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Conserved domains on  [gi|569004292|ref|XP_006526206|]
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oxysterol-binding protein-related protein 1 isoform X2 [Mus musculus]

Protein Classification

OSBP family protein( domain architecture ID 12789656)

OSBP (oxysterol-binding protein) family protein may be involved in the transport, synthesis, and/or regulation of sterols; also contains ankyrin repeat (ANK) domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
507-902 0e+00

Oxysterol-binding protein;


:

Pssm-ID: 460126  Cd Length: 366  Bit Score: 561.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  507 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKPFNP 586
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPFNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  587 LLGETYELVRDDLGFRLISEQVSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLDHNEAYTWTN 666
Cdd:pfam01237  81 LLGETFELVRPDKGFRFIAEQVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  667 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 745
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  746 fdaykkndkknteeKKNSKQTSSSEESDEMPVPDSEsvfiipgSVLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkEMESV 825
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGE-------SRLLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004292  826 IPKTDCRLRPDIRAMENGEIDLASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYSGAQDWIYSGSYWDRNY 902
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
229-324 3.80e-54

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13285:

Pssm-ID: 473070  Cd Length: 125  Bit Score: 183.75  E-value: 3.80e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 229 KVVHKALKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTV 308
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80
                         90
                 ....*....|....*..
gi 569004292 309 HCFRVP-KNSVQQSRER 324
Cdd:cd13285   81 HRFKVPpKNNPVVTRKK 97
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 1.35e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   1 MNTEAEQQLLHHA-RNGNAEEVRKLLAAMArmevvaDIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLND 79
Cdd:COG0666   82 AKDDGGNTLLHAAaRNGDLEIVKLLLEAGA------DVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  80 MGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAkeathdkeirnmleavertqqrkleelLLGAAREGRTAEVSA 159
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004292 160 LLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHILV 226
Cdd:COG0666  205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
 
Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
507-902 0e+00

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 561.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  507 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKPFNP 586
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPFNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  587 LLGETYELVRDDLGFRLISEQVSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLDHNEAYTWTN 666
Cdd:pfam01237  81 LLGETFELVRPDKGFRFIAEQVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  667 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 745
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  746 fdaykkndkknteeKKNSKQTSSSEESDEMPVPDSEsvfiipgSVLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkEMESV 825
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGE-------SRLLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004292  826 IPKTDCRLRPDIRAMENGEIDLASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYSGAQDWIYSGSYWDRNY 902
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
229-324 3.80e-54

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: 183.75  E-value: 3.80e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 229 KVVHKALKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTV 308
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80
                         90
                 ....*....|....*..
gi 569004292 309 HCFRVP-KNSVQQSRER 324
Cdd:cd13285   81 HRFKVPpKNNPVVTRKK 97
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 1.35e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   1 MNTEAEQQLLHHA-RNGNAEEVRKLLAAMArmevvaDIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLND 79
Cdd:COG0666   82 AKDDGGNTLLHAAaRNGDLEIVKLLLEAGA------DVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  80 MGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAkeathdkeirnmleavertqqrkleelLLGAAREGRTAEVSA 159
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004292 160 LLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHILV 226
Cdd:COG0666  205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-111 8.27e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 8.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   10 LHHA-RNGNAEEVRKLLaamarmEVVADIDCKgrskSNLGWTPLHLACYFGHKQVVEdLLKAGAKVNMlNDMGDTPLHRA 88
Cdd:pfam12796   1 LHLAaKNGNLELVKLLL------ENGADANLQ----DKNGRTALHLAAKNGHLEIVK-LLLEHADVNL-KDNGRTALHYA 68
                          90       100
                  ....*....|....*....|...
gi 569004292   89 AFTGRKELVLLLLEYDADSTVVN 111
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
14-216 3.09e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.05  E-value: 3.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  14 RNGNAEEVRKLLAAMArmevvADIdckgRSKSNLGWTPLH--LACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHraAFT 91
Cdd:PHA03095  92 YNATTLDVIKLLIKAG-----ADV----NAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  92 GRK----ELVLLLLEYDADSTVVNGSGQTAKEathdkeirNMLEAVeRTQQRKLEELL------LGAAREGRTAEVS-AL 160
Cdd:PHA03095 161 KSRnanvELLRLLIDAGADVYAVDDRFRSLLH--------HHLQSF-KPRARIVRELIragcdpAATDMLGNTPLHSmAT 231
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004292 161 LSRPNPP----------DVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:PHA03095 232 GSSCKRSlvlplliagiSINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
48-76 5.65e-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: 5.65e-06
                           10        20
                   ....*....|....*....|....*....
gi 569004292    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 2.52e-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: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   9 LLHHARNGNAEEVRKLLaamarmeVVADIDCKGRSKsnLGWTPLHLACYFGHKQVVEDLLKAGAK-VN--MLNDM--GDT 83
Cdd:cd22192   21 LLLAAKENDVQAIKKLL-------KCPSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPElVNepMTSDLyqGET 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  84 PLHRAAFTGRKELVLLLLEYDADstVVNgsgqtaKEATHdkeirnmleAVERTQQRKL----EELLLGAAREGRTAEVSA 159
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGAD--VVS------PRATG---------TFFRPGPKNLiyygEHPLSFAACVGNEEIVRL 154
                        170       180
                 ....*....|....*....|..
gi 569004292 160 LLSRPNppDVNCSDQLGNTPLH 181
Cdd:cd22192  155 LIEHGA--DIRAQDSLGNTVLH 174
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
238-314 3.49e-04

