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Conserved domains on  [gi|119621586|gb|EAX01181|]
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oxysterol binding protein-like 1A, isoform CRA_b [Homo sapiens]

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;
548-919 3.84e-164

Oxysterol-binding protein;


:

Pssm-ID: 460126  Cd Length: 366  Bit Score: 483.58  E-value: 3.84e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  548 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKP--- 624
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPfnp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  625 ---------------------VSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLEHNEAYTWTN 683
Cdd:pfam01237  81 llgetfelvrpdkgfrfiaeqVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  684 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 762
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  763 fdaykkndkknteeKKNSKQMSTSEELDEMPVPDSEsvfiipgSVLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkDMESV 842
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGE-------SRLLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119621586  843 IPKTDCRLRPDIRAMENGEIDQASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYNGAQDWIYSGSYWDRNY 919
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
 229-352 6.08e-78

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: 249.23  E-value: 6.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 229 KVIYKALKRYEGPLWKSSRFFGWRLFWVVLEHGVLSWYRKQPDAVHNIYRQGCKHLTQAVCTVKSTDSCLFFIKCFDDTI 308
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119621586 309 HGFRVP-KNSLQQSREDWLEAIEEHSAYSTHYCSQDQLTDEEEED 352
Cdd:cd13285   81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 4.06e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 4.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   1 MNTEAEQQLLHHA-RNGNAEEVRQLLETmarnevIADINckgrSKSNLGWTPLHLACYFGHRQVVQDLLKAGAEVNVLND 79
Cdd:COG0666   82 AKDDGGNTLLHAAaRNGDLEIVKLLLEA------GADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  80 MGDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSGQTAkevthaeeirsmleavertqqrkleelLLAAAREGKTTELTA 159
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621586 160 LLNrpNPPDVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLAQGAEMKHILV 226
Cdd:COG0666  205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
 
Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
548-919 3.84e-164

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 483.58  E-value: 3.84e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  548 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKP--- 624
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPfnp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  625 ---------------------VSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLEHNEAYTWTN 683
Cdd:pfam01237  81 llgetfelvrpdkgfrfiaeqVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  684 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 762
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  763 fdaykkndkknteeKKNSKQMSTSEELDEMPVPDSEsvfiipgSVLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkDMESV 842
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGE-------SRLLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119621586  843 IPKTDCRLRPDIRAMENGEIDQASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYNGAQDWIYSGSYWDRNY 919
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
 229-352 6.08e-78

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: 249.23  E-value: 6.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 229 KVIYKALKRYEGPLWKSSRFFGWRLFWVVLEHGVLSWYRKQPDAVHNIYRQGCKHLTQAVCTVKSTDSCLFFIKCFDDTI 308
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119621586 309 HGFRVP-KNSLQQSREDWLEAIEEHSAYSTHYCSQDQLTDEEEED 352
Cdd:cd13285   81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 4.06e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 4.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   1 MNTEAEQQLLHHA-RNGNAEEVRQLLETmarnevIADINckgrSKSNLGWTPLHLACYFGHRQVVQDLLKAGAEVNVLND 79
Cdd:COG0666   82 AKDDGGNTLLHAAaRNGDLEIVKLLLEA------GADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  80 MGDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSGQTAkevthaeeirsmleavertqqrkleelLLAAAREGKTTELTA 159
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621586 160 LLNrpNPPDVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLAQGAEMKHILV 226
Cdd:COG0666  205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-111 2.19e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   10 LHHA-RNGNAEEVRQLLEtmarneVIADINCKgrskSNLGWTPLHLACYFGHRQVVQdLLKAGAEVNVlNDMGDTPLHRA 88
Cdd:pfam12796   1 LHLAaKNGNLELVKLLLE------NGADANLQ----DKNGRTALHLAAKNGHLEIVK-LLLEHADVNL-KDNGRTALHYA 68

