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Conserved domains on  [gi|1958740230|ref|XP_038952525|]
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oxysterol-binding protein-related protein 1 isoform X1 [Rattus norvegicus]

Protein Classification

oxysterol-binding protein-related protein( domain architecture ID 12789548)

oxysterol-binding protein-related protein is a lipid transporter involved in lipid counter-transport between the endoplasmic reticulum and the plasma membrane; similar to Homo sapiens oxysterol-binding protein-related protein 1

Gene Ontology:  GO:0008289|GO:0008142|GO:0006869
PubMed:  26784528|26715851|29536114|26811291|34999137|16709169|24196413|12573443
SCOP:  4000415
TCDB:  2.D.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
549-944 0e+00

Oxysterol-binding protein;


:

Pssm-ID: 460126  Cd Length: 366  Bit Score: 557.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 549 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSFSDPVERMQCVAAFAVSAVASQWERTGKPFNP 628
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPFNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 629 LLGETYELVRDDLGFRLISEQVSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLEHNEAYTWTN 708
Cdd:pfam01237  81 LLGETFELVRPDKGFRFIAEQVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 709 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 787
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 788 fdaykkndkknteeKKNSKQASASEESDEMPVPDSESVfvipgsaLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkEMETV 867
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGESR-------LLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958740230 868 IPKTDCRLRPDIRAMENGEIDQASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYSGAQDWIYSGSYWDRNY 944
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
 230-353 1.07e-75

Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 has 2 forms, a long (ORP1L) and a short (ORP1S). ORP1L contains 3 N-terminal ankyrin repeats, followed by a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains only an OSBP-related domain. ORP1L is proposed to function in motility and distribution of late endosomes, autophagy, and macrophage lipid metabolism. ORP1S is proposed to function in vesicle transport from Golgi. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270102  Cd Length: 125  Bit Score: 243.46  E-value: 1.07e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 230 QVVHKALKRFEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDGCLFSVRCFDDTV 309
Cdd:cd13285     1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958740230 310 HGFRVP-KNSLQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEED 353
Cdd:cd13285    81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 5.05e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 5.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   1 MNTEAEQQLLHHA-RNGNAEEVRKLLEAMAraevvaDIDckgrSKSNLGWTPLHLACYFGHKQVVQDLLKAGAKVNMLND 79
Cdd:COG0666    82 AKDDGGNTLLHAAaRNGDLEIVKLLLEAGA------DVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  80 LGDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSGQTAkeathdkeirqmleavertqqrkleelLLGAAREGRTAEVSA 159
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958740230 160 LLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAHGTEMKHILV 226
Cdd:COG0666   205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
 
Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
549-944 0e+00

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 557.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 549 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSFSDPVERMQCVAAFAVSAVASQWERTGKPFNP 628
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPFNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 629 LLGETYELVRDDLGFRLISEQVSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLEHNEAYTWTN 708
Cdd:pfam01237  81 LLGETFELVRPDKGFRFIAEQVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 709 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 787
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 788 fdaykkndkknteeKKNSKQASASEESDEMPVPDSESVfvipgsaLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkEMETV 867
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGESR-------LLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958740230 868 IPKTDCRLRPDIRAMENGEIDQASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYSGAQDWIYSGSYWDRNY 944
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
 230-353 1.07e-75

Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 has 2 forms, a long (ORP1L) and a short (ORP1S). ORP1L contains 3 N-terminal ankyrin repeats, followed by a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains only an OSBP-related domain. ORP1L is proposed to function in motility and distribution of late endosomes, autophagy, and macrophage lipid metabolism. ORP1S is proposed to function in vesicle transport from Golgi. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270102  Cd Length: 125  Bit Score: 243.46  E-value: 1.07e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 230 QVVHKALKRFEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDGCLFSVRCFDDTV 309
Cdd:cd13285     1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958740230 310 HGFRVP-KNSLQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEED 353
Cdd:cd13285    81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 5.05e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 5.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   1 MNTEAEQQLLHHA-RNGNAEEVRKLLEAMAraevvaDIDckgrSKSNLGWTPLHLACYFGHKQVVQDLLKAGAKVNMLND 79
Cdd:COG0666    82 AKDDGGNTLLHAAaRNGDLEIVKLLLEAGA------DVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  80 LGDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSGQTAkeathdkeirqmleavertqqrkleelLLGAAREGRTAEVSA 159
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958740230 160 LLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAHGTEMKHILV 226
Cdd:COG0666   205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-111 1.48e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  10 LHHA-RNGNAEEVRKLLEAMARAevvadidckgRSKSNLGWTPLHLACYFGHKQVVQdLLKAGAKVNMlNDLGDTPLHRA 88
Cdd:pfam12796   1 LHLAaKNGNLELVKLLLENGADA----------NLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNL-KDNGRTALHYA 68