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: 40.61  E-value: 3.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   238 YEGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYR-----QGCKhLTQAVCTVKPTDSCLFSIRCFDDTVHC 310
Cdd:smart00233   3 KEGWLYKksGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKgsidlSGCT-VREAPDPDSSKKPHCFEIKTSDRKTLL 81

                   ....
gi 569004292   311 FRVP 314
Cdd:smart00233  82 LQAE 85
 
Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
507-902 0e+00

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 561.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  507 SIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKPFNP 586
Cdd:pfam01237   1 SLWSILKKNIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRVKKPFNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  587 LLGETYELVRDDLGFRLISEQVSHHPPISAFHAEglNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLDHNEAYTWTN 666
Cdd:pfam01237  81 LLGETFELVRPDKGFRFIAEQVSHHPPISAFHAE--SKGWTFWGEIAPKSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  667 PTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFG-KELHKVEGYIQDKSKKKLCALYGKWTECLYSvdpat 745
Cdd:pfam01237 159 PTTYVHNIIFGKLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSNEVTGKVYDKNGKVLYTLSGKWNESLYI----- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  746 fdaykkndkknteeKKNSKQTSSSEESDEMPVPDSEsvfiipgSVLLWRIAPRPPNsaqMYNFTSFAMVLNEVDkEMESV 825
Cdd:pfam01237 234 --------------KDVSTGKKSSEDDSVEEQPDGE-------SRLLWKAGPLPNA---YYGFTSFAVTLNELT-DELGK 288
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004292  826 IPKTDCRLRPDIRAMENGEIDLASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQ-GPNPYSGAQDWIYSGSYWDRNY 902
Cdd:pfam01237 289 LPPTDSRLRPDQRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKvKDDPVTGEEYWKYKGGYWERRE 366
PH_ORP1 cd13285
Human Oxysterol binding protein related protein 1 Pleckstrin homology (PH) domain; Human ORP1 ...
229-324 3.80e-54

