRALLPKG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237     81 ALRVVEESWNAYPYTRTRFTCPFV-EKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDP 159
Cdd:pfam02121   80 ALYVEEKAWNAYPYTKTVYTCPFMkEKFSITIETVHKPDNGTQENVLNLSSEELAKREVVVIDIANDKVSSKDYKEEEDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    160 KLFQSTKTQRGPLSENWIEEYKkqvfPIMCAYKLCKVEFRYWGMQSKIERFIHdTGLRRVMVRAHRQAWCWQDEWYGLSM 239
Cdd:pfam02121  160 TLFKSEKTGRGPLKEGWKKSTS----PIMCAYKLVTVEFKWWGLQTRVESFIH-KALRDIFLKFHRQAFCWIDEWYGMTM 234

                          250
                   ....*....|.
gi 24308237    240 ENIRELEKEAQ 250
Cdd:pfam02121  235 EDIRELEEETQ 245
SRPBCC_PITP cd07815
Lipid-binding SRPBCC domain of Class I and Class II Phosphatidylinositol Transfer Proteins; ...
 3-257 5.04e-132

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: 405.94  E-value: 5.04e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    3 IKEYRIPLPMTVEEYRIAQLYMIQKKSRNETyGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKAAL 82
Cdd:cd07815    2 IKEFRIVLPLTVEEYQIGQLYMVAKASKEET-GSGEGVEVLKNEPYEDENGGKGQYTHKIYHLGSKLPSWLRALAPKSAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237   83 RVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPKLF 162
Cdd:cd07815   81 TIEEKSWNAYPYCKTVYSCPFFEKFSISIESMHKPDLGTQENAHNLSAEQLAQRKVVVIDIANDSVASKDYKPEEDPKLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237  163 QSTKTQRGPLSENWIEEYKkqvfPIMCAYKLCKVEFRYWGMQSKIERFIHdTGLRRVMVRAHRQAWCWQDEWYGLSMENI 242
Cdd:cd07815  161 KSKKTGRGPLRKGWRKSTK----PIMCAYKLVTVDFPYWGLQNKVENFIQ-KVERDVFLNYHRQAFCWIDEWFDLTMEDI 235

                        250
                 ....*....|....*
gi 24308237  243 RELEKEAQLMLSRKM 257
Cdd:cd07815  236 REFEEETKELLDAKR 250
SRPBCC_PITPNA-B_like cd08888
Lipid-binding SRPBCC domain of mammalian PITPNA, -B, and related proteins (Class I PITPs); ...
 2-256 4.52e-101

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: 322.47  E-value: 4.52e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    2 IIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETyGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKAA 81
Cdd:cd08888    1 LIKEFRVILPLSVEEYQVGQLYSVAEASKNET-GGGEGIEVLVNEPYEKDDGEKGQYTHKIYHLQSKVPGFVRMLAPEGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237   82 LRVVEESWNAYPYTRTRFTCPFV-EKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPV--PHNeYKTEED 158
Cdd:cd08888   80 LEIHEKAWNAYPYCRTIITNEYMkEDFLIIIETWHKPDLGTQENVHNLDPEEWKEVEVVYIDIADRSQvdPKD-YKADED 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237  159 PKLFQSTKTQRGPLSENWIEE-YKKQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTgLRRVMVRAHRQAWCWQDEWYGL 237
Cdd:cd08888  159 PAKFQSEKTGRGPLGPNWKKElVNQKDCPIMCAYKLVTVEFKWWGLQNKVENFIQKQ-ERRLFTNFHRQVFCWLDKWHGL 237

                        250
                 ....*....|....*....
gi 24308237  238 SMENIRELEKEAQLMLSRK 256
Cdd:cd08888  238 TMDDIRRMEDETKKELDEM 256
SRPBCC_PITPNC1_like cd08890
Lipid-binding SRPBCC domain of mammalian PITPNC1,and related proteins (Class IIB PITPs); This ...
 2-258 2.10e-91

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: 295.56  E-value: 2.10e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    2 IIKEYRIPLPMTVEEYRIAQLYMIQKKSrNETYGEGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPSWFRSILPKAa 81
Cdd:cd08890    1 LLKEYRICMPLTVEEYRIGQLYMISRHS-HEQSERGEGVEVVQNEPCEDPEHGNGQFTEKRVYLNSRLPSWARAVVPKI- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237   82 LRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAGENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPKL 161
Cdd:cd08890   79 FYVTEKAWNYYPYTITEYTCSFLPKFSIHIETKYEDNKGKSENCIFLSEAELSEREVCHLDIAYDEIPEKYYKEEEDPKY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237  162 FQSTKTQRGPLSENWIEEYKkqvfPIMCAYKLCKVEFRYWGMQSKIERFIHdTGLRRVMVRAHRQAWCWQDEWYGLSMEN 241
Cdd:cd08890  159 FKSEKTGRGPLKEGWRETHK----PIMCSYKLVTVKFEVWGLQTRVEQFVH-KVVRDILLLGHRQAFAWVDEWYDMTMDD 233

