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Conserved domains on  [gi|1207185434|ref|XP_021334529|]
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alsin [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_alsin cd13269
Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...
 907-1018 3.49e-47

Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual specificity for Rac1 and Rab5 GTPases. Alsin mutations in the form of truncated proteins are responsible for motor function disorders including juvenile-onset amyotrophic lateral sclerosis, familial juvenile primary lateral sclerosis, and infantile-onset ascending hereditary spastic paralysis. The alsin protein is widely expressed in the developing CNS including neurons of the cerebral cortex, brain stem, spinal cord, and cerebellum. Alsin contains a regulator of chromosome condensation 1 (RCC1) domain, a Rho guanine nucleotide exchanging factor (RhoGEF) domain, a PH domain, a Membrane Occupation and Recognition Nexus (MORN), a vacuolar protein sorting 9 (Vps9) domain, and a Dbl homology (DH) domain. Alsin interacts with Rab5 through its Vps9 domain and through this interaction modulates early endosome fusion and trafficking. The GEF activity of alsin towards Rab5 is regulated by Rac1 function. The GEF activity of alsin for Rac1 occurs via its DH domain and this interaction plays a role in promoting spinal motor neuron survival via multiple Rac-dependent signaling pathways. 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: 241423  Cd Length: 106  Bit Score: 164.10  E-value: 3.49e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  907 EALRKPSRRLVCESSNKGLTLQNAGRFSASWFILFNDVLVHAQgsipskklFSSHYVYPLATLWVEPISDESLGLLGLKL 986
Cdd:cd13269      1 DSLRSPDRRLIRESSTRPLTLQNAGRFSSHWFILFNDALVHAQ--------FSTHHIFPLATLWVEPIPDEDSGQNALKI 72

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1207185434  987 TTPEDSFVVLATSPLEKGKWLRAINQAIDEVL 1018
Cdd:cd13269     73 TTPEESFTLVASTPQEKAEWLRAINQAIDQAL 104
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1055-1212 3.00e-42

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 156.65  E-value: 3.00e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1055 DAKYEGRWLSGKPHGKGNLKWPDGTMYCGTFKSGLEDGFGDFmtpstTFNKFERYQGHWKEGKMHGFGTFWYASGEVYEG 1134
Cdd:COG4642    124 GGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTL-----TYADGDRYEGEFKNGKRHGQGTLTYANGDVYEG 198

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185434 1135 SFRENMRHGHGMLRSgkvaspSSSSVFVGQWVQGKRTGYGVCdDFSRGEKYMGIWHDDQRHGDGVVITQFGLYYEGNF 1212
Cdd:COG4642    199 EFKNGQRHGQGTYTY------ADGDRYEGEFKNGKRHGQGTL-TYADGDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 46-213 1.04e-26

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


:

Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 113.53  E-value: 1.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434   46 ALGSLHGLLLIEGGQVYSFGEQPWKPV----EPPPASLVLESTLSGqhVISVSAGSYHCSAVTEDGLVLMWGENSYGQCG 121
Cdd:COG5184    155 AAGGYHTCALKSDGTVWCWGANSYGQLgdgtTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLG 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  122 VSGTDRVPSPTPVTVVDDethppqlvrVLNVACGAQHTLALSNKHEVWAWGSG--CQLGLVTNVfPVWKPQKVEHLVGry 199
Cdd:COG5184    233 DGTTTDRATPVQVAGLTG---------VVAIAAGGSHTCALKSDGTVWCWGDNsyGQLGDGTTT-DRSTPVKVPGLSG-- 300

                          170
                   ....*....|....
gi 1207185434  200 VVQIACGAFHSLAL 213
Cdd:COG5184    301 VVAVAAGSSHTCAL 314
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 1559-1657 2.45e-22

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


:

Pssm-ID: 460489  Cd Length: 104  Bit Score: 93.43  E-value: 2.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1559 TAVETLQQISTAFTPSDKLQVIQLTFEEVTQDVQAILcQDFLWCMDDLFPIFLYVVLRARIRNLGSEVSLIEDLTDSNLQ 1638
Cdd:pfam02204    3 QAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSN-RDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDLL 81

                           90
                   ....*....|....*....
gi 1207185434 1639 LGQLGFMLTTLKACYNQIQ 1657
Cdd:pfam02204   82 SGEEGYYLTTLEAALEFIE 100
ATS1 super family cl34932
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 530-631 1.53e-17