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: 183.75  E-value: 3.80e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 229 KVVHKALKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTV 308
Cdd:cd13285    1 KVINKVVKRFEGQLWKSSRFFGWRSYWVVLEDGVLSWYHKQADAAAGIKRQGCKSLTQAKCTVKSTDSCFFTIRCFDDTV 80
                         90
                 ....*....|....*..
gi 569004292 309 HCFRVP-KNSVQQSRER 324
Cdd:cd13285   81 HRFKVPpKNNPVVTRKK 97
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-226 1.35e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   1 MNTEAEQQLLHHA-RNGNAEEVRKLLAAMArmevvaDIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLND 79
Cdd:COG0666   82 AKDDGGNTLLHAAaRNGDLEIVKLLLEAGA------DVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  80 MGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAkeathdkeirnmleavertqqrkleelLLGAAREGRTAEVSA 159
Cdd:COG0666  152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP---------------------------LHLAAENGHLEIVKL 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004292 160 LLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHILV 226
Cdd:COG0666  205 LLE--AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-225 3.37e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 3.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   9 LLHHARNGNAEEVRKLLAAMARMEVVADIDCKGRSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRA 88
Cdd:COG0666   15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  89 AFTGRKELVLLLLEYDADSTVVNGSGQT----AKEATHDKEIRNMLEA---VERtQQRKLEELLLGAAREGRTAEVSALL 161
Cdd:COG0666   95 ARNGDLEIVKLLLEAGADVNARDKDGETplhlAAYNGNLEIVKLLLEAgadVNA-QDNDGNTPLHLAAANGNLEIVKLLL 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569004292 162 SrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHIL 225
Cdd:COG0666  174 E--AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-149 6.74e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 6.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   9 LLHHA-RNGNAEEVRKLLAAmarmevVADIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHR 87
Cdd:COG0666  156 PLHLAaANGNLEIVKLLLEA------GADVN----ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569004292  88 AAFTGRKELVLLLLEYDADSTVVNGSGQTAKEATHDKEIRNMLEAVERTQQRKLEELLLGAA 149
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-111 8.27e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 8.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   10 LHHA-RNGNAEEVRKLLaamarmEVVADIDCKgrskSNLGWTPLHLACYFGHKQVVEdLLKAGAKVNMlNDMGDTPLHRA 88
Cdd:pfam12796   1 LHLAaKNGNLELVKLLL------ENGADANLQ----DKNGRTALHLAAKNGHLEIVK-LLLEHADVNL-KDNGRTALHYA 68
                          90       100
                  ....*....|....*....|...
gi 569004292   89 AFTGRKELVLLLLEYDADSTVVN 111
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-206 6.92e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 6.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   52 LHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYdadstvvngsgqtakeathdkeirnmle 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004292  132 avertqqrkleelllgaaregrtaevsallsrpnpPDVNCSDQlGNTPLHCAAYRAHKQCVLKLLRSGADPSLKN 206
Cdd:pfam12796  53 -----------------------------------ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
14-216 3.09e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.05  E-value: 3.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  14 RNGNAEEVRKLLAAMArmevvADIdckgRSKSNLGWTPLH--LACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHraAFT 91
Cdd:PHA03095  92 YNATTLDVIKLLIKAG-----ADV----NAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  92 GRK----ELVLLLLEYDADSTVVNGSGQTAKEathdkeirNMLEAVeRTQQRKLEELL------LGAAREGRTAEVS-AL 160
Cdd:PHA03095 161 KSRnanvELLRLLIDAGADVYAVDDRFRSLLH--------HHLQSF-KPRARIVRELIragcdpAATDMLGNTPLHSmAT 231
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004292 161 LSRPNPP----------DVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:PHA03095 232 GSSCKRSlvlplliagiSINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank_4 pfam13637
Ankyrin repeats (many copies);
48-101 3.50e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.91  E-value: 3.50e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 569004292   48 GWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLL 101
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
10-216 1.03e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  10 LHHARNGNAEEVRKLLAamarmevvaDIDCKGRSKSNLGWTPLHLACYFGH-----KQVVEDLLKAGAKVNMLNDMGDTP 84
Cdd:PHA03100  39 LYLAKEARNIDVVKILL---------DNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  85 LHRAAFT--GRKELVLLLLEYDADSTVVNGSGQtakeathdkeirNMLEAVERTQQRKLE--ELLL--GAAREGRTaEVS 158
Cdd:PHA03100 110 LLYAISKksNSYSIVEYLLDNGANVNIKNSDGE------------NLLHLYLESNKIDLKilKLLIdkGVDINAKN-RVN 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 569004292 159 ALLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:PHA03100 177 YLLS--YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
18-228 1.30e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  18 AEEVRKLLAAmarmevVADIDCKGrsksNLGWTPLHLACYFGHKQ---VVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRK 94
Cdd:PHA03095  27 VEEVRRLLAA------GADVNFRG----EYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  95 ELVL-LLLEYDADSTVVNGSGQTA------KEATHDKEIRNMLEAvertqqrkleelllGA---ARE--GRTAeVSALLS 162
Cdd:PHA03095  97 LDVIkLLIKAGADVNAKDKVGRTPlhvylsGFNINPKVIRLLLRK--------------GAdvnALDlyGMTP-LAVLLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 163 RPNPP------------DVNCSDQLGNTPLH--CAAYRAHKQCVLKLLRSGADPSLKNKNDQKPL-DLAQGAEMKHILVG 227
Cdd:PHA03095 162 SRNANvellrllidagaDVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSLVL 241