                          90       100
                  ....*....|....*....|...
gi 1958740230  89 AFTGRKELVMLLLEYNADTTVVN 111
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-216 4.79e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 4.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   8 QLLHHARNGNAEEVRKLLEAMAraevvaDIDCKGRSksnlGWTPLHlaCYFGHKQ---VVQDLLKAGAKVNMLNDLGDTP 84
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGA------DVNAPERC----GFTPLH--LYLYNATtldVIKLLIKAGADVNAKDKVGRTP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  85 LHR--AAFTGRKELVMLLLEYNADTTVVNGSGQT---------------------AKEATHDKEIR------QMLEAVeR 135
Cdd:PHA03095  121 LHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplavllksrnanvellrllidAGADVYAVDDRfrsllhHHLQSF-K 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 136 TQQRKLEELL------LGAAREGRTAEVS-ALLSRPNPP----------DVNCSDQLGNTPLHCAAYRAHKQCVLKLLRS 198
Cdd:PHA03095  200 PRARIVRELIragcdpAATDMLGNTPLHSmATGSSCKRSlvlplliagiSINARNRYGQTPLHYAAVFNNPRACRRLIAL 279

                         250
                  ....*....|....*...
gi 1958740230 199 GADPSLKNKNDQKPLDLA 216
Cdd:PHA03095  280 GADINAVSSDGNTPLSLM 297
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 240-335 6.58e-06

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 45.62  E-value: 6.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  240 EGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYR-----QGCKhLTQAVCTVKPTDGCLFSVRCFDDTVHGF 312
Cdd:smart00233   4 EGWLYKksGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKgsidlSGCT-VREAPDPDSSKKPHCFEIKTSDRKTLLL 82

                           90       100
                   ....*....|....*....|...
gi 1958740230  313 RVPKnslQQSREKWLEAIEEHSA 335
Cdd:smart00233  83 QAES---EEEREKWVEALRKAIA 102
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-76 7.19e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 7.19e-06
                           10        20
                   ....*....|....*....|....*....
gi 1958740230   48 GWTPLHLACYFGHKQVVQDLLKAGAKVNM 76
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 9-181 1.48e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   9 LLHHARNGNAEEVRKLLEAMaraevvadiDCKGRSKSNLGWTPLHLACYFGHKQVVQDLLKAGAK-VN--MLNDL--GDT 83
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCP---------SCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepMTSDLyqGET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  84 PLHRAAFTGRKELVMLLLEYNADTtvvngsgQTAKeATHdkeirqmleAVERTQQRKL----EELLLGAAREGRTAEVSA 159
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADV-------VSPR-ATG---------TFFRPGPKNLiyygEHPLSFAACVGNEEIVRL 154

                         170       180
                  ....*....|....*....|..
gi 1958740230 160 LLSRPNppDVNCSDQLGNTPLH 181
Cdd:cd22192   155 LIEHGA--DIRAQDSLGNTVLH 174
 
Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
549-944 0e+00

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 557.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 549 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSFSDPVERMQCVAAFAVSAVASQWERTGKPFNP 628
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPFNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 629 LLGETYELVRDDLGFRLISEQVSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLEHNEAYTWTN 708
Cdd:pfam01237  81 LLGETFELVRPDKGFRFIAEQVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 709 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 787
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 788 fdaykkndkknteeKKNSKQASASEESDEMPVPDSESVfvipgsaLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkEMETV 867
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGESR-------LLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958740230 868 IPKTDCRLRPDIRAMENGEIDQASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYSGAQDWIYSGSYWDRNY 944
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
 230-353 1.07e-75

Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 has 2 forms, a long (ORP1L) and a short (ORP1S). ORP1L contains 3 N-terminal ankyrin repeats, followed by a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains only an OSBP-related domain. ORP1L is proposed to function in motility and distribution of late endosomes, autophagy, and macrophage lipid metabolism. ORP1S is proposed to function in vesicle transport from Golgi. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270102  Cd Length: 125  Bit Score: 243.46  E-value: 1.07e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 230 QVVHKALKRFEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDGCLFSVRCFDDTV 309
Cdd:cd13285     1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958740230 310 HGFRVP-KNSLQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEED 353
Cdd:cd13285    81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 5.05e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 5.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   1 MNTEAEQQLLHHA-RNGNAEEVRKLLEAMAraevvaDIDckgrSKSNLGWTPLHLACYFGHKQVVQDLLKAGAKVNMLND 79
Cdd:COG0666    82 AKDDGGNTLLHAAaRNGDLEIVKLLLEAGA------DVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  80 LGDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSGQTAkeathdkeirqmleavertqqrkleelLLGAAREGRTAEVSA 159
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958740230 160 LLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAHGTEMKHILV 226
Cdd:COG0666   205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-225 2.95e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.04  E-value: 2.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   9 LLHHARNGNAEEVRKLLEAMARAEVVADIDCKGRSKSNLGWTPLHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHRA 88
Cdd:COG0666    15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  89 AFTGRKELVMLLLEYNADTTVVNGSGQT----AKEATHDKEIRQMLEA---VERtQQRKLEELLLGAAREGRTAEVSALL 161
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGETplhlAAYNGNLEIVKLLLEAgadVNA-QDNDGNTPLHLAAANGNLEIVKLLL 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958740230 162 SrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAHGTEMKHIL 225
Cdd:COG0666   174 E--AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-149 2.76e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.41  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   9 LLHHA-RNGNAEEVRKLLEAmaraevVADIDckgrSKSNLGWTPLHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHR 87
Cdd:COG0666   156 PLHLAaANGNLEIVKLLLEA------GADVN----ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958740230  88 AAFTGRKELVMLLLEYNADTTVVNGSGQTAKEATHDKEIRQMLEAVERTQQRKLEELLLGAA 149
Cdd:COG0666   226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-111 1.48e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  10 LHHA-RNGNAEEVRKLLEAMARAevvadidckgRSKSNLGWTPLHLACYFGHKQVVQdLLKAGAKVNMlNDLGDTPLHRA 88
Cdd:pfam12796   1 LHLAaKNGNLELVKLLLENGADA----------NLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNL-KDNGRTALHYA 68

                          90       100
                  ....*....|....*....|...
gi 1958740230  89 AFTGRKELVMLLLEYNADTTVVN 111
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-206 1.29e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  52 LHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHRAAFTGRKELVMLLLEYnadttvvngsgqtakeathdkeirqmle 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958740230 132 avertqqrkleelllgaaregrtaevsallsrpnpPDVNCSDQlGNTPLHCAAYRAHKQCVLKLLRSGADPSLKN 206
Cdd:pfam12796  53 -----------------------------------ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-216 4.79e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 4.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   8 QLLHHARNGNAEEVRKLLEAMAraevvaDIDCKGRSksnlGWTPLHlaCYFGHKQ---VVQDLLKAGAKVNMLNDLGDTP 84
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGA------DVNAPERC----GFTPLH--LYLYNATtldVIKLLIKAGADVNAKDKVGRTP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  85 LHR--AAFTGRKELVMLLLEYNADTTVVNGSGQT---------------------AKEATHDKEIR------QMLEAVeR 135
Cdd:PHA03095  121 LHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplavllksrnanvellrllidAGADVYAVDDRfrsllhHHLQSF-K 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 136 TQQRKLEELL------LGAAREGRTAEVS-ALLSRPNPP----------DVNCSDQLGNTPLHCAAYRAHKQCVLKLLRS 198
Cdd:PHA03095  200 PRARIVRELIragcdpAATDMLGNTPLHSmATGSSCKRSlvlplliagiSINARNRYGQTPLHYAAVFNNPRACRRLIAL 279