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


The actual alignment was detected with superfamily member COG5184:

Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 86.18  E-value: 1.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  530 VWSWGKGHEGQLGHGDYLPRLQPLCIKSLSKkeVVKITAGANHSLALTAQCQVYSWGSEKFGQLGR-----MNSPSTVPN 604
Cdd:COG5184     19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDgtttdRTTPVKVPG 96

                           90       100
                   ....*....|....*....|....*...
gi 1207185434  605 LTTVSdgirvwDVAAGQTHTL-LLADGD 631
Cdd:COG5184     97 LTGVV------AVAAGYYHSCaLKSDGT 118
 
Name Accession Description Interval E-value
PH_alsin cd13269
Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...
 907-1018 3.49e-47

Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual specificity for Rac1 and Rab5 GTPases. Alsin mutations in the form of truncated proteins are responsible for motor function disorders including juvenile-onset amyotrophic lateral sclerosis, familial juvenile primary lateral sclerosis, and infantile-onset ascending hereditary spastic paralysis. The alsin protein is widely expressed in the developing CNS including neurons of the cerebral cortex, brain stem, spinal cord, and cerebellum. Alsin contains a regulator of chromosome condensation 1 (RCC1) domain, a Rho guanine nucleotide exchanging factor (RhoGEF) domain, a PH domain, a Membrane Occupation and Recognition Nexus (MORN), a vacuolar protein sorting 9 (Vps9) domain, and a Dbl homology (DH) domain. Alsin interacts with Rab5 through its Vps9 domain and through this interaction modulates early endosome fusion and trafficking. The GEF activity of alsin towards Rab5 is regulated by Rac1 function. The GEF activity of alsin for Rac1 occurs via its DH domain and this interaction plays a role in promoting spinal motor neuron survival via multiple Rac-dependent signaling pathways. 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: 241423  Cd Length: 106  Bit Score: 164.10  E-value: 3.49e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  907 EALRKPSRRLVCESSNKGLTLQNAGRFSASWFILFNDVLVHAQgsipskklFSSHYVYPLATLWVEPISDESLGLLGLKL 986
Cdd:cd13269      1 DSLRSPDRRLIRESSTRPLTLQNAGRFSSHWFILFNDALVHAQ--------FSTHHIFPLATLWVEPIPDEDSGQNALKI 72

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1207185434  987 TTPEDSFVVLATSPLEKGKWLRAINQAIDEVL 1018
Cdd:cd13269     73 TTPEESFTLVASTPQEKAEWLRAINQAIDQAL 104
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1055-1212 3.00e-42

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 156.65  E-value: 3.00e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1055 DAKYEGRWLSGKPHGKGNLKWPDGTMYCGTFKSGLEDGFGDFmtpstTFNKFERYQGHWKEGKMHGFGTFWYASGEVYEG 1134
Cdd:COG4642    124 GGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTL-----TYADGDRYEGEFKNGKRHGQGTLTYANGDVYEG 198

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185434 1135 SFRENMRHGHGMLRSgkvaspSSSSVFVGQWVQGKRTGYGVCdDFSRGEKYMGIWHDDQRHGDGVVITQFGLYYEGNF 1212
Cdd:COG4642    199 EFKNGQRHGQGTYTY------ADGDRYEGEFKNGKRHGQGTL-TYADGDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 46-213 1.04e-26

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 113.53  E-value: 1.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434   46 ALGSLHGLLLIEGGQVYSFGEQPWKPV----EPPPASLVLESTLSGqhVISVSAGSYHCSAVTEDGLVLMWGENSYGQCG 121
Cdd:COG5184    155 AAGGYHTCALKSDGTVWCWGANSYGQLgdgtTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLG 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  122 VSGTDRVPSPTPVTVVDDethppqlvrVLNVACGAQHTLALSNKHEVWAWGSG--CQLGLVTNVfPVWKPQKVEHLVGry 199
Cdd:COG5184    233 DGTTTDRATPVQVAGLTG---------VVAIAAGGSHTCALKSDGTVWCWGDNsyGQLGDGTTT-DRSTPVKVPGLSG-- 300

                          170
                   ....*....|....
gi 1207185434  200 VVQIACGAFHSLAL 213
Cdd:COG5184    301 VVAVAAGSSHTCAL 314
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1058-1222 5.22e-23

