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Conserved domains on  [gi|569004288|ref|XP_006526204|]
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oxysterol-binding protein-related protein 1 isoform X1 [Mus musculus]

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;
548-943 0e+00

Oxysterol-binding protein;


:

Pssm-ID: 460126  Cd Length: 366  Bit Score: 560.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  548 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKPFNP 627
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPFNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  628 LLGETYELVRDDLGFRLISEQVSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLDHNEAYTWTN 707
Cdd:pfam01237  81 LLGETFELVRPDKGFRFIAEQVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  708 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 786
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  787 fdaykkndkknteeKKNSKQTSSSEESDEMPVPDSEsvfiipgSVLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkEMESV 866
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGE-------SRLLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004288  867 IPKTDCRLRPDIRAMENGEIDLASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYSGAQDWIYSGSYWDRNY 943
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
 229-352 8.03e-76

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: 243.84  E-value: 8.03e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 229 KVVHKALKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTV 308
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 569004288 309 HCFRVP-KNSVQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEED 352
Cdd:cd13285   81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 1.43e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   1 MNTEAEQQLLHHA-RNGNAEEVRKLLAAMArmevvaDIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLND 79
Cdd:COG0666   82 AKDDGGNTLLHAAaRNGDLEIVKLLLEAGA------DVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  80 MGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAkeathdkeirnmleavertqqrkleelLLGAAREGRTAEVSA 159
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004288 160 LLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHILV 226
Cdd:COG0666  205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
 
Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
548-943 0e+00

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 560.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  548 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKPFNP 627
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPFNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  628 LLGETYELVRDDLGFRLISEQVSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLDHNEAYTWTN 707
Cdd:pfam01237  81 LLGETFELVRPDKGFRFIAEQVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  708 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 786
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  787 fdaykkndkknteeKKNSKQTSSSEESDEMPVPDSEsvfiipgSVLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkEMESV 866
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGE-------SRLLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004288  867 IPKTDCRLRPDIRAMENGEIDLASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYSGAQDWIYSGSYWDRNY 943
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
 229-352 8.03e-76

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: 243.84  E-value: 8.03e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 229 KVVHKALKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTV 308
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 569004288 309 HCFRVP-KNSVQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEED 352
Cdd:cd13285   81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 1.43e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   1 MNTEAEQQLLHHA-RNGNAEEVRKLLAAMArmevvaDIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLND 79
Cdd:COG0666   82 AKDDGGNTLLHAAaRNGDLEIVKLLLEAGA------DVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  80 MGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAkeathdkeirnmleavertqqrkleelLLGAAREGRTAEVSA 159
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004288 160 LLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHILV 226
Cdd:COG0666  205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-111 8.65e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 8.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   10 LHHA-RNGNAEEVRKLLaamarmEVVADIDCKgrskSNLGWTPLHLACYFGHKQVVEdLLKAGAKVNMlNDMGDTPLHRA 88
Cdd:pfam12796   1 LHLAaKNGNLELVKLLL------ENGADANLQ----DKNGRTALHLAAKNGHLEIVK-LLLEHADVNL-KDNGRTALHYA 68

                          90       100
                  ....*....|....*....|...
gi 569004288   89 AFTGRKELVLLLLEYDADSTVVN 111
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 14-216 3.28e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.05  E-value: 3.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  14 RNGNAEEVRKLLAAMArmevvADIdckgRSKSNLGWTPLH--LACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHraAFT 91
Cdd:PHA03095  92 YNATTLDVIKLLIKAG-----ADV----NAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  92 GRK----ELVLLLLEYDADSTVVNGSGQTAKEathdkeirNMLEAVeRTQQRKLEELL------LGAAREGRTAEVS-AL 160
Cdd:PHA03095 161 KSRnanvELLRLLIDAGADVYAVDDRFRSLLH--------HHLQSF-KPRARIVRELIragcdpAATDMLGNTPLHSmAT 231

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004288 161 LSRPNPP----------DVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:PHA03095 232 GSSCKRSlvlplliagiSINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 238-334 1.04e-07

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: 51.01  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   238 YEGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYR-----QGCKhLTQAVCTVKPTDSCLFSIRCFDDTVHC 310
Cdd:smart00233   3 KEGWLYKksGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKgsidlSGCT-VREAPDPDSSKKPHCFEIKTSDRKTLL 81