                         250
                  ....*....|....*...
gi 1958740230 199 GADPSLKNKNDQKPLDLA 216
Cdd:PHA03095  280 GADINAVSSDGNTPLSLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 10-225 3.99e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.31  E-value: 3.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  10 LHHARNGNAEEVRKLLeamaraevvADIDCKGRSKSNLGWTPLHLACYFGH-----KQVVQDLLKAGAKVNMLNDLGDTP 84
Cdd:PHA03100   39 LYLAKEARNIDVVKIL---------LDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  85 LHRAAFT--GRKELVMLLLEYNADTTVVNGSGQTakeathdkeirqMLEAVERTQQRKLE--ELLL--GAAREGRTaEVS 158
Cdd:PHA03100  110 LLYAISKksNSYSIVEYLLDNGANVNIKNSDGEN------------LLHLYLESNKIDLKilKLLIdkGVDINAKN-RVN 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958740230 159 ALLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAHGTEMKHIL 225
Cdd:PHA03100  177 YLLS--YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
48-101 4.04e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.91  E-value: 4.04e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958740230  48 GWTPLHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHRAAFTGRKELVMLLL 101
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 18-228 5.65e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 5.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  18 AEEVRKLLEAmaraevVADIDCKGrsksNLGWTPLHLACYFGHKQ---VVQDLLKAGAKVNMLNDLGDTPLHRAAFTGRK 94
Cdd:PHA03095   27 VEEVRRLLAA------GADVNFRG----EYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  95 ELVM-LLLEYNADTTVVNGSGQTA------KEATHDKEIRQMLEAvertqqrkleelllGA---ARE--GRTAeVSALLS 162
Cdd:PHA03095   97 LDVIkLLIKAGADVNAKDKVGRTPlhvylsGFNINPKVIRLLLRK--------------GAdvnALDlyGMTP-LAVLLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 163 RPNPP------------DVNCSDQLGNTPLH--CAAYRAHKQCVLKLLRSGADPSLKNKNDQKPL-DLAHGTEMKHILVG 227
Cdd:PHA03095  162 SRNANvellrllidagaDVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSLVL 241


                  .
gi 1958740230 228 N 228
Cdd:PHA03095  242 P 242
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-247 3.46e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  63 VVQDLLKAGAKVNMLNDLGDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSGQTAKEATHDKEIRQMLEAV--ERTQQRK 140
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIidNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 141 LEELLLGAAREgrTAEVSALLSRPNPPDVNCSDQLGNTPLHCAAYR-AHKQCVLKLLRSGADPSLKNKNDQKPLDL---- 215
Cdd:PHA02876  240 NDLSLLKAIRN--EDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLmakn 317

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958740230 216 AHGTEMKHILVGNKQVVHKALKRFEGPLWKSS 247
Cdd:PHA02876  318 GYDTENIRTLIMLGADVNAADRLYITPLHQAS 349
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-111 8.80e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 8.80e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958740230  36 DIDckgrSKSNLGWTPLHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHRAAFTGRKELVMLLLEYNADTTVVN 111
Cdd:PHA03100  184 PIN----IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 8-103 1.33e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   8 QLLHHARNGNAEEVRKLLEAMAraevvaDIDCKGRSksnlGWTPLHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHR 87
Cdd:PTZ00322   85 ELCQLAASGDAVGARILLTGGA------DPNCRDYD----GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154

                          90
                  ....*....|....*.
gi 1958740230  88 AAFTGRKELVMLLLEY 103
Cdd:PTZ00322  155 AEENGFREVVQLLSRH 170
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 7-236 6.37e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 6.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   7 QQLLHHA-RNGNAEEVRKLLEAmaRAEV-VADIDckgrsksnlGWTPLHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTP 84
Cdd:PHA02874  125 KTFLHYAiKKGDLESIKMLFEY--GADVnIEDDN---------GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  85 LHRAAFTGRKELVMLLLEYNADTTVVNGSGQTakeATHDKEIrqmleavertQQRKLEELLLgaaregrtaevsallsrp 164
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT---PLHNAII----------HNRSAIELLI------------------ 242

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958740230 165 NPPDVNCSDQLGNTPLHCA-AYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAhgteMKHIlvgNKQVVHKAL 236
Cdd:PHA02874  243 NNASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA----FKYI---NKDPVIKDI 308
PH_FAPP1_FAPP2 cd01247
Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain; Human FAPP1 (also ...
 240-330 7.07e-09

Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain; Human FAPP1 (also called PLEKHA3/Pleckstrin homology domain-containing, family A member 3) regulates secretory transport from the trans-Golgi network to the plasma membrane. It is recruited through binding of PH domain to phosphatidylinositol 4-phosphate (PtdIns(4)P) and a small GTPase ADP-ribosylation factor 1 (ARF1). These two binding sites have little overlap the FAPP1 PH domain to associate with both ligands simultaneously and independently. FAPP1 has a N-terminal PH domain followed by a short proline-rich region. FAPP1 is a member of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), and Goodpasture antigen binding protein (GPBP). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. FAPP2 (also called PLEKHA8/Pleckstrin homology domain-containing, family A member 8), a member of the Glycolipid lipid transfer protein(GLTP) family has an N-terminal PH domain that targets the TGN and C-terminal GLTP domain. FAPP2 functions to traffic glucosylceramide (GlcCer) which is made in the Golgi. It's interaction with vesicle-associated membrane protein-associated protein (VAP) could be a means of regulation. Some FAPP2s share the FFAT-like motifs found in GLTP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269951  Cd Length: 100  Bit Score: 53.95  E-value: 7.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 240 EGPLWKSSRFF-GWKLFWVVLEHGVLSWYRKQpDAVHnsyrQGCK-HLTQAVC--TVKPTDGCLFSVrcfddtvhgfRVP 315
Cdd:cd01247     2 EGVLWKWTNYLsGWQPRWFVLDDGVLSYYKSQ-EEVN----QGCKgSVKMSVCeiIVHPTDPTRMDL----------IIP 66

                          90       100
                  ....*....|....*....|..
gi 1958740230 316 -------KNSLQQSREKWLEAI 330
Cdd:cd01247    67 geqhfylKASSAAERQRWLVAL 88
PH_ORP9 cd13290
Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 ...
 240-333 1.61e-08

Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 is proposed to function in regulation of Akt phosphorylation. ORP9 has 2 forms, a long (ORP9L) and a short (ORP9S). ORP9L contains an N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains a FFAT motif and an OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241444  Cd Length: 102  Bit Score: 53.22  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 240 EGPLWKSSRFF-GWKLFWVVLEH--GVLSWYRKQpDAVHNSYRQGCKHLTQAVCTVKPTDGCLFSVRCFDDTVHgFRVpK 316
Cdd:cd13290     2 EGPLSKWTNVMkGWQYRWFVLDDnaGLLSYYTSK-EKMMRGSRRGCVRLKGAVVGIDDEDDSTFTITVDQKTFH-FQA-R 78

                          90
                  ....*....|....*..
gi 1958740230 317 NSLQqsREKWLEAIEEH 333
Cdd:cd13290    79 DAEE--RERWIRALEDT 93
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 50-213 5.77e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 5.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  50 TPLHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHRAAFTGRKELVMLLLEYNADTTVVngsgqtAKEATHDKEIRQM 129
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL------PIPCIEKDMIKTI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 130 LEAVER--TQQRKLEELLLGAAREGRTAEVSALLSRpnPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNK 207
Cdd:PHA02874  111 LDCGIDvnIKDAELKTFLHYAIKKGDLESIKMLFEY--GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188


                  ....*.
gi 1958740230 208 NDQKPL 213
Cdd:PHA02874  189 NGESPL 194
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-236 1.80e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  10 LHHARNGNA--EEVRKLLEAMAraevvaDIDckgrSKSNLGWTPLHLACYFGH-KQVVQDLLKAGAKVNMLNDLGDTPLH 86
Cdd:PHA02876  277 LHHASQAPSlsRLVPKLLERGA------DVN----AKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLH 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  87 RAAFTGR-KELVMLLLEYNADttvVNGSGQTAKEATHDKEIRQML----------EAVERTQQRKLEELLLGAAREGRTA 155
Cdd:PHA02876  347 QASTLDRnKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVviintlldygADIEALSQKIGTALHFALCGTNPYM 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 156 EVSALLSRPnpPDVNCSDQLGNTPLHCAAYRAHKQCVLK-LLRSGADPSLKNKNDQKPLDLA------------HGTEMK 222
Cdd:PHA02876  424 SVKTLIDRG--ANVNSKNKDLSTPLHYACKKNCKLDVIEmLLDNGADVNAINIQNQYPLLIAleyhgivnillhYGAELR 501