                          90       100
                  ....*....|....*....|...
gi 119621586   89 AFTGRKELVMLLLEYNADTTIVN 111
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-216 3.62e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.83  E-value: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   8 QLLHHARNGNAEEVRQLLETMArneviaDINCKGRSksnlGWTPLHLACYFGHR-QVVQDLLKAGAEVNVLNDMGDTPLH 86
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGA------DVNAPERC----GFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLH 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  87 R--AAFTGRKELVMLLLEYNADTTIVNGSGQTA-------KEVThAEEIRSMLEAVERTQQRK------LEELLLAA-AR 150
Cdd:PHA03095 123 VylSGFNINPKVIRLLLRKGADVNALDLYGMTPlavllksRNAN-VELLRLLIDAGADVYAVDdrfrslLHHHLQSFkPR 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 151 EGKTTELTALLNRPNPPDVncsdqLGNTPLHCAAyrAHKQCA----LKLLRSGADPNLKNKNDQKPLDLA 216
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDM-----LGNTPLHSMA--TGSSCKrslvLPLLIAGISINARNRYGQTPLHYA 264
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-76 1.29e-05

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: 42.57  E-value: 1.29e-05
                           10        20
                   ....*....|....*....|....*....
gi 119621586    48 GWTPLHLACYFGHRQVVQDLLKAGAEVNV 76
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 238-334 4.44e-05

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: 43.31  E-value: 4.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   238 YEGPLWK--SSRFFGWRLFWVVLEHGVLSWYRKQPDAVHNIYR-----QGCKhLTQAVCTVKSTDSCLFFIKCFDDTIHG 310
Cdd:smart00233   3 KEGWLYKksGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKgsidlSGCT-VREAPDPDSSKKPHCFEIKTSDRKTLL 81

                           90       100
                   ....*....|....*....|....
gi 119621586   311 FRVPKnslQQSREDWLEAIEEHSA 334
Cdd:smart00233  82 LQAES---EEEREKWVEALRKAIA 102
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 9-238 9.14e-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: 46.16  E-value: 9.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   9 LLHHARNGNAEEVRQLLETMArneviADINCKGrsksNLGWTPLHLACYFGHRQVVQDLLKAGAE-VN--VLNDM--GDT 83
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPS-----CDLFQRG----ALGETALHVAALYDNLEAAVVLMEAAPElVNepMTSDLyqGET 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  84 PLHRAAFTGRKELVMLLLEYNADTTIVNGSGqtakevthaeeirsmleAVERTQQRKL----EELLLAAAREGKTTELTA 159
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGADVVSPRATG-----------------TFFRPGPKNLiyygEHPLSFAACVGNEEIVRL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 160 LLNRPNppDVNCSDQLGNTPLHCAAYRAHKQCAL----------KLLRSGADPNLKNKNDQKPLDLAqGAEmkhilvGNK 229
Cdd:cd22192  155 LIEHGA--DIRAQDSLGNTVLHILVLQPNKTFACqmydlilsydKEDDLQPLDLVPNNQGLTPFKLA-AKE------GNI 225

                        250
                 ....*....|.
gi 119621586 230 VIYKAL--KRY 238
Cdd:cd22192  226 VMFQHLvqKRR 236
 
Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
548-919 3.84e-164

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 483.58  E-value: 3.84e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  548 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKP--- 624
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPfnp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  625 ---------------------VSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLEHNEAYTWTN 683
Cdd:pfam01237  81 llgetfelvrpdkgfrfiaeqVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  684 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 762
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  763 fdaykkndkknteeKKNSKQMSTSEELDEMPVPDSEsvfiipgSVLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkDMESV 842
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGE-------SRLLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119621586  843 IPKTDCRLRPDIRAMENGEIDQASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYNGAQDWIYSGSYWDRNY 919
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
 229-352 6.08e-78