                           90       100
                   ....*....|....*....|....
gi 569004288   311 FRVPKnsvQQSREKWLEAIEEHSA 334
Cdd:smart00233  82 LQAES---EEEREKWVEALRKAIA 102
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-76 6.02e-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: 43.73  E-value: 6.02e-06
                           10        20
                   ....*....|....*....|....*....
gi 569004288    48 GWTPLHLACYFGHKQVVEDLLKAGAKVNM 76
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 9-181 2.66e-04

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: 44.62  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   9 LLHHARNGNAEEVRKLLaamarmeVVADIDCKGRSKsnLGWTPLHLACYFGHKQVVEDLLKAGAK-VN--MLNDM--GDT 83
Cdd:cd22192   21 LLLAAKENDVQAIKKLL-------KCPSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPElVNepMTSDLyqGET 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  84 PLHRAAFTGRKELVLLLLEYDADstVVNgsgqtaKEATHdkeirnmleAVERTQQRKL----EELLLGAAREGRTAEVSA 159
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGAD--VVS------PRATG---------TFFRPGPKNLiyygEHPLSFAACVGNEEIVRL 154

                        170       180
                 ....*....|....*....|..
gi 569004288 160 LLSRPNppDVNCSDQLGNTPLH 181
Cdd:cd22192  155 LIEHGA--DIRAQDSLGNTVLH 174
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 238-334 4.75e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  238 YEGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYR-----QGCKhLTQAVCTVKPTDSCLFSIRCFDDT-VH 309
Cdd:pfam00169   3 KEGWLLKkgGGKKKSWKKRYFVLFDGSLLYYKDDKSGKSKEPKgsislSGCE-VVEVVASDSPKRKFCFELRTGERTgKR 81

                          90       100
                  ....*....|....*....|....*
gi 569004288  310 CFRVpKNSVQQSREKWLEAIEEHSA 334
Cdd:pfam00169  82 TYLL-QAESEEERKDWIKAIQSAIR 105
 
Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
548-943 0e+00

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 560.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  548 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKPFNP 627
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPFNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  628 LLGETYELVRDDLGFRLISEQVSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLDHNEAYTWTN 707
Cdd:pfam01237  81 LLGETFELVRPDKGFRFIAEQVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  708 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 786
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  787 fdaykkndkknteeKKNSKQTSSSEESDEMPVPDSEsvfiipgSVLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkEMESV 866
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGE-------SRLLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004288  867 IPKTDCRLRPDIRAMENGEIDLASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYSGAQDWIYSGSYWDRNY 943
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
 229-352 8.03e-76

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: 243.84  E-value: 8.03e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 229 KVVHKALKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTV 308
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 569004288 309 HCFRVP-KNSVQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEED 352
Cdd:cd13285   81 HRFKVPpKNNPVVTRKKWLEALEEHSAYSTHYCTQEQLSDDEDED 125
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 1.43e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   1 MNTEAEQQLLHHA-RNGNAEEVRKLLAAMArmevvaDIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLND 79
Cdd:COG0666   82 AKDDGGNTLLHAAaRNGDLEIVKLLLEAGA------DVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  80 MGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAkeathdkeirnmleavertqqrkleelLLGAAREGRTAEVSA 159
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004288 160 LLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHILV 226
Cdd:COG0666  205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-225 3.57e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 3.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   9 LLHHARNGNAEEVRKLLAAMARMEVVADIDCKGRSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRA 88
Cdd:COG0666   15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  89 AFTGRKELVLLLLEYDADSTVVNGSGQT----AKEATHDKEIRNMLEA---VERtQQRKLEELLLGAAREGRTAEVSALL 161
Cdd:COG0666   95 ARNGDLEIVKLLLEAGADVNARDKDGETplhlAAYNGNLEIVKLLLEAgadVNA-QDNDGNTPLHLAAANGNLEIVKLLL 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569004288 162 SrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHIL 225
Cdd:COG0666  174 E--AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-149 7.14e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 7.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   9 LLHHA-RNGNAEEVRKLLAAmarmevVADIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHR 87
Cdd:COG0666  156 PLHLAaANGNLEIVKLLLEA------GADVN----ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569004288  88 AAFTGRKELVLLLLEYDADSTVVNGSGQTAKEATHDKEIRNMLEAVERTQQRKLEELLLGAA 149
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-111 8.65e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 8.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   10 LHHA-RNGNAEEVRKLLaamarmEVVADIDCKgrskSNLGWTPLHLACYFGHKQVVEdLLKAGAKVNMlNDMGDTPLHRA 88
Cdd:pfam12796   1 LHLAaKNGNLELVKLLL------ENGADANLQ----DKNGRTALHLAAKNGHLEIVK-LLLEHADVNL-KDNGRTALHYA 68