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 106.46  E-value: 5.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1058 YEGRWLSGKPHGKGNLKWPDGTMYCGTFKSGLEDGFGDFMTPSTTfnkfeRYQGHWKEGKMHGFGTFWYASGEVYEGSFR 1137
Cdd:PLN03185    34 YEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGT-----TYKGRWRLNLKHGLGYQRYPNGDVFEGSWI 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1138 ENMRHGHGMLrsgkvaSPSSSSVFVGQWVQGKRTGYGVCdDFSRGEKYMGIWHDDQRHGDGVVITQFGLYYEGNFCNNRM 1217
Cdd:PLN03185   109 QGLQEGPGKY------TWANGNVYLGDMKGGKMSGKGTL-TWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLK 181


                   ....*
gi 1207185434 1218 MGNGT 1222
Cdd:PLN03185   182 DGKGV 186
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 1559-1657 2.45e-22

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


Pssm-ID: 460489  Cd Length: 104  Bit Score: 93.43  E-value: 2.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1559 TAVETLQQISTAFTPSDKLQVIQLTFEEVTQDVQAILcQDFLWCMDDLFPIFLYVVLRARIRNLGSEVSLIEDLTDSNLQ 1638
Cdd:pfam02204    3 QAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSN-RDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDLL 81

                           90
                   ....*....|....*....
gi 1207185434 1639 LGQLGFMLTTLKACYNQIQ 1657
Cdd:pfam02204   82 SGEEGYYLTTLEAALEFIE 100
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 530-631 1.53e-17

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 86.18  E-value: 1.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  530 VWSWGKGHEGQLGHGDYLPRLQPLCIKSLSKkeVVKITAGANHSLALTAQCQVYSWGSEKFGQLGR-----MNSPSTVPN 604
Cdd:COG5184     19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDgtttdRTTPVKVPG 96

                           90       100
                   ....*....|....*....|....*...
gi 1207185434  605 LTTVSdgirvwDVAAGQTHTL-LLADGD 631
Cdd:COG5184     97 LTGVV------AVAAGYYHSCaLKSDGT 118
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
529-576 5.20e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 64.85  E-value: 5.20e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207185434  529 EVWSWGKGHEGQLGHGDYLPRLQPLCIKSLSKKEVVKITAGANHSLAL 576
Cdd:pfam00415    3 RVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
167-213 1.44e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 1.44e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207185434  167 EVWAWGSG--CQLGLVTNVfPVWKPQKVEHLVGRYVVQIACGAFHSLAL 213
Cdd:pfam00415    3 RVYTWGRNdyGQLGLGTTE-NVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
1108-1127 7.79e-06

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 43.87  E-value: 7.79e-06
                            10        20
                    ....*....|....*....|
gi 1207185434  1108 RYQGHWKEGKMHGFGTFWYA 1127
Cdd:smart00698    2 RYEGEWRNGKRHGRGVYTYA 21
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 1109-1131 1.64e-05

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 42.78  E-value: 1.64e-05
                           10        20
                   ....*....|....*....|...
gi 1207185434 1109 YQGHWKEGKMHGFGTFWYASGEV 1131
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 1604-1656 3.74e-03

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


Pssm-ID: 128469  Cd Length: 117  Bit Score: 38.98  E-value: 3.74e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1207185434  1604 DDLFPIFLYVVLRARIRNLGSEVSLIEDLTDSNLQLGQLGFMLTTLKACYNQI 1656
Cdd:smart00167   47 DDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSLLTGEGGYYLTSLSAALALI 99
 
Name Accession Description Interval E-value
PH_alsin cd13269
Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...
 907-1018 3.49e-47

Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual specificity for Rac1 and Rab5 GTPases. Alsin mutations in the form of truncated proteins are responsible for motor function disorders including juvenile-onset amyotrophic lateral sclerosis, familial juvenile primary lateral sclerosis, and infantile-onset ascending hereditary spastic paralysis. The alsin protein is widely expressed in the developing CNS including neurons of the cerebral cortex, brain stem, spinal cord, and cerebellum. Alsin contains a regulator of chromosome condensation 1 (RCC1) domain, a Rho guanine nucleotide exchanging factor (RhoGEF) domain, a PH domain, a Membrane Occupation and Recognition Nexus (MORN), a vacuolar protein sorting 9 (Vps9) domain, and a Dbl homology (DH) domain. Alsin interacts with Rab5 through its Vps9 domain and through this interaction modulates early endosome fusion and trafficking. The GEF activity of alsin towards Rab5 is regulated by Rac1 function. The GEF activity of alsin for Rac1 occurs via its DH domain and this interaction plays a role in promoting spinal motor neuron survival via multiple Rac-dependent signaling pathways. 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: 241423  Cd Length: 106  Bit Score: 164.10  E-value: 3.49e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  907 EALRKPSRRLVCESSNKGLTLQNAGRFSASWFILFNDVLVHAQgsipskklFSSHYVYPLATLWVEPISDESLGLLGLKL 986
Cdd:cd13269      1 DSLRSPDRRLIRESSTRPLTLQNAGRFSSHWFILFNDALVHAQ--------FSTHHIFPLATLWVEPIPDEDSGQNALKI 72