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: 249.23  E-value: 6.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 229 KVIYKALKRYEGPLWKSSRFFGWRLFWVVLEHGVLSWYRKQPDAVHNIYRQGCKHLTQAVCTVKSTDSCLFFIKCFDDTI 308
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119621586 309 HGFRVP-KNSLQQSREDWLEAIEEHSAYSTHYCSQDQLTDEEEED 352
Cdd:cd13285   81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 4.06e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 4.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   1 MNTEAEQQLLHHA-RNGNAEEVRQLLETmarnevIADINckgrSKSNLGWTPLHLACYFGHRQVVQDLLKAGAEVNVLND 79
Cdd:COG0666   82 AKDDGGNTLLHAAaRNGDLEIVKLLLEA------GADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  80 MGDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSGQTAkevthaeeirsmleavertqqrkleelLLAAAREGKTTELTA 159
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119621586 160 LLNrpNPPDVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLAQGAEMKHILV 226
Cdd:COG0666  205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-225 1.22e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   9 LLHHARNGNAEEVRQLLETMARNEVIADINCKGRSKSNLGWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRA 88
Cdd:COG0666   15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  89 AFTGRKELVMLLLEYNADTTIVNGSGQTAKEVT----HAEEIRSMLEA---VERtQQRKLEELLLAAAREGKTTELTALL 161
Cdd:COG0666   95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayngNLEIVKLLLEAgadVNA-QDNDGNTPLHLAAANGNLEIVKLLL 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119621586 162 NrpNPPDVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLAQGAEMKHIL 225
Cdd:COG0666  174 E--AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-149 4.05e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.94  E-value: 4.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   9 LLHHA-RNGNAEEVRQLLEtmaRNeviADINckgrSKSNLGWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHR 87
Cdd:COG0666  156 PLHLAaANGNLEIVKLLLE---AG---ADVN----ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119621586  88 AAFTGRKELVMLLLEYNADTTIVNGSGQTAKEVTHAEEIRSMLEAVERTQQRKLEELLLAAA 149
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-111 2.19e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   10 LHHA-RNGNAEEVRQLLEtmarneVIADINCKgrskSNLGWTPLHLACYFGHRQVVQdLLKAGAEVNVlNDMGDTPLHRA 88
Cdd:pfam12796   1 LHLAaKNGNLELVKLLLE------NGADANLQ----DKNGRTALHLAAKNGHLEIVK-LLLEHADVNL-KDNGRTALHYA 68

                          90       100
                  ....*....|....*....|...
gi 119621586   89 AFTGRKELVMLLLEYNADTTIVN 111
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-206 1.31e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   52 LHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLLEYnadttivngsgqtakevthaeeirsmle 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119621586  132 avertqqrkleelllaaaregktteltallnrpnpPDVNCSDQlGNTPLHCAAYRAHKQCALKLLRSGADPNLKN 206
Cdd:pfam12796  53 -----------------------------------ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-216 3.62e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.83  E-value: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   8 QLLHHARNGNAEEVRQLLETMArneviaDINCKGRSksnlGWTPLHLACYFGHR-QVVQDLLKAGAEVNVLNDMGDTPLH 86
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGA------DVNAPERC----GFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLH 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  87 R--AAFTGRKELVMLLLEYNADTTIVNGSGQTA-------KEVThAEEIRSMLEAVERTQQRK------LEELLLAA-AR 150
Cdd:PHA03095 123 VylSGFNINPKVIRLLLRKGADVNALDLYGMTPlavllksRNAN-VELLRLLIDAGADVYAVDdrfrslLHHHLQSFkPR 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 151 EGKTTELTALLNRPNPPDVncsdqLGNTPLHCAAyrAHKQCA----LKLLRSGADPNLKNKNDQKPLDLA 216
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDM-----LGNTPLHSMA--TGSSCKrslvLPLLIAGISINARNRYGQTPLHYA 264
PHA03095 PHA03095
ankyrin-like protein; Provisional
 14-216 3.58e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.67  E-value: 3.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  14 RNGNAEEVRQLLETMArneviADINckgrSKSNLGWTPLH--LACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHraAFT 91
Cdd:PHA03095  92 YNATTLDVIKLLIKAG-----ADVN----AKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  92 GRK----ELVMLLLEYNADTTIVNGSGQTAKEVtHAEEIRsmleaverTQQRKLEELLL-----AAAREGKTTELTALLN 162
Cdd:PHA03095 161 KSRnanvELLRLLIDAGADVYAVDDRFRSLLHH-HLQSFK--------PRARIVRELIRagcdpAATDMLGNTPLHSMAT 231