                          90       100
                  ....*....|....*....|...
gi 569004288   89 AFTGRKELVLLLLEYDADSTVVN 111
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-206 7.24e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 7.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   52 LHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYdadstvvngsgqtakeathdkeirnmle 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004288  132 avertqqrkleelllgaaregrtaevsallsrpnpPDVNCSDQlGNTPLHCAAYRAHKQCVLKLLRSGADPSLKN 206
Cdd:pfam12796  53 -----------------------------------ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 14-216 3.28e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.05  E-value: 3.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  14 RNGNAEEVRKLLAAMArmevvADIdckgRSKSNLGWTPLH--LACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHraAFT 91
Cdd:PHA03095  92 YNATTLDVIKLLIKAG-----ADV----NAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  92 GRK----ELVLLLLEYDADSTVVNGSGQTAKEathdkeirNMLEAVeRTQQRKLEELL------LGAAREGRTAEVS-AL 160
Cdd:PHA03095 161 KSRnanvELLRLLIDAGADVYAVDDRFRSLLH--------HHLQSF-KPRARIVRELIragcdpAATDMLGNTPLHSmAT 231

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004288 161 LSRPNPP----------DVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:PHA03095 232 GSSCKRSlvlplliagiSINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank_4 pfam13637
Ankyrin repeats (many copies);
48-101 3.80e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.91  E-value: 3.80e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 569004288   48 GWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLL 101
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 10-216 9.48e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 9.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  10 LHHARNGNAEEVRKLLAamarmevvaDIDCKGRSKSNLGWTPLHLACYFGH-----KQVVEDLLKAGAKVNMLNDMGDTP 84
Cdd:PHA03100  39 LYLAKEARNIDVVKILL---------DNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  85 LHRAAFT--GRKELVLLLLEYDADSTVVNGSGQtakeathdkeirNMLEAVERTQQRKLE--ELLL--GAAREGRTaEVS 158
Cdd:PHA03100 110 LLYAISKksNSYSIVEYLLDNGANVNIKNSDGE------------NLLHLYLESNKIDLKilKLLIdkGVDINAKN-RVN 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 569004288 159 ALLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:PHA03100 177 YLLS--YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 18-228 1.38e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  18 AEEVRKLLAAmarmevVADIDCKGrsksNLGWTPLHLACYFGHKQ---VVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRK 94
Cdd:PHA03095  27 VEEVRRLLAA------GADVNFRG----EYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  95 ELVL-LLLEYDADSTVVNGSGQTA------KEATHDKEIRNMLEAvertqqrkleelllGA---ARE--GRTAeVSALLS 162
Cdd:PHA03095  97 LDVIkLLIKAGADVNAKDKVGRTPlhvylsGFNINPKVIRLLLRK--------------GAdvnALDlyGMTP-LAVLLK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 163 RPNPP------------DVNCSDQLGNTPLH--CAAYRAHKQCVLKLLRSGADPSLKNKNDQKPL-DLAQGAEMKHILVG 227
Cdd:PHA03095 162 SRNANvellrllidagaDVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSLVL 241


                 .
gi 569004288 228 N 228
Cdd:PHA03095 242 P 242
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-215 1.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  63 VVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAKEATHDKEIRNMLEAV--ERTQQRK 140
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIidNRSNINK 239