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1207185434  987 TTPEDSFVVLATSPLEKGKWLRAINQAIDEVL 1018
Cdd:cd13269     73 TTPEESFTLVASTPQEKAEWLRAINQAIDQAL 104
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1055-1212 3.00e-42

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 156.65  E-value: 3.00e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1055 DAKYEGRWLSGKPHGKGNLKWPDGTMYCGTFKSGLEDGFGDFmtpstTFNKFERYQGHWKEGKMHGFGTFWYASGEVYEG 1134
Cdd:COG4642    124 GGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTL-----TYADGDRYEGEFKNGKRHGQGTLTYANGDVYEG 198

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185434 1135 SFRENMRHGHGMLRSgkvaspSSSSVFVGQWVQGKRTGYGVCdDFSRGEKYMGIWHDDQRHGDGVVITQFGLYYEGNF 1212
Cdd:COG4642    199 EFKNGQRHGQGTYTY------ADGDRYEGEFKNGKRHGQGTL-TYADGDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1058-1237 1.92e-38

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 145.48  E-value: 1.92e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1058 YEGRWLSGKPHGKGNLKWPDGTMYCGTFKSGLEDGFGdfmtpSTTFNKFERYQGHWKEGKMHGFGTFWYASGEVYEGSFR 1137
Cdd:COG4642    104 GGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGG-----IYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1138 ENMRHGHGMLRSgkvaspSSSSVFVGQWVQGKRTGYGVCDdFSRGEKYMGIWHDDQRHGDGVVITQFGLYYEGNFCNNRM 1217
Cdd:COG4642    179 NGKRHGQGTLTY------ANGDVYEGEFKNGQRHGQGTYT-YADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKR 251

                          170       180
                   ....*....|....*....|
gi 1207185434 1218 MGNGTLLCDDDTVFEGDFQD 1237
Cdd:COG4642    252 HGQGTMTYADGSVYEGEWKN 271
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1043-1276 3.58e-30

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 121.60  E-value: 3.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1043 SNYTFSKEGRLKDAKYEGRWLSGKPHGKGNLKWPDGTMYCGTFKSGLEDGFGDFMTPSTTFNKFERYQ-------GHWKE 1115
Cdd:COG4642     31 GEGGGGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGGEGGVTAAGGGGGGGGGKGDGGDGGGGEGGFgggggggGGKKG 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1116 GKMHGFGTFWYASGEVYEGSFRENMRHGHGMLRSgkvaspSSSSVFVGQWVQGKRTGYGVcDDFSRGEKYMGIWHDDQRH 1195
Cdd:COG4642    111 GGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTF------PNGDVYEGEFKNGKPHGQGT-LTYADGDRYEGEFKNGKRH 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1196 GDGVVITQFGLYYEGNFCNNRMMGNGTLLCDDDTVFEGDFQDDwTLCGKGILFMPNGDsfdgVFDGHWGSGLRV-AGTFT 1274
Cdd:COG4642    184 GQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNG-KRHGQGTLTYADGD----RYEGEFKNGKRHgQGTMT 258


                   ..
gi 1207185434 1275 KP 1276
Cdd:COG4642    259 YA 260
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 46-213 1.04e-26

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 113.53  E-value: 1.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434   46 ALGSLHGLLLIEGGQVYSFGEQPWKPV----EPPPASLVLESTLSGqhVISVSAGSYHCSAVTEDGLVLMWGENSYGQCG 121
Cdd:COG5184    155 AAGGYHTCALKSDGTVWCWGANSYGQLgdgtTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLG 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  122 VSGTDRVPSPTPVTVVDDethppqlvrVLNVACGAQHTLALSNKHEVWAWGSG--CQLGLVTNVfPVWKPQKVEHLVGry 199
Cdd:COG5184    233 DGTTTDRATPVQVAGLTG---------VVAIAAGGSHTCALKSDGTVWCWGDNsyGQLGDGTTT-DRSTPVKVPGLSG-- 300