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119621586 163 RPNPP------------DVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLA 216
Cdd:PHA03095 232 GSSCKrslvlplliagiSINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 32-238 5.93e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 5.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  32 EVIADINCKGRSKSNLGWTPLHLACYFGH-----RQVVQDLLKAGAEVNVLNDMGDTPLHRAAFT--GRKELVMLLLEYN 104
Cdd:PHA03100  52 KILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 105 ADTTIVNGSGQTakevthaeeirsMLEAVERTQQRKLE--ELLLA-AAREGKTTELTALLNrpNPPDVNCSDQLGNTPLH 181
Cdd:PHA03100 132 ANVNIKNSDGEN------------LLHLYLESNKIDLKilKLLIDkGVDINAKNRVNYLLS--YGVPINIKDVYGFTPLH 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119621586 182 CAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLAqgaemkhILVGNKVIYKALKRY 238
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA-------ILNNNKEIFKLLLNN 247
Ank_4 pfam13637
Ankyrin repeats (many copies);
48-101 4.10e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 4.10e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119621586   48 GWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLL 101
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 8-103 4.63e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 4.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   8 QLLHHARNGNAEEVRQLLETMArneviaDINCKGRSksnlGWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHR 87
Cdd:PTZ00322  85 ELCQLAASGDAVGARILLTGGA------DPNCRDYD----GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154

                         90
                 ....*....|....*.
gi 119621586  88 AAFTGRKELVMLLLEY 103
Cdd:PTZ00322 155 AEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-215 5.43e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 5.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  63 VVQDLLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSGQTAKEVT----HAEEIRSMLEavERTQQ 138
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAvdskNIDTIKAIID--NRSNI 237

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119621586 139 RKLEELLLAAARegkTTEL-TALLNRPNPPDVNCSDQLGNTPLHCAAYR-AHKQCALKLLRSGADPNLKNKNDQKPLDL 215
Cdd:PHA02876 238 NKNDLSLLKAIR---NEDLeTSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYL 313
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 35-111 6.37e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.38  E-value: 6.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  35 ADINCKGR------------SKSNLGWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLLE 102
Cdd:PHA03100 167 VDINAKNRvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                 ....*....
gi 119621586 103 YNADTTIVN 111
Cdd:PHA03100 247 NGPSIKTII 255
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-240 2.49e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  35 ADINCKGRSKSNlgwTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSG 114
Cdd:PHA02878 158 ADINMKDRHKGN---TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 115 QTAKEVthaeeirsmleAVERTQQRKLEELLLAAAregktteltallnrpnpPDVNC-SDQLGNTPLHCAayrAHKQCAL 193
Cdd:PHA02878 235 NTPLHI-----------SVGYCKDYDILKLLLEHG-----------------VDVNAkSYILGLTALHSS---IKSERKL 283

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119621586 194 K-LLRSGADPNLKNKNDQKPLDLA----QGAEMKHILVGN----KVIYKALKRYEG 240
Cdd:PHA02878 284 KlLLEYGADINSLNSYKLTPLSSAvkqyLCINIGRILISNicllKRIKPDIKNSEG 339
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-117 4.05e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  10 LHHA-RNGNAEEVRQLLETMArneviaDINckgrSKSNLGWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRA 88
Cdd:COG0666  190 LHLAaENGHLEIVKLLLEAGA------DVN----AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259

                         90       100
                 ....*....|....*....|....*....
gi 119621586  89 AFTGRKELVMLLLEYNADTTIVNGSGQTA 117
Cdd:COG0666  260 AAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 50-213 1.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.44  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  50 TPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLLEYNADTTIVngsgqtAKEVTHAEEIRSM 129
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL------PIPCIEKDMIKTI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 130 LEAVER--TQQRKLEELLLAAAREGKTTELTALLNRpnPPDVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNK 207
Cdd:PHA02874 111 LDCGIDvnIKDAELKTFLHYAIKKGDLESIKMLFEY--GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188