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004288 141 LEELLLGAAREgrTAEVSALLSRPNPPDVNCSDQLGNTPLHCAAYR-AHKQCVLKLLRSGADPSLKNKNDQKPLDL 215
Cdd:PHA02876 240 NDLSLLKAIRN--EDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYL 313
PH_FAPP1_FAPP2 cd01247
Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain; Human FAPP1 (also ...
 239-329 2.28e-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: 55.49  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 239 EGPLWKSSRFF-GWKLFWVVLEHGVLSWYRKQpDAVHnsyrQGCK-HLTQAVC--TVKPTDSCLFSIrcfddtvhcfRVP 314
Cdd:cd01247    2 EGVLWKWTNYLsGWQPRWFVLDDGVLSYYKSQ-EEVN----QGCKgSVKMSVCeiIVHPTDPTRMDL----------IIP 66

                         90       100
                 ....*....|....*....|..
gi 569004288 315 -------KNSVQQSREKWLEAI 329
Cdd:cd01247   67 geqhfylKASSAAERQRWLVAL 88
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 9-106 4.40e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.68  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   9 LLHHARNGNAEEVRKLLaamarMEVVADIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRA 88
Cdd:PHA03100 162 LIDKGVDINAKNRVNYL-----LSYGVPIN----IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232

                         90
                 ....*....|....*...
gi 569004288  89 AFTGRKELVLLLLEYDAD 106
Cdd:PHA03100 233 ILNNNKEIFKLLLNNGPS 250
PH_ORP9 cd13290
Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 ...
 239-332 4.71e-09

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: 54.76  E-value: 4.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 239 EGPLWKSSRFF-GWKLFWVVLEH--GVLSWYRKQpDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTVHcFRVpK 315
Cdd:cd13290    2 EGPLSKWTNVMkGWQYRWFVLDDnaGLLSYYTSK-EKMMRGSRRGCVRLKGAVVGIDDEDDSTFTITVDQKTFH-FQA-R 78

                         90
                 ....*....|....*..
gi 569004288 316 NSvqQSREKWLEAIEEH 332
Cdd:cd13290   79 DA--EERERWIRALEDT 93
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 8-103 5.66e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 5.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   8 QLLHHARNGNAEEVRKLLAAMArmevvaDIDCKGRSksnlGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHR 87
Cdd:PTZ00322  85 ELCQLAASGDAVGARILLTGGA------DPNCRDYD----GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154

                         90
                 ....*....|....*.
gi 569004288  88 AAFTGRKELVLLLLEY 103
Cdd:PTZ00322 155 AEENGFREVVQLLSRH 170
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 7-309 1.13e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.44  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   7 QQLLHHA-RNGNAEEVRKLLaamarmEVVADIDCKGRSksnlGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPL 85
Cdd:PHA02874 125 KTFLHYAiKKGDLESIKMLF------EYGADVNIEDDN----GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  86 HRAAFTGRKELVLLLLEYDADSTVVNGSGQTakeATHDKEIRNmleavertqqRKLEELLLgaaregrtaevsallsrpN 165
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFT---PLHNAIIHN----------RSAIELLI------------------N 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 166 PPDVNCSDQLGNTPLHCA-AYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHILVGNKVVHKALKRYEGPLwK 244
Cdd:PHA02874 244 NASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIKEADKL-K 322

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004288 245 SSRFFGWKlfwVVLEHGVLSWYRKQPD---AVHNSYRQGCKHLTQAVCTVKPT-------DSCLFSIRCFDDTVH 309
Cdd:PHA02874 323 DSDFLEHI---EIKDNKEFSDFIKECNeeiEDMKKTKCGCDKNIFDLCLIRIKhkfdgneDSIKDYLNCLDDNSH 394
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-235 1.23e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  10 LHHArnGNAEEVRKLLAAMarMEVVADIDckgrSKSNLGWTPLHLACYFGH-KQVVEDLLKAGAKVNMLNDMGDTPLHRA 88
Cdd:PHA02876 277 LHHA--SQAPSLSRLVPKL--LERGADVN----AKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQA 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  89 AFTGR-KELVLLLLEYDADstvVNGSGQTAKEATHDKEIRNML----------EAVERTQQRKLEELLLGAAREGRTAEV 157
Cdd:PHA02876 349 STLDRnKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVviintlldygADIEALSQKIGTALHFALCGTNPYMSV 425