                          170
                   ....*....|....
gi 1207185434  200 VVQIACGAFHSLAL 213
Cdd:COG5184    301 VVAVAAGSSHTCAL 314
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 30-213 2.44e-25

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 109.30  E-value: 2.44e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434   30 SVSPEKLLLSRPVLHAALGSLHGLLLIEGGQVYSFGE-------QPWKPVEPPPASLvleSTLSGqhVISVSAGSYHCSA 102
Cdd:COG5184     38 RSTPVRVPGLSNVVAVAAGGDHTCALKADGTVWCWGNnsygqlgDGTTTDRTTPVKV---PGLTG--VVAVAAGYYHSCA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  103 VTEDGLVLMWGENSYGQCGVSGTDRVPSPTPVtvvddethPPQLVRVLNVACGAQHTLALSNKHEVWAWGSG--CQLGLV 180
Cdd:COG5184    113 LKSDGTVWCWGDNSSGQLGDGTTTNRLTPVQV--------DAGLSGVVAIAAGGYHTCALKSDGTVWCWGANsyGQLGDG 184

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1207185434  181 TNVfPVWKPQKVEHLVGryVVQIACGAFHSLAL 213
Cdd:COG5184    185 TTT-DRPTPVQVGGLSG--VVAVAAGGDHSCAL 214
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 30-213 2.44e-24

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 106.21  E-value: 2.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434   30 SVSPEKLLLSRPVLHAALGSLHGLLLIEGGQVYSFGEQPWKPVEPPPASLVL-----ESTLSGqhVISVSAGSYHCSAVT 104
Cdd:COG5184     88 RTTPVKVPGLTGVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTTNRLtpvqvDAGLSG--VVAIAAGGYHTCALK 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  105 EDGLVLMWGENSYGQCGVSGTDRVPSPTPVTVVDDethppqlvrVLNVACGAQHTLALSNKHEVWAWG---SGcQLGLVT 181
Cdd:COG5184    166 SDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG---------VVAVAAGGDHSCALKSDGTVWCWGsnsSG-QLGDGT 235

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1207185434  182 NVfPVWKPQKVEHLVGryVVQIACGAFHSLAL 213
Cdd:COG5184    236 TT-DRATPVQVAGLTG--VVAIAAGGSHTCAL 264
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1058-1222 5.22e-23

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 106.46  E-value: 5.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1058 YEGRWLSGKPHGKGNLKWPDGTMYCGTFKSGLEDGFGDFMTPSTTfnkfeRYQGHWKEGKMHGFGTFWYASGEVYEGSFR 1137
Cdd:PLN03185    34 YEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGT-----TYKGRWRLNLKHGLGYQRYPNGDVFEGSWI 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1138 ENMRHGHGMLrsgkvaSPSSSSVFVGQWVQGKRTGYGVCdDFSRGEKYMGIWHDDQRHGDGVVITQFGLYYEGNFCNNRM 1217
Cdd:PLN03185   109 QGLQEGPGKY------TWANGNVYLGDMKGGKMSGKGTL-TWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLK 181


                   ....*
gi 1207185434 1218 MGNGT 1222
Cdd:PLN03185   182 DGKGV 186
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 46-213 1.13e-22

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 101.21  E-value: 1.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434   46 ALGSLHGLLLIEGGQVYSFGEQPW------------KPVEPPPASlvlestlsgqHVISVSAGSYHCSAVTEDGLVLMWG 113
Cdd:COG5184      4 AAGGSHSCALKSDGTVWCWGDNSYgqlgdgtttdrsTPVRVPGLS----------NVVAVAAGGDHTCALKADGTVWCWG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  114 ENSYGQCGVSGTDRVPSPTPVtvvddethpPQLVRVLNVACGAQHTLALSNKHEVWAWGSGC--QLGLVTNVfPVWKPQK 191
Cdd:COG5184     74 NNSYGQLGDGTTTDRTTPVKV---------PGLTGVVAVAAGYYHSCALKSDGTVWCWGDNSsgQLGDGTTT-NRLTPVQ 143