                 ....*.
gi 119621586 208 NDQKPL 213
Cdd:PHA02874 189 NGESPL 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 7-224 3.17e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 3.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   7 QQLLHHA-RNGNAEEVRQLLETMArNEVIADINckgrsksnlGWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPL 85
Cdd:PHA02874 125 KTFLHYAiKKGDLESIKMLFEYGA-DVNIEDDN---------GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  86 HRAAFTGRKELVMLLLEYNADTTIVNGSGQTAkevTHAEEIRSmleavertqqRKLEELLLaaaregktteltallnrpN 165
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP---LHNAIIHN----------RSAIELLI------------------N 243

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 166 PPDVNCSDQLGNTPLHCA-AYRAHKQCALKLLRSGADPNLKNKNDQKPLDLAqgaeMKHI 224
Cdd:PHA02874 244 NASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA----FKYI 299
PH_FAPP1_FAPP2 cd01247
Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain; Human FAPP1 (also ...
 239-329 5.80e-08

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: 51.25  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 239 EGPLWKSSRFF-GWRLFWVVLEHGVLSWYRKQpDAVHniyrQGCK-HLTQAVC--TVKSTDSCLffikcFDDTIHG---F 311
Cdd:cd01247    2 EGVLWKWTNYLsGWQPRWFVLDDGVLSYYKSQ-EEVN----QGCKgSVKMSVCeiIVHPTDPTR-----MDLIIPGeqhF 71

                         90
                 ....*....|....*...
gi 119621586 312 RVpKNSLQQSREDWLEAI 329
Cdd:cd01247   72 YL-KASSAAERQRWLVAL 88
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 59-223 9.33e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 9.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  59 GHRQVVQDLLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSGQTAK----EVTHAEEIRSMLEAVE 134
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaiSAKHHKIFRILYHFAS 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 135 RTQQRKLEELLLAAAREGKTTELTALLNRpnPPDVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQ---- 210
Cdd:PLN03192 616 ISDPHAAGDLLCTAAKRNDLTAMKELLKQ--GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDfspt 693

                        170
                 ....*....|...
gi 119621586 211 KPLDLAQGAEMKH 223
Cdd:PLN03192 694 ELRELLQKRELGH 706
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 2-218 1.07e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   2 NTEAEQQLLHHARNG-NAEEVRQLLETMArneviaDINCKGRsksnLGWTPLHLACYFG-HRQVVQDLLKAGAEVNVLND 79
Cdd:PHA02876 304 NIKGETPLYLMAKNGyDTENIRTLIMLGA------DVNAADR----LYITPLHQASTLDrNKDIVITLLELGANVNARDY 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  80 MGDTPLHRAAFTGRKELVMLLLEYNADttivngsgqtakevthaeeirsmleaVERTQQRKLEELLLAAAREGKTTELTA 159
Cdd:PHA02876 374 CDKTPIHYAAVRNNVVIINTLLDYGAD--------------------------IEALSQKIGTALHFALCGTNPYMSVKT 427

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119621586 160 LLNRpnPPDVNCSDQLGNTPLHcaaYRAHKQCALK----LLRSGADPNLKNKNDQKPLDLAQG 218
Cdd:PHA02876 428 LIDR--GANVNSKNKDLSTPLH---YACKKNCKLDviemLLDNGADVNAINIQNQYPLLIALE 485
Ank_5 pfam13857
Ankyrin repeats (many copies);
160-216 1.08e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 1.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119621586  160 LLNRpNPPDVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLA 216
Cdd:pfam13857   1 LLEH-GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PH_ORP9 cd13290
Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 ...
 239-332 1.97e-07

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: 50.14  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 239 EGPLWKSSRFF-GWRLFWVVLEH--GVLSWYRKQpDAVHNIYRQGCKHLTQAVCTVKSTDSCLFFIKCFDDTIHgFRVpK 315
Cdd:cd13290    2 EGPLSKWTNVMkGWQYRWFVLDDnaGLLSYYTSK-EKMMRGSRRGCVRLKGAVVGIDDEDDSTFTITVDQKTFH-FQA-R 78

                         90
                 ....*....|....*..
gi 119621586 316 NSLQqsREDWLEAIEEH 332
Cdd:cd13290   79 DAEE--RERWIRALEDT 93
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-79 7.00e-07