                         250
                  ....*....|....
gi 1958740230 223 hilvgNKQVVHKAL 236
Cdd:PHA02876  502 -----DSRVLHKSL 510
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-137 2.17e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.65  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   9 LLH-HARN--GNAEEVRKLLEAmaraevvadiDCKGRSKSNLGWTPLHLACYFGHKQ--VVQDLLKAGAKVNMLNDLGDT 83
Cdd:PHA03095  190 LLHhHLQSfkPRARIVRELIRA----------GCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQT 259

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958740230  84 PLHRAAFTGRKELVMLLLEYNADTTVVNGSGQT-AKEATHDKEIRqMLEAVERTQ 137
Cdd:PHA03095  260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTpLSLMVRNNNGR-AVRAALAKN 313
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-250 2.51e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  35 ADIDCKGRSKSNlgwTPLHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSG 114
Cdd:PHA02878  158 ADINMKDRHKGN---TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 115 QT----AKEATHDKEIRQMLeavertqqrkLEElllGAaregrtaevsallsrpnppDVNC-SDQLGNTPLHCAayrAHK 189
Cdd:PHA02878  235 NTplhiSVGYCKDYDILKLL----------LEH---GV-------------------DVNAkSYILGLTALHSS---IKS 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958740230 190 QCVLK-LLRSGADPSLKNKNDQKPLDLAHGTEMKhILVGNKQVVHKALKRFEGPLWKSSRFF 250
Cdd:PHA02878  280 ERKLKlLLEYGADINSLNSYKLTPLSSAVKQYLC-INIGRILISNICLLKRIKPDIKNSEGF 340
Ank_5 pfam13857
Ankyrin repeats (many copies);
166-216 2.88e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 2.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958740230 166 PPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PH_GPBP cd13283
Goodpasture antigen binding protein Pleckstrin homology (PH) domain; The GPBP (also called ...
 251-337 4.59e-07

Goodpasture antigen binding protein Pleckstrin homology (PH) domain; The GPBP (also called Collagen type IV alpha-3-binding protein/hCERT; START domain-containing protein 11/StARD11; StAR-related lipid transfer protein 11) is a kinase that phosphorylates an N-terminal region of the alpha 3 chain of type IV collagen, which is commonly known as the goodpasture antigen. Its splice variant the ceramide transporter (CERT) mediates the cytosolic transport of ceramide. There have been additional splice variants identified, but all of them function as ceramide transport proteins. GPBP and CERT both contain an N-terminal PH domain, followed by a serine rich domain, and a C-terminal START domain. However, GPBP has an additional serine rich domain just upstream of its START domain. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270100 [Multi-domain]  Cd Length: 100  Bit Score: 48.82  E-value: 4.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 251 GWKLFWVVLEHGVLSWYRKQPDAVHnsyrqGCK---HLTQAVCTVKPTDGCLFSVrCFDDTVHGFRVpknSLQQSREKWL 327
Cdd:cd13283    14 GWQDRYFVLKDGTLSYYKSESEKEY-----GCRgsiSLSKAVIKPHEFDECRFDV-SVNDSVWYLRA---ESPEERQRWI 84

                          90
                  ....*....|
gi 1958740230 328 EAIEEHSAYS 337
Cdd:cd13283    85 DALESHKAAS 94
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 149-216 8.03e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 8.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958740230 149 AREGRTAEVSALLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:PTZ00322   90 AASGDAVGARILLT--GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-79 1.18e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.74  E-value: 1.18e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958740230  48 GWTPLHLACY-FGHKQVVQDLLKAGAKVNMLND 79
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
148-196 2.03e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958740230 148 AAREGRTAEVSALLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLL 196
Cdd:pfam13637   8 AAASGHLELLRLLLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 59-241 2.30e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  59 GHKQVVQDLLKAGAKVNMLNDLGDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSGQTAK----EATHDKEIRQMLEAVE 134
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaiSAKHHKIFRILYHFAS 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 135 RTQQRKLEELLLGAAREGRTAEVSALLSRpnPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQ---- 210
Cdd:PLN03192  616 ISDPHAAGDLLCTAAKRNDLTAMKELLKQ--GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDfspt 693