                          170       180
                   ....*....|....*....|..
gi 1207185434  192 VEHLVGRyVVQIACGAFHSLAL 213
Cdd:COG5184    144 VDAGLSG-VVAIAAGGYHTCAL 164
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 1559-1657 2.45e-22

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


Pssm-ID: 460489  Cd Length: 104  Bit Score: 93.43  E-value: 2.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1559 TAVETLQQISTAFTPSDKLQVIQLTFEEVTQDVQAILcQDFLWCMDDLFPIFLYVVLRARIRNLGSEVSLIEDLTDSNLQ 1638
Cdd:pfam02204    3 QAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSN-RDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDLL 81

                           90
                   ....*....|....*....
gi 1207185434 1639 LGQLGFMLTTLKACYNQIQ 1657
Cdd:pfam02204   82 SGEEGYYLTTLEAALEFIE 100
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1058-1271 3.45e-22

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 104.14  E-value: 3.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1058 YEGRWLSGKPHGKGNLKWPDGTMYCGTFKSGLEDGFGDFMTPSTTfnkfeRYQGHWKEGKMHGFGTFWYASGEVYEGSFR 1137
Cdd:PLN03185    11 YSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGA-----TYEGEFSGGYMHGSGTYTGTDGTTYKGRWR 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1138 ENMRHGHGMLRSgkvaspSSSSVFVGQWVQGKRTGYGVCdDFSRGEKYMGIWHDDQRHGDGVVITQFGLYYEGNFCNNRM 1217
Cdd:PLN03185    86 LNLKHGLGYQRY------PNGDVFEGSWIQGLQEGPGKY-TWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMM 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207185434 1218 MGNGTLLCDDDTVFEGdfqdDWTLC---GKGIlFMPNGdSFDGVFDGHWGSGLRVAG 1271
Cdd:PLN03185   159 HGFGVYTWSDGGCYVG----TWTRGlkdGKGV-FYPAG-SRVPAVQEFYLNALRKRG 209
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 91-213 4.59e-22

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 99.67  E-value: 4.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434   91 ISVSAGSYHCSAVTEDGLVLMWGENSYGQCGVSGTDRVPSPTPVtvvddethpPQLVRVLNVACGAQHTLALSNKHEVWA 170
Cdd:COG5184      1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVRV---------PGLSNVVAVAAGGDHTCALKADGTVWC 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1207185434  171 WGSGC--QLGLVTNVfPVWKPQKVEHLVGryVVQIACGAFHSLAL 213
Cdd:COG5184     72 WGNNSygQLGDGTTT-DRTTPVKVPGLTG--VVAVAAGYYHSCAL 113
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 32-178 1.60e-19

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 91.96  E-value: 1.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434   32 SPEKLLLSRPVLHAALGSLHGLLLIEGGQVYSFGE----QPWKPVEPPPASLVLESTLSGqhVISVSAGSYHCSAVTEDG 107
Cdd:COG5184    191 TPVQVGGLSGVVAVAAGGDHSCALKSDGTVWCWGSnssgQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDG 268

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207185434  108 LVLMWGENSYGQCGVSGTDRVPSPTPVTVVDDETHppqlvrvlnVACGAQHTLALSNKHEVWAWGSGC--QLG 178
Cdd:COG5184    269 TVWCWGDNSYGQLGDGTTTDRSTPVKVPGLSGVVA---------VAAGSSHTCALLTDGTVWCWGDNAygQLG 332
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 530-631 1.53e-17

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 86.18  E-value: 1.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  530 VWSWGKGHEGQLGHGDYLPRLQPLCIKSLSKkeVVKITAGANHSLALTAQCQVYSWGSEKFGQLGR-----MNSPSTVPN 604
Cdd:COG5184     19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDgtttdRTTPVKVPG 96

                           90       100
                   ....*....|....*....|....*...
gi 1207185434  605 LTTVSdgirvwDVAAGQTHTL-LLADGD 631
Cdd:COG5184     97 LTGVV------AVAAGYYHSCaLKSDGT 118
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 529-633 1.87e-17

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 85.80  E-value: 1.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  529 EVWSWGKGHEGQLGHGDYLPRLQPLCIKSLSKkeVVKITAGANHSLALTAQCQVYSWGSEKFGQLGRMN-----SPSTVP 603
Cdd:COG5184    219 TVWCWGSNSSGQLGDGTTTDRATPVQVAGLTG--VVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDGTttdrsTPVKVP 296