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: 46.13  E-value: 7.00e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 119621586   48 GWTPLHLACY-FGHRQVVQDLLKAGAEVNVLND 79
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
143-196 2.29e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119621586  143 ELLLAAAREGKTTELTALLNrpNPPDVNCSDQLGNTPLHCAAYRAHKQCALKLL 196
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-207 2.38e-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: 44.97  E-value: 2.38e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 119621586  176 GNTPLHCAAYRA-HKQCALKLLRSGADPNLKNK 207
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
48-88 2.63e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 2.63e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 119621586   48 GWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRA 88
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 168-216 4.52e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 4.52e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 119621586 168 DVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLA 216
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-142 4.88e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 4.88e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119621586  67 LLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSGQTAKEVTHAEEIRSMLEAVERTQQRKLE 142
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-76 1.29e-05

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: 42.57  E-value: 1.29e-05
                           10        20
                   ....*....|....*....|....*....
gi 119621586    48 GWTPLHLACYFGHRQVVQDLLKAGAEVNV 76
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PH_GPBP cd13283
Goodpasture antigen binding protein Pleckstrin homology (PH) domain; The GPBP (also called ...
 250-336 3.44e-05

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: 43.43  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 250 GWRLFWVVLEHGVLSWYRKQPDAVHniyrqGCK---HLTQAVCTVKSTDSCLFFIkCFDDTIHGFRVpknSLQQSREDWL 326
Cdd:cd13283   14 GWQDRYFVLKDGTLSYYKSESEKEY-----GCRgsiSLSKAVIKPHEFDECRFDV-SVNDSVWYLRA---ESPEERQRWI 84

                         90
                 ....*....|
gi 119621586 327 EAIEEHSAYS 336
Cdd:cd13283   85 DALESHKAAS 94
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-76 3.90e-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: 41.47  E-value: 3.90e-05
                          10        20
                  ....*....|....*....|....*....
gi 119621586   48 GWTPLHLACYFGHRQVVQDLLKAGAEVNV 76
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 238-334 4.44e-05

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: 43.31  E-value: 4.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   238 YEGPLWK--SSRFFGWRLFWVVLEHGVLSWYRKQPDAVHNIYR-----QGCKhLTQAVCTVKSTDSCLFFIKCFDDTIHG 310
Cdd:smart00233   3 KEGWLYKksGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKgsidlSGCT-VREAPDPDSSKKPHCFEIKTSDRKTLL 81

                           90       100
                   ....*....|....*....|....
gi 119621586   311 FRVPKnslQQSREDWLEAIEEHSA 334
Cdd:smart00233  82 LQAES---EEEREKWVEALRKAIA 102
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 238-329 5.09e-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: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 238 YEGPLWK--SSRFFGWRLFWVVLEHGVLSWYRKQPDAVHNIYRQ-GCKHLTQAVCTVKSTDSCLFFIKCFDDTIHGFRVP 314
Cdd:cd00821    1 KEGYLLKrgGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSiPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQAD 80

                         90
                 ....*....|....*
gi 119621586 315 KnslQQSREDWLEAI 329
Cdd:cd00821   81 S---EEERQEWLKAL 92
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 10-116 8.67e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 8.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  10 LHHA-RNGNAEEVRQLLETmarNEVIADINCKGrsksnlGWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRA 88
Cdd:PHA02875  72 LHDAvEEGDVKAVEELLDL---GKFADDVFYKD------GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142

                         90       100
                 ....*....|....*....|....*...
gi 119621586  89 AFTGRKELVMLLLEYNADTTIVNGSGQT 116
Cdd:PHA02875 143 VMMGDIKGIELLIDHKACLDIEDCCGCT 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 9-238 9.14e-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: 46.16  E-value: 9.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586   9 LLHHARNGNAEEVRQLLETMArneviADINCKGrsksNLGWTPLHLACYFGHRQVVQDLLKAGAE-VN--VLNDM--GDT 83
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPS-----CDLFQRG----ALGETALHVAALYDNLEAAVVLMEAAPElVNepMTSDLyqGET 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  84 PLHRAAFTGRKELVMLLLEYNADTTIVNGSGqtakevthaeeirsmleAVERTQQRKL----EELLLAAAREGKTTELTA 159
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGADVVSPRATG-----------------TFFRPGPKNLiyygEHPLSFAACVGNEEIVRL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 160 LLNRPNppDVNCSDQLGNTPLHCAAYRAHKQCAL----------KLLRSGADPNLKNKNDQKPLDLAqGAEmkhilvGNK 229
Cdd:cd22192  155 LIEHGA--DIRAQDSLGNTVLHILVLQPNKTFACqmydlilsydKEDDLQPLDLVPNNQGLTPFKLA-AKE------GNI 225