                 .
gi 569004292 228 N 228
Cdd:PHA03095 242 P 242
PHA02876 PHA02876
ankyrin repeat protein; Provisional
63-215 9.73e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 9.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  63 VVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAKEATHDKEIRNMLEAV--ERTQQRK 140
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIidNRSNINK 239
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004292 141 LEELLLGAAREgrTAEVSALLSRPNPPDVNCSDQLGNTPLHCAAYR-AHKQCVLKLLRSGADPSLKNKNDQKPLDL 215
Cdd:PHA02876 240 NDLSLLKAIRN--EDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYL 313
PHA03100 PHA03100
ankyrin repeat protein; Provisional
9-106 4.61e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.68  E-value: 4.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   9 LLHHARNGNAEEVRKLLaamarMEVVADIDckgrSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRA 88
Cdd:PHA03100 162 LIDKGVDINAKNRVNYL-----LSYGVPIN----IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
                         90
                 ....*....|....*...
gi 569004292  89 AFTGRKELVLLLLEYDAD 106
Cdd:PHA03100 233 ILNNNKEIFKLLLNNGPS 250
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
8-103 5.33e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 5.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   8 QLLHHARNGNAEEVRKLLAAMArmevvaDIDCKGRSksnlGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHR 87
Cdd:PTZ00322  85 ELCQLAASGDAVGARILLTGGA------DPNCRDYD----GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
                         90
                 ....*....|....*.
gi 569004292  88 AAFTGRKELVLLLLEY 103
Cdd:PTZ00322 155 AEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
10-235 9.49e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 9.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  10 LHHArnGNAEEVRKLLAAMarMEVVADIDckgrSKSNLGWTPLHLACYFGH-KQVVEDLLKAGAKVNMLNDMGDTPLHRA 88
Cdd:PHA02876 277 LHHA--SQAPSLSRLVPKL--LERGADVN----AKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQA 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  89 AFTGR-KELVLLLLEYDADstvVNGSGQTAKEATHDKEIRNML----------EAVERTQQRKLEELLLGAAREGRTAEV 157
Cdd:PHA02876 349 STLDRnKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVviintlldygADIEALSQKIGTALHFALCGTNPYMSV 425
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 158 SALLSRPnpPDVNCSDQLGNTPLHCAAYRAHKQCVLK-LLRSGADPSLKNKNDQKPLDLA------------QGAEMKHi 224
Cdd:PHA02876 426 KTLIDRG--ANVNSKNKDLSTPLHYACKKNCKLDVIEmLLDNGADVNAINIQNQYPLLIAleyhgivnillhYGAELRD- 502
                        250
                 ....*....|.
gi 569004292 225 lvgNKVVHKAL 235
Cdd:PHA02876 503 ---SRVLHKSL 510
PHA02874 PHA02874
ankyrin repeat protein; Provisional
7-309 1.07e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.44  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   7 QQLLHHA-RNGNAEEVRKLLaamarmEVVADIDCKGRSksnlGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPL 85
Cdd:PHA02874 125 KTFLHYAiKKGDLESIKMLF------EYGADVNIEDDN----GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  86 HRAAFTGRKELVLLLLEYDADSTVVNGSGQTakeATHDKEIRNmleavertqqRKLEELLLgaaregrtaevsallsrpN 165
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFT---PLHNAIIHN----------RSAIELLI------------------N 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 166 PPDVNCSDQLGNTPLHCA-AYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHILVGNKVVHKALKRYEGPLwK 244
Cdd:PHA02874 244 NASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIKEADKL-K 322
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004292 245 SSRFFGWKlfwVVLEHGVLSWYRKQPD---AVHNSYRQGCKHLTQAVCTVKPT-------DSCLFSIRCFDDTVH 309
Cdd:PHA02874 323 DSDFLEHI---EIKDNKEFSDFIKECNeeiEDMKKTKCGCDKNIFDLCLIRIKhkfdgneDSIKDYLNCLDDNSH 394
PHA02874 PHA02874
ankyrin repeat protein; Provisional
50-213 9.01e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 9.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  50 TPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVV------NGSGQTAKEATHD 123
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILpipcieKDMIKTILDCGID 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 124 KEIRNmleavertqqRKLEELLLGAAREGRTAEVSALLSRpnPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPS 203
Cdd:PHA02874 117 VNIKD----------AELKTFLHYAIKKGDLESIKMLFEY--GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                        170
                 ....*....|
gi 569004292 204 LKNKNDQKPL 213
Cdd:PHA02874 185 VKDNNGESPL 194
PH_FAPP1_FAPP2 cd01247
Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain; Human FAPP1 (also ...
239-302 1.80e-07