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958740230 211 KPLDLAHGTEMKH--ILVGNKQVVHKALKRFEG 241
Cdd:PLN03192  694 ELRELLQKRELGHsiTIVDSVPADEPDLGRDGG 726
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-216 2.39e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 2.39e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958740230 145 LLGAAREGRTAEVSALLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVlKLLRSGADPSLKNkNDQKPLDLA 216
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKD-NGRTALHYA 68
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 39-130 4.95e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 4.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  39 CKGRSKSNLGWTPLHLA--CYFGHKQVVQDLLKAGAKVNMLNDL----------------GDTPLHRAAFTGRKELVMLL 100
Cdd:PHA03100  132 ANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRVnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYL 211

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958740230 101 LEYNADTTVVNGSGQTAKE---ATHDKEIRQML 130
Cdd:PHA03100  212 LDLGANPNLVNKYGDTPLHiaiLNNNKEIFKLL 244
PH_Osh1p_Osh2p_yeast cd13292
Yeast oxysterol binding protein homologs 1 and 2 Pleckstrin homology (PH) domain; Yeast Osh1p ...
 251-336 5.44e-06

Yeast oxysterol binding protein homologs 1 and 2 Pleckstrin homology (PH) domain; Yeast Osh1p is proposed to function in postsynthetic sterol regulation, piecemeal microautophagy of the nucleus, and cell polarity establishment. Yeast Osh2p is proposed to function in sterol metabolism and cell polarity establishment. Both Osh1p and Osh2p contain 3 N-terminal ankyrin repeats, a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. OSBP andOsh1p PH domains specifically localize to the Golgi apparatus in a PtdIns4P-dependent manner. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241446  Cd Length: 103  Bit Score: 45.76  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 251 GWKLFWVVLEHGVLSWYRKQPDavHNSYRQGCKHLTQAVCTVKPTDGCLFSVRCFDDTVHGFRVPKNSLQQsREKWLEAI 330
Cdd:cd13292    17 GYKTRWFVLEDGVLSYYRHQDD--EGSACRGSINMKNARLVSDPSEKLRFEVSSKTSGSPKWYLKANHPVE-AARWIQAL 93


                  ....*.
gi 1958740230 331 EEHSAY 336
Cdd:cd13292    94 QKAIEW 99
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-207 6.15e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 6.15e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958740230 176 GNTPLHCAAYRA-HKQCVLKLLRSGADPSLKNK 207
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 240-335 6.58e-06

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 45.62  E-value: 6.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  240 EGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYR-----QGCKhLTQAVCTVKPTDGCLFSVRCFDDTVHGF 312
Cdd:smart00233   4 EGWLYKksGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKgsidlSGCT-VREAPDPDSSKKPHCFEIKTSDRKTLLL 82

                           90       100
                   ....*....|....*....|...
gi 1958740230  313 RVPKnslQQSREKWLEAIEEHSA 335
Cdd:smart00233  83 QAES---EEEREKWVEALRKAIA 102
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-76 7.19e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 7.19e-06
                           10        20
                   ....*....|....*....|....*....
gi 1958740230   48 GWTPLHLACYFGHKQVVQDLLKAGAKVNM 76
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-168 1.14e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  67 LLKAGAKVNMLNDLGDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSGQTAkeathdkeirqmLEAVERTQQRKLEELLL 146
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP------------LELAEENGFREVVQLLS 168

                          90       100
                  ....*....|....*....|..
gi 1958740230 147 GAAREGRTAEVSAllsrpnPPD 168
Cdd:PTZ00322  169 RHSQCHFELGANA------KPD 184
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 9-181 1.48e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230   9 LLHHARNGNAEEVRKLLEAMaraevvadiDCKGRSKSNLGWTPLHLACYFGHKQVVQDLLKAGAK-VN--MLNDL--GDT 83
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCP---------SCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepMTSDLyqGET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  84 PLHRAAFTGRKELVMLLLEYNADTtvvngsgQTAKeATHdkeirqmleAVERTQQRKL----EELLLGAAREGRTAEVSA 159
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADV-------VSPR-ATG---------TFFRPGPKNLiyygEHPLSFAACVGNEEIVRL 154

                         170       180
                  ....*....|....*....|..
gi 1958740230 160 LLSRPNppDVNCSDQLGNTPLH 181
Cdd:cd22192   155 LIEHGA--DIRAQDSLGNTVLH 174
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 240-330 5.55e-05