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 158 SALLSRPnpPDVNCSDQLGNTPLHCAAYRAHKQCVLK-LLRSGADPSLKNKNDQKPLDLA------------QGAEMKHi 224
Cdd:PHA02876 426 KTLIDRG--ANVNSKNKDLSTPLHYACKKNCKLDVIEmLLDNGADVNAINIQNQYPLLIAleyhgivnillhYGAELRD- 502

                        250
                 ....*....|.
gi 569004288 225 lvgNKVVHKAL 235
Cdd:PHA02876 503 ---SRVLHKSL 510
PH_GPBP cd13283
Goodpasture antigen binding protein Pleckstrin homology (PH) domain; The GPBP (also called ...
 250-336 2.54e-08

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: 52.29  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 250 GWKLFWVVLEHGVLSWYRKQPDAVHnsyrqGCK---HLTQAVCTVKPTDSCLFSIrCFDDTVHCFRVpknSVQQSREKWL 326
Cdd:cd13283   14 GWQDRYFVLKDGTLSYYKSESEKEY-----GCRgsiSLSKAVIKPHEFDECRFDV-SVNDSVWYLRA---ESPEERQRWI 84

                         90
                 ....*....|
gi 569004288 327 EAIEEHSAYS 336
Cdd:cd13283   85 DALESHKAAS 94
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 50-213 9.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 9.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  50 TPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVV------NGSGQTAKEATHD 123
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILpipcieKDMIKTILDCGID 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 124 KEIRNmleavertqqRKLEELLLGAAREGRTAEVSALLSRpnPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPS 203
Cdd:PHA02874 117 VNIKD----------AELKTFLHYAIKKGDLESIKMLFEY--GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                        170
                 ....*....|
gi 569004288 204 LKNKNDQKPL 213
Cdd:PHA02874 185 VKDNNGESPL 194
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 238-334 1.04e-07

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: 51.01  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   238 YEGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYR-----QGCKhLTQAVCTVKPTDSCLFSIRCFDDTVHC 310
Cdd:smart00233   3 KEGWLYKksGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKgsidlSGCT-VREAPDPDSSKKPHCFEIKTSDRKTLL 81

                           90       100
                   ....*....|....*....|....
gi 569004288   311 FRVPKnsvQQSREKWLEAIEEHSA 334
Cdd:smart00233  82 LQAES---EEEREKWVEALRKAIA 102
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 569004288  166 PPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-137 5.76e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   9 LLH-HARN--GNAEEVRKLLAAmarmevvadiDCKGRSKSNLGWTPLHLACYFGHKQ--VVEDLLKAGAKVNMLNDMGDT 83
Cdd:PHA03095 190 LLHhHLQSfkPRARIVRELIRA----------GCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQT 259

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 569004288  84 PLHRAAFTGRKELVLLLLEYDADSTVVNGSGQT-AKEATHDKEIRnMLEAVERTQ 137
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTpLSLMVRNNNGR-AVRAALAKN 313
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 59-240 6.78e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  59 GHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAK----EATHDKEIRNMLEAVE 134
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaiSAKHHKIFRILYHFAS 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 135 RTQQRKLEELLLGAAREGRTAEVSALLSRpnPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQ---- 210
Cdd:PLN03192 616 ISDPHAAGDLLCTAAKRNDLTAMKELLKQ--GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDfspt 693

                        170       180       190
                 ....*....|....*....|....*....|...
gi 569004288 211 KPLDLAQGAEMKH---ILVGNKVVHKALKRYEG 240
Cdd:PLN03192 694 ELRELLQKRELGHsitIVDSVPADEPDLGRDGG 726
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 149-216 8.02e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 8.02e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004288 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 9.82e-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: 45.74  E-value: 9.82e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 569004288   48 GWTPLHLACY-FGHKQVVEDLLKAGAKVNMLND 79
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-224 1.52e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  145 LLGAAREGRTAEVSALLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVlKLLRSGADPSLKNkNDQKPLDLAqgAEMKHI 224
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKD-NGRTALHYA--ARSGHL 74
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 238-329 1.72e-06

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: 47.15  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 238 YEGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQ-GCKHLTQAVCTVKPTDSCLFSIRCFDDTVHCFRVP 314
Cdd:cd00821    1 KEGYLLKrgGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSiPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQAD 80