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: 50.10  E-value: 1.80e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004292 239 EGPLWKSSRFF-GWKLFWVVLEHGVLSWYRKQpDAVHnsyrQGCK-HLTQAVC--TVKPTDSCLFSIR 302
Cdd:cd01247    2 EGVLWKWTNYLsGWQPRWFVLDDGVLSYYKSQ-EEVN----QGCKgSVKMSVCeiIVHPTDPTRMDLI 64
Ank_5 pfam13857
Ankyrin repeats (many copies);
166-216 2.73e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 2.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 569004292  166 PPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLA 216
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
9-137 5.45e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 5.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   9 LLH-HARN--GNAEEVRKLLAAmarmevvadiDCKGRSKSNLGWTPLHLACYFGHKQ--VVEDLLKAGAKVNMLNDMGDT 83
Cdd:PHA03095 190 LLHhHLQSfkPRARIVRELIRA----------GCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQT 259
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 569004292  84 PLHRAAFTGRKELVLLLLEYDADSTVVNGSGQT-AKEATHDKEIRnMLEAVERTQ 137
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTpLSLMVRNNNGR-AVRAALAKN 313
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
59-240 6.41e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 6.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  59 GHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAK----EATHDKEIRNMLEAVE 134
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaiSAKHHKIFRILYHFAS 615
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 135 RTQQRKLEELLLGAAREGRTAEVSALLSRpnPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQ---- 210
Cdd:PLN03192 616 ISDPHAAGDLLCTAAKRNDLTAMKELLKQ--GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDfspt 693
                        170       180       190
                 ....*....|....*....|....*....|...
gi 569004292 211 KPLDLAQGAEMKH---ILVGNKVVHKALKRYEG 240
Cdd:PLN03192 694 ELRELLQKRELGHsitIVDSVPADEPDLGRDGG 726
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
149-216 7.58e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 7.58e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004292 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 9.04e-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: 9.04e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 569004292   48 GWTPLHLACY-FGHKQVVEDLLKAGAKVNMLND 79
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-224 1.46e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  145 LLGAAREGRTAEVSALLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVlKLLRSGADPSLKNkNDQKPLDLAqgAEMKHI 224
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKD-NGRTALHYA--ARSGHL 74
Ank_4 pfam13637
Ankyrin repeats (many copies);
148-196 1.79e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.79e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 569004292  148 AAREGRTAEVSALLSrpNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLL 196
Cdd:pfam13637   8 AAASGHLELLRLLLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
35-240 2.64e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.03  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  35 ADIDCKGRSKSNlgwTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSG 114
Cdd:PHA02878 158 ADINMKDRHKGN---TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 115 QTAkeathdkeirnMLEAVERTQQRKLEELLLgaareGRTAEVSALlsrpnppdvncSDQLGNTPLHCAayrAHKQCVLK 194
Cdd:PHA02878 235 NTP-----------LHISVGYCKDYDILKLLL-----EHGVDVNAK-----------SYILGLTALHSS---IKSERKLK 284
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 569004292 195 -LLRSGADPSLKNKNDQKPLDLA----QGAEMKHILVGN----KVVHKALKRYEG 240
Cdd:PHA02878 285 lLLEYGADINSLNSYKLTPLSSAvkqyLCINIGRILISNicllKRIKPDIKNSEG 339
PHA03100 PHA03100
ankyrin repeat protein; Provisional
61-130 2.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 2.91e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569004292  61 KQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAKE---ATHDKEIRNML 130
Cdd:PHA03100 172 KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHiaiLNNNKEIFKLL 244
PH_ORP9 cd13290
Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 ...
239-326 5.18e-06