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 42.91  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 240 EGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQ-GCKHLTQAVCTVKPTDGCLFSVRCFDDTVHGFRVPK 316
Cdd:cd00821     2 EGYLLKrgGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSiPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQADS 81

                          90
                  ....*....|....
gi 1958740230 317 nslQQSREKWLEAI 330
Cdd:cd00821    82 ---EEERQEWLKAL 92
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-76 6.74e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 6.74e-05
                          10        20
                  ....*....|....*....|....*....
gi 1958740230  48 GWTPLHLACYFGHKQVVQDLLKAGAKVNM 76
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
48-88 6.97e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 6.97e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958740230  48 GWTPLHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHRA 88
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-117 1.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958740230  67 LLKAG-AKVNMLNDLGDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSGQTA 117
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 176-204 2.77e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 2.77e-04
                           10        20
                   ....*....|....*....|....*....
gi 1958740230  176 GNTPLHCAAYRAHKQCVLKLLRSGADPSL 204
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-111 9.12e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 9.12e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958740230  81 GDTPLHRAA-FTGRKELVMLLLEYNADTTVVN 111
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-117 9.16e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 9.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958740230  81 GDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSGQTA 117
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-163 1.02e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  48 GWTPLHLACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSGQTA---KEATHDK 124
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPliiAMAKGDI 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958740230 125 EIRQML----EAVERTQQRKLEELLLGAAREGRTAEVSALLSR 163
Cdd:PHA02875  182 AICKMLldsgANIDYFGKNGCVAALCYAIENNKIDIVRLFIKR 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
176-236 1.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958740230 176 GNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAhgtemkhILVGNKQVVHKAL 236
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA-------ASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 81-106 1.53e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.53e-03
                           10        20
                   ....*....|....*....|....*.
gi 1958740230   81 GDTPLHRAAFTGRKELVMLLLEYNAD 106
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 55-216 1.58e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  55 ACYFGHKQVVQDLLKAGAKVNMLNDLGDTPLHRAAFTGRKELVMLLLEYNADTTVvngsgqtakeatHDKEIRQML-EAV 133
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV------------KYPDIESELhDAV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 134 ERTQQRKLEELLLgaarEGRTAEvsallsrpnppDVNCSDqlGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPL 213
Cdd:PHA02875   77 EEGDVKAVEELLD----LGKFAD-----------DVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139


                  ...
gi 1958740230 214 DLA 216
Cdd:PHA02875  140 HLA 142
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 10-116 2.19e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  10 LHHA-RNGNAEEVRKLLEAMARAEVvadidckgrsKSNLGWTPLHLAC-YFGHKQVVQDLLKAGAKVNMLND-LGDTPLH 86
Cdd:PHA02878  205 LHHAvKHYNKPIVHILLENGASTDA----------RDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALH 274

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958740230  87 RAAFTGRKelVMLLLEYNADTTVVNGSGQT 116
Cdd:PHA02878  275 SSIKSERK--LKLLLEYGADINSLNSYKLT 302
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-206 2.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230  62 QVVQDLLKAGAKVNMLN-DLGDTPLHRAAFTGRKELVMLLLEYNADttvVNGSGQTAKEATHdkeirqmlEAVERTQQRK 140
Cdd:PHA02878  148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGAN---VNIPDKTNNSPLH--------HAVKHYNKPI 216

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958740230 141 LEELLlgaaregrtaevsallsrPNPPDVNCSDQLGNTPLHCAAYRAHKQCVLK-LLRSGADPSLKN 206
Cdd:PHA02878  217 VHILL------------------ENGASTDARDKCGNTPLHISVGYCKDYDILKlLLEHGVDVNAKS 265
PHA02946 PHA02946
ankyin-like protein; Provisional
 127-220 4.85e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958740230 127 RQMLEAVERTQQRKLEELLLG-AAREGRTAEvsALLSRPNPPdvNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLK 205
Cdd:PHA02946   26 RNMLQAIEPSGNYHILHAYCGiKGLDERFVE--ELLHRGYSP--NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNAC 101

                          90
                  ....*....|....*
gi 1958740230 206 NKNDQKPLDLAHGTE 220
Cdd:PHA02946  102 DKQHKTPLYYLSGTD 116
 
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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