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1207185434  604 NLTTVSdgirvwDVAAGQTHTL-LLADGDCY 633
Cdd:COG5184    297 GLSGVV------AVAAGSSHTCaLLTDGTVW 321
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 529-631 4.97e-17

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 84.64  E-value: 4.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  529 EVWSWGKGHEGQLGHGDYLPRLQPLCIKSLSkkEVVKITAGANHSLALTAQCQVYSWGSEKFGQLGR-----MNSPSTVP 603
Cdd:COG5184    169 TVWCWGANSYGQLGDGTTTDRPTPVQVGGLS--GVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDgtttdRATPVQVA 246

                           90       100
                   ....*....|....*....|....*....
gi 1207185434  604 NLTTVSdgirvwDVAAGQTHTL-LLADGD 631
Cdd:COG5184    247 GLTGVV------AIAAGGSHTCaLKSDGT 269
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 529-630 6.03e-17

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 84.26  E-value: 6.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  529 EVWSWGKGHEGQLGHGDYLPRLQPLCIKSLSkkEVVKITAGANHSLALTAQCQVYSWGSEKFGQLGR-MNSPSTVPnlTT 607
Cdd:COG5184     68 TVWCWGNNSYGQLGDGTTTDRTTPVKVPGLT--GVVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDgTTTNRLTP--VQ 143

                           90       100
                   ....*....|....*....|....*
gi 1207185434  608 VSDGIRVW-DVAAGQTHTL-LLADG 630
Cdd:COG5184    144 VDAGLSGVvAIAAGGYHTCaLKSDG 168
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 529-630 1.47e-16

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 83.10  E-value: 1.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  529 EVWSWGKGHEGQLGHGDYLPRLQPLCIkSLSKKEVVKITAGANHSLALTAQCQVYSWGSEKFGQLGRMNSPST-----VP 603
Cdd:COG5184    118 TVWCWGDNSSGQLGDGTTTNRLTPVQV-DAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRptpvqVG 196

                           90       100
                   ....*....|....*....|....*...
gi 1207185434  604 NLTTVSdgirvwDVAAGQTHTL-LLADG 630
Cdd:COG5184    197 GLSGVV------AVAAGGDHSCaLKSDG 218
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1071-1268 1.75e-14

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 79.11  E-value: 1.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1071 GNLKWPDGTMYCGTFKSGLEDGFGDFMTPSTTFnkferYQGHWKEGKMHGFGTFWYASGEVYEGSFRENMRHGHGMLRSg 1150
Cdd:PLN03185     1 GELVLSNGDFYSGSLLGNVPEGPGKYLWSDGCM-----YEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTG- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1151 kvaspSSSSVFVGQWVQGKRTGYGvCDDFSRGEKYMGIWHDDQRHGDGVVITQFGLYYEGNFCNNRMMGNGTLLCDDDTV 1230
Cdd:PLN03185    75 -----TDGTTYKGRWRLNLKHGLG-YQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDS 148

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1207185434 1231 FEGDFQDDwTLCGKGILFMPNGdsfdGVFDGHWGSGLR 1268
Cdd:PLN03185   149 YEGQWLDG-MMHGFGVYTWSDG----GCYVGTWTRGLK 181
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1056-1175 1.08e-13

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 76.41  E-value: 1.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1056 AKYEGRWLSGKPHGKG----------------NLK-------WPDGTMYCGTFKSGLEDGFGDFmtpstTFNKFERYQGH 1112
Cdd:PLN03185    55 ATYEGEFSGGYMHGSGtytgtdgttykgrwrlNLKhglgyqrYPNGDVFEGSWIQGLQEGPGKY-----TWANGNVYLGD 129

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207185434 1113 WKEGKMHGFGTFWYASGEVYEGSFRENMRHGHGmlrsgkVASPSSSSVFVGQWVQGKRTGYGV 1175
Cdd:PLN03185   130 MKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFG------VYTWSDGGCYVGTWTRGLKDGKGV 186
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
529-576 5.20e-13

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 64.85  E-value: 5.20e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207185434  529 EVWSWGKGHEGQLGHGDYLPRLQPLCIKSLSKKEVVKITAGANHSLAL 576
Cdd:pfam00415    3 RVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1107-1275 4.37e-12