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: 45.90  E-value: 5.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 239 EGPLWKSSRFF-GWKLFWVVLEH--GVLSWYRKQpDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTVHcFRvpk 315
Cdd:cd13290    2 EGPLSKWTNVMkGWQYRWFVLDDnaGLLSYYTSK-EKMMRGSRRGCVRLKGAVVGIDDEDDSTFTITVDQKTFH-FQ--- 76
                         90
                 ....*....|.
gi 569004292 316 nsVQQSRERAQ 326
Cdd:cd13290   77 --ARDAEERER 85
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
176-207 5.60e-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: 5.60e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 569004292  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 5.65e-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: 5.65e-06
                           10        20
                   ....*....|....*....|....*....
gi 569004292    48 GWTPLHLACYFGHKQVVEDLLKAGAKVNM 76
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
48-88 2.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 569004292   48 GWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRA 88
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
67-168 3.87e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  67 LLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAkeathdkeirnmLEAVERTQQRKLEELLL 146
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP------------LELAEENGFREVVQLLS 168
                         90       100
                 ....*....|....*....|..
gi 569004292 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 4.90e-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: 41.09  E-value: 4.90e-05
                          10        20
                  ....*....|....*....|....*....
gi 569004292   48 GWTPLHLACYFGHKQVVEDLLKAGAKVNM 76
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PH_Osh1p_Osh2p_yeast cd13292
Yeast oxysterol binding protein homologs 1 and 2 Pleckstrin homology (PH) domain; Yeast Osh1p ...
250-296 9.52e-05

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: 42.30  E-value: 9.52e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 569004292 250 GWKLFWVVLEHGVLSWYRKQPDavHNSYRQGCKHLtqAVCTVKPTDS 296
Cdd:cd13292   17 GYKTRWFVLEDGVLSYYRHQDD--EGSACRGSINM--KNARLVSDPS 59
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-117 1.49e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569004292   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 2.52e-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: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   9 LLHHARNGNAEEVRKLLaamarmeVVADIDCKGRSKsnLGWTPLHLACYFGHKQVVEDLLKAGAK-VN--MLNDM--GDT 83
Cdd:cd22192   21 LLLAAKENDVQAIKKLL-------KCPSCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAAPElVNepMTSDLyqGET 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  84 PLHRAAFTGRKELVLLLLEYDADstVVNgsgqtaKEATHdkeirnmleAVERTQQRKL----EELLLGAAREGRTAEVSA 159
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGAD--VVS------PRATG---------TFFRPGPKNLiyygEHPLSFAACVGNEEIVRL 154
                        170       180
                 ....*....|....*....|..
gi 569004292 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 2.89e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 2.89e-04
                           10        20
                   ....*....|....*....|....*....
gi 569004292   176 GNTPLHCAAYRAHKQCVLKLLRSGADPSL 204
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
238-314 3.49e-04