                        250
                 ....*....|.
gi 119621586 230 VIYKAL--KRY 238
Cdd:cd22192  226 VMFQHLvqKRR 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-117 1.34e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119621586   67 LLKAG-AEVNVLNDMGDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSGQTA 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 1.37e-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: 39.88  E-value: 1.37e-04
                           10        20
                   ....*....|....*....|....*....
gi 119621586   176 GNTPLHCAAYRAHKQCALKLLRSGADPNL 204
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-111 4.38e-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: 38.42  E-value: 4.38e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119621586   81 GDTPLHRAA-FTGRKELVMLLLEYNADTTIVN 111
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PH_Osh1p_Osh2p_yeast cd13292
Yeast oxysterol binding protein homologs 1 and 2 Pleckstrin homology (PH) domain; Yeast Osh1p ...
 250-272 5.18e-04

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: 40.37  E-value: 5.18e-04
                         10        20
                 ....*....|....*....|...
gi 119621586 250 GWRLFWVVLEHGVLSWYRKQPDA 272
Cdd:cd13292   17 GYKTRWFVLEDGVLSYYRHQDDE 39
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 55-216 5.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 5.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  55 ACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLLEYNADTTiVNGSGqtakevthaeeIRSML-EAV 133
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPD-VKYPD-----------IESELhDAV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 134 ERTQQRKLEELLLAaareGKTTEltallnrpnppDVNCSDqlGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPL 213
Cdd:PHA02875  77 EEGDVKAVEELLDL----GKFAD-----------DVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139


                 ...
gi 119621586 214 DLA 216
Cdd:PHA02875 140 HLA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
176-216 8.74e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 8.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 119621586  176 GNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLA 216
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-117 1.19e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 119621586   81 GDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSGQTA 117
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 80-109 1.49e-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: 1.49e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 119621586    80 MGDTPLHRAAFTGRKELVMLLLEYNADTTI 109
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PH_ORP_plant cd13294
Plant Oxysterol binding protein related protein Pleckstrin homology (PH) domain; Plant ORPs ...
 250-330 3.04e-03

Plant Oxysterol binding protein related protein Pleckstrin homology (PH) domain; Plant ORPs contain a N-terminal PH domain and a C-terminal OSBP-related domain. Not much is known about its specific function in plants to date. Members here include: Arabidopsis, spruce, and petunia. 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: 241448  Cd Length: 100  Bit Score: 37.86  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586 250 GWRLFWVVLEHGVLSWYR-KQPDAVHNIyrqGCKHLTQAVCTVKSTDSCLFFIKCFDDTIHgFRVPKNslqQSREDWLEA 328
Cdd:cd13294   14 GWRSRWFVLQDGVLSYYKvHGPDKVKPS---GEVHLKVSSIRESRSDDKKFYIFTGTKTLH-LRAESR---EDRAAWLEA 86


                 ..
gi 119621586 329 IE 330
Cdd:cd13294   87 LQ 88
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 15-109 4.97e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.51  E-value: 4.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119621586  15 NGNAEEVRQLLETMARNEVIAD--INCKGRSKSNLGWTPLHLACYFGHRQVVQDLLKAGAEVNVL-----------ND-- 79
Cdd:cd22194  106 NENTKEIVRILLAFAEENGILDrfINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkykHEgf 185

                         90       100       110
                 ....*....|....*....|....*....|.
gi 119621586  80 -MGDTPLHRAAFTGRKELVMLLLEyNADTTI 109
Cdd:cd22194  186 yFGETPLALAACTNQPEIVQLLME-KESTDI 215
 
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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