                         90
                 ....*....|....*
gi 569004288 315 KnsvQQSREKWLEAI 329
Cdd:cd00821   81 S---EEERQEWLKAL 92
Ank_4 pfam13637
Ankyrin repeats (many copies);
148-196 1.95e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.95e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 569004288  148 AAREGRTAEVSALLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLL 196
Cdd:pfam13637   8 AAASGHLELLRLLLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-130 2.86e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 2.86e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569004288  61 KQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAKE---ATHDKEIRNML 130
Cdd:PHA03100 172 KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHiaiLNNNKEIFKLL 244
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-240 3.10e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  35 ADIDCKGRSKSNlgwTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSG 114
Cdd:PHA02878 158 ADINMKDRHKGN---TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 115 QTAkeathdkeirnMLEAVERTQQRKLEELLLgaareGRTAEVSALlsrpnppdvncSDQLGNTPLHCAayrAHKQCVLK 194
Cdd:PHA02878 235 NTP-----------LHISVGYCKDYDILKLLL-----EHGVDVNAK-----------SYILGLTALHSS---IKSERKLK 284

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 569004288 195 -LLRSGADPSLKNKNDQKPLDLA----QGAEMKHILVGN----KVVHKALKRYEG 240
Cdd:PHA02878 285 lLLEYGADINSLNSYKLTPLSSAvkqyLCINIGRILISNicllKRIKPDIKNSEG 339
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-207 5.97e-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: 5.97e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 569004288  176 GNTPLHCAAYRA-HKQCVLKLLRSGADPSLKNK 207
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-76 6.02e-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: 43.73  E-value: 6.02e-06
                           10        20
                   ....*....|....*....|....*....
gi 569004288    48 GWTPLHLACYFGHKQVVEDLLKAGAKVNM 76
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PH_Osh1p_Osh2p_yeast cd13292
Yeast oxysterol binding protein homologs 1 and 2 Pleckstrin homology (PH) domain; Yeast Osh1p ...
 250-335 8.68e-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: 45.38  E-value: 8.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 250 GWKLFWVVLEHGVLSWYRKQPDavHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTVHCFRVPKNS-VQQSRekWLEA 328
Cdd:cd13292   17 GYKTRWFVLEDGVLSYYRHQDD--EGSACRGSINMKNARLVSDPSEKLRFEVSSKTSGSPKWYLKANHpVEAAR--WIQA 92


                 ....*..
gi 569004288 329 IEEHSAY 335
Cdd:cd13292   93 LQKAIEW 99
Ank_5 pfam13857
Ankyrin repeats (many copies);
48-88 2.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 569004288   48 GWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRA 88
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-168 4.08e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  67 LLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAkeathdkeirnmLEAVERTQQRKLEELLL 146
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP------------LELAEENGFREVVQLLS 168

                         90       100
                 ....*....|....*....|..
gi 569004288 147 GAAREGRTAEVSAllsrpnPPD 168
Cdd:PTZ00322 169 RHSQCHFELGANA------KPD 184
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-76 5.11e-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: 41.09  E-value: 5.11e-05
                          10        20
                  ....*....|....*....|....*....
gi 569004288   48 GWTPLHLACYFGHKQVVEDLLKAGAKVNM 76
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-117 1.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569004288   67 LLKAG-AKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTA 117
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 9-181 2.66e-04

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: 44.62  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288   9 LLHHARNGNAEEVRKLLaamarmeVVADIDCKGRSKsnLGWTPLHLACYFGHKQVVEDLLKAGAK-VN--MLNDM--GDT 83
Cdd:cd22192   21 LLLAAKENDVQAIKKLL-------KCPSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPElVNepMTSDLyqGET 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  84 PLHRAAFTGRKELVLLLLEYDADstVVNgsgqtaKEATHdkeirnmleAVERTQQRKL----EELLLGAAREGRTAEVSA 159
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGAD--VVS------PRATG---------TFFRPGPKNLiyygEHPLSFAACVGNEEIVRL 154

                        170       180
                 ....*....|....*....|..
gi 569004288 160 LLSRPNppDVNCSDQLGNTPLH 181
Cdd:cd22192  155 LIEHGA--DIRAQDSLGNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 176-204 3.02e-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: 3.02e-04
                           10        20
                   ....*....|....*....|....*....
gi 569004288   176 GNTPLHCAAYRAHKQCVLKLLRSGADPSL 204
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PH_ACAP cd13250
ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP ...
 239-330 1.05e-03

ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. 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: 270070  Cd Length: 98  Bit Score: 39.12  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 239 EGPLWK-SSRFFG-WKLFWVVLEHGVLSWYRKQpdavhNSYRQGCKHLTQAVCTVKPTDSClfsircfdDTVHCFRV--P 314
Cdd:cd13250    2 EGYLFKrSSNAFKtWKRRWFSLQNGQLYYQKRD-----KKDEPTVMVEDLRLCTVKPTEDS--------DRRFCFEVisP 68

                         90       100
                 ....*....|....*....|..
gi 569004288 315 KNSV------QQSREKWLEAIE 330
Cdd:cd13250   69 TKSYmlqaesEEDRQAWIQAIQ 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
176-216 1.50e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 569004288  176 GNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 80-106 1.88e-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: 36.41  E-value: 1.88e-03
                           10        20
                   ....*....|....*....|....*..
gi 569004288    80 MGDTPLHRAAFTGRKELVLLLLEYDAD 106
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-117 2.20e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 2.20e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 569004288   81 GDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTA 117
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
PHA02946 PHA02946
ankyin-like protein; Provisional
 127-220 3.65e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 127 RNMLEAVERTQQRKLEELLLG-AAREGRTAEvsALLSRPNPPdvNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLK 205
Cdd:PHA02946  26 RNMLQAIEPSGNYHILHAYCGiKGLDERFVE--ELLHRGYSP--NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNAC 101

                         90
                 ....*....|....*
gi 569004288 206 NKNDQKPLDLAQGAE 220
Cdd:PHA02946 102 DKQHKTPLYYLSGTD 116
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-106 4.55e-03

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: 35.31  E-value: 4.55e-03
                          10        20
                  ....*....|....*....|....*.
gi 569004288   81 GDTPLHRAAFTGRKELVLLLLEYDAD 106
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 238-334 4.75e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  238 YEGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYR-----QGCKhLTQAVCTVKPTDSCLFSIRCFDDT-VH 309
Cdd:pfam00169   3 KEGWLLKkgGGKKKSWKKRYFVLFDGSLLYYKDDKSGKSKEPKgsislSGCE-VVEVVASDSPKRKFCFELRTGERTgKR 81

                          90       100
                  ....*....|....*....|....*
gi 569004288  310 CFRVpKNSVQQSREKWLEAIEEHSA 334
Cdd:pfam00169  82 TYLL-QAESEEERKDWIKAIQSAIR 105
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-206 5.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 5.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  62 QVVEDLLKAGAKVNMLN-DMGDTPLHRAAFTGRKELVLLLLEYDADstvVNGSGQTAKEATHdkeirnmlEAVERTQQRK 140
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGAN---VNIPDKTNNSPLH--------HAVKHYNKPI 216

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004288 141 LEELLlgaaregrtaevsallsrPNPPDVNCSDQLGNTPLHCAAYRAHKQCVLK-LLRSGADPSLKN 206
Cdd:PHA02878 217 VHILL------------------ENGASTDARDKCGNTPLHISVGYCKDYDILKlLLEHGVDVNAKS 265
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 55-216 5.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 5.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  55 ACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVvngsgqtakeatHDKEIRNML-EAV 133
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV------------KYPDIESELhDAV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288 134 ERTQQRKLEELLLgaarEGRTAEvsallsrpnppDVNCSDqlGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPL 213
Cdd:PHA02875  77 EEGDVKAVEELLD----LGKFAD-----------DVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139


                 ...
gi 569004288 214 DLA 216
Cdd:PHA02875 140 HLA 142
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-111 7.06e-03

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: 34.96  E-value: 7.06e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 569004288   81 GDTPLHRAA-FTGRKELVLLLLEYDADSTVVN 111
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-163 8.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 8.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004288  48 GWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTA---KEATHDK 124
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPliiAMAKGDI 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 569004288 125 EIRNML----EAVERTQQRKLEELLLGAAREGRTAEVSALLSR 163
Cdd:PHA02875 182 AICKMLldsgANIDYFGKNGCVAALCYAIENNKIDIVRLFIKR 224
 
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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