                        250
                 ....*....|....*..
gi 24308237  242 IRELEKEAQLMLSRKMA 258
Cdd:cd08890  234 VREYERTIQEKTNEKIG 250
DDHD pfam02862
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ...
 715-962 1.37e-55

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: 193.42  E-value: 1.37e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    715 FDFEITDLFLFGCPLGLVLALR-KTVIP--ALDVFQLRPACQQVYNLFHPADPSASRLEPLLERRFHALPPFSVPRYQRY 791
Cdd:pfam02862    1 LDFEVENFFLLGSPLGLFLALRgAQIAGrsRSDHIYGSPACKQLYNIFHPYDPVAYRLEPLIDPAYSNLKPVLIPYYKKR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    792 P-----LGDGCSTLLADVLQTHNA------------AFQEHGAPSSPGTAPASRGFRRASEISIASQVSGMAESYTASSI 854
Cdd:pfam02862   81 GlrhleLGEGLTRIGAAVGQSVSGlwsslssgaslnRSLGLSDESSASSADSEQSHERSSEASSASESSLQAQSSSAPSS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    855 AqkapdalshtpsvrrlsllalpAPSPTTPGPHPPARKASPGLERAPGLPELDIGEVAAKWWGqkRIDYALYcPDALTA- 933
Cdd:pfam02862  161 T----------------------SSSNGIKEIEETELDWSESERKADKLEREEAKVRALNPNG--RIDYVLQ-EGALESq 215

                          250       260       270
                   ....*....|....*....|....*....|
gi 24308237    934 -FPTVALphlfHASYWESTDVVSFLLRQVM 962
Cdd:pfam02862  216 yLSALTS----HLSYWESEDVALFLLRQLL 241
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 1108-1239 9.80e-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: 167.45  E-value: 9.80e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237    1108 VVFS-IDGSFAAS------VSIMGSDpKVRAGAVDVVRHWQDLGYLIIYVTGRPDMQKQRVVAWLAQ-----HNFPHGVV 1175
Cdd:smart00775    1 IVISdIDGTITKSdvlghvVPIIGKD-WTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQikqdgHNLPHGPV 79

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24308237    1176 SFCDG----------LVHDPLRHKANFLKLLISEL---HLRVHAAYGS-TKDVAVYSAISLSPMQIYIVGRPTKKLQQ 1239
Cdd:smart00775   80 LLSPDrlfaalhrevISKKPEVFKIACLRDIKNLFppqGNPFYAGFGNrITDVISYSAVGIPPSRIFTINPKGEVHQE 157
YqfW COG5663
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];
1116-1204 1.33e-05

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


Pssm-ID: 444382 [Multi-domain]  Cd Length: 187  Bit Score: 47.15  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237 1116 FAASVSIMGSDPKVRAGAVDVVRHWQDlGYLIIYVTGRPDMQKQRVVAWLAQHNFP-HGVVsfcdgLVHDplRHKANFLK 1194
Cdd:COG5663   55 FEENEEEIYTEAPPVPGAKEVLNKLKD-QHELYYITARPKHLEEVTENWLEKHGIPyDELI-----LLGS--HDKVEAAK 126

                         90
                 ....*....|
gi 24308237 1195 llisELHLRV 1204
Cdd:COG5663  127 ----ELGIDL 132
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 1108-1205 6.60e-03

C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319805  Cd Length: 145  Bit Score: 38.66  E-value: 6.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308237 1108 VVFSIDGSFA-----------------ASVSIMGSDPKVRAGaVDVVRHWQDLGYLIIYVTGRPDMQKQRVVAWLAQHNF 1170
Cdd:cd07502    4 VIFDLDGTLAdtngrqpylerrprdwdAFFEAADHDPPNAPV-IELVKESALTGYEIVYLSGRPERYRRDTLRWLAKHGI 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 24308237 1171 PhgvvsfcDGLVH---DPLRHKANFLKLLISELHLRVH 1205
Cdd:cd07502   83 P-------DDALHmrgNADRRKDRRVKLEILRRLIRTR 113
 
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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