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: 40.61  E-value: 3.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292   238 YEGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYR-----QGCKhLTQAVCTVKPTDSCLFSIRCFDDTVHC 310
Cdd:smart00233   3 KEGWLYKksGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKgsidlSGCT-VREAPDPDSSKKPHCFEIKTSDRKTLL 81

                   ....
gi 569004292   311 FRVP 314
Cdd:smart00233  82 LQAE 85
Ank_4 pfam13637
Ankyrin repeats (many copies);
176-216 1.42e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 569004292  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 1.80e-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: 1.80e-03
                           10        20
                   ....*....|....*....|....*..
gi 569004292    80 MGDTPLHRAAFTGRKELVLLLLEYDAD 106
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-117 2.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 569004292   81 GDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTA 117
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
238-312 2.08e-03

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: 38.29  E-value: 2.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004292 238 YEGPLWK--SSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQ-GCKHLTQAVCTVKPTDSCLFSIRCFDDTVHCFR 312
Cdd:cd00821    1 KEGYLLKrgGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSiPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQ 78
PHA02946 PHA02946
ankyin-like protein; Provisional
127-220 3.07e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 127 RNMLEAVERTQQRKLEELLLG-AAREGRTAEvsALLSRPNPPdvNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLK 205
Cdd:PHA02946  26 RNMLQAIEPSGNYHILHAYCGiKGLDERFVE--ELLHRGYSP--NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNAC 101
                         90
                 ....*....|....*
gi 569004292 206 NKNDQKPLDLAQGAE 220
Cdd:PHA02946 102 DKQHKTPLYYLSGTD 116
PH_GPBP cd13283
Goodpasture antigen binding protein Pleckstrin homology (PH) domain; The GPBP (also called ...
250-312 3.69e-03

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: 37.65  E-value: 3.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004292 250 GWKLFWVVLEHGVLSWYRKQPDAVHnsyrqGCK---HLTQAVCTVKPTDSCLFSIrCFDDTVHCFR 312
Cdd:cd13283   14 GWQDRYFVLKDGTLSYYKSESEKEY-----GCRgsiSLSKAVIKPHEFDECRFDV-SVNDSVWYLR 73
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
81-106 4.36e-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: 4.36e-03
                          10        20
                  ....*....|....*....|....*.
gi 569004292   81 GDTPLHRAAFTGRKELVLLLLEYDAD 106
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02878 PHA02878
ankyrin repeat protein; Provisional
62-206 5.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 5.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  62 QVVEDLLKAGAKVNMLN-DMGDTPLHRAAFTGRKELVLLLLEYDADstvVNGSGQTAKEATHdkeirnmlEAVERTQQRK 140
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGAN---VNIPDKTNNSPLH--------HAVKHYNKPI 216
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004292 141 LEELLlgaaregrtaevsallsrPNPPDVNCSDQLGNTPLHCAAYRAHKQCVLK-LLRSGADPSLKN 206
Cdd:PHA02878 217 VHILL------------------ENGASTDARDKCGNTPLHISVGYCKDYDILKlLLEHGVDVNAKS 265
PHA02875 PHA02875
ankyrin repeat protein; Provisional
55-216 5.48e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  55 ACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVvngsgqtakeatHDKEIRNML-EAV 133
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV------------KYPDIESELhDAV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292 134 ERTQQRKLEELLLgaarEGRTAEvsallsrpnppDVNCSDqlGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPL 213
Cdd:PHA02875  77 EEGDVKAVEELLD----LGKFAD-----------DVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                 ...
gi 569004292 214 DLA 216
Cdd:PHA02875 140 HLA 142
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
81-111 6.56e-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: 6.56e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 569004292   81 GDTPLHRAA-FTGRKELVLLLLEYDADSTVVN 111
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
48-163 8.44e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 8.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004292  48 GWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTA---KEATHDK 124
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPliiAMAKGDI 181
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 569004292 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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