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 71.02  E-value: 4.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1107 ERYQGHWKEGKMHGFGTFWYASGEVYEGSFRENMRHGHgmlrsGKVASPSSSSV---FVGQWVQGKRTGYGvcddfSRGE 1183
Cdd:PLN03185     9 DFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGN-----GKISWPSGATYegeFSGGYMHGSGTYTG-----TDGT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1184 KYMGIWHDDQRHGDGVVITQFGLYYEGNFCNNRMMGNGTLLCDDDTVFEGDFQDDwTLCGKGILFMPNGDSF-----DGV 1258
Cdd:PLN03185    79 TYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGG-KMSGKGTLTWVSGDSYegqwlDGM 157

                          170       180
                   ....*....|....*....|.
gi 1207185434 1259 FDGH----WGSGLRVAGTFTK 1275
Cdd:PLN03185   158 MHGFgvytWSDGGCYVGTWTR 178
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
167-213 1.44e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 1.44e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207185434  167 EVWAWGSG--CQLGLVTNVfPVWKPQKVEHLVGRYVVQIACGAFHSLAL 213
Cdd:pfam00415    3 RVYTWGRNdyGQLGLGTTE-NVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
PH_Phafin2-like cd01218
Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain; ...
 903-1013 2.37e-11

Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain; Phafin2 is differentially expressed in the liver cancer cell and regulates the structure and function of the endosomes through Rab5-dependent processes. Phafin2 modulates the cell's response to extracellular stimulation by modulating the receptor density on the cell surface. Phafin2 contains a PH domain and a FYVE 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: 269927 [Multi-domain]  Cd Length: 123  Bit Score: 62.66  E-value: 2.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434  903 GKNLEALRKPSRRLVCESSnkgLTLQNAGRFSASWFILFNDVLVHaqGSI-PSKKLFSSHYVYPLATLWVEPISDESLGL 981
Cdd:cd01218     17 GGSGQPLVKPGRVLVGEGV---LTKVCRKKPKPRQFFLFNDILVY--GSIvINKKKYNKQRIIPLEDVKIEDLEDTGELK 91

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1207185434  982 LGLKLTTPEDSFVVLATSPLEKGKWLRAINQA 1013
Cdd:cd01218     92 NGWQIISPKKSFVVYAATATEKSEWMDHINKC 123
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 564-630 5.80e-10

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 63.07  E-value: 5.80e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207185434  564 VKITAGANHSLALTAQCQVYSWGSEKFGQLGRM-----NSPSTVPNLTTVSdgirvwDVAAGQTHTL-LLADG 630
Cdd:COG5184      1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGDGtttdrSTPVRVPGLSNVV------AVAAGGDHTCaLKADG 67
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
106-162 1.07e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 55.60  E-value: 1.07e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207185434  106 DGLVLMWGENSYGQCGVSGTDRVPSPTPVTVVDDethppqlVRVLNVACGAQHTLAL 162
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSG-------NKVVQVACGGDHTVAL 50
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 30-132 1.65e-09

Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 444065 [Multi-domain]  Cd Length: 343  Bit Score: 61.53  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434   30 SVSPEKLLLSRPVLHAALGSLHGLLLIEGGQVYSFG------------EQPWKPVEPPPASlvlestlsgqHVISVSAGS 97
Cdd:COG5184    239 RATPVQVAGLTGVVAIAAGGSHTCALKSDGTVWCWGdnsygqlgdgttTDRSTPVKVPGLS----------GVVAVAAGS 308

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1207185434   98 YHCSAVTEDGLVLMWGENSYGQCGVSGTDRVPSPT 132
Cdd:COG5184    309 SHTCALLTDGTVWCWGDNAYGQLGDGTTTDRSTPV 343
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
90-119 8.68e-08

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 49.34  E-value: 8.68e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207185434   90 VISVSAGSYHCSAVTEDGLVLMWGENSYGQ 119
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
1046-1142 3.05e-07

Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 51.99  E-value: 3.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207185434 1046 TFSKEGRLKdakYEGRWLSGKPHGKGNLKWPDGTM-YCGTFKSGLEDGfgdfmtPSTTF--NKFERYQGHWKEGKMHGFG 1122
Cdd:COG2849     72 TYYPNGQLK---SEGTYKNGKLEGEWKEYYENGKLkSEGNYKNGKLHG------EWKEYyeNGKLKEEGNYKNGKKDGVW 142

                           90       100
                   ....*....|....*....|.
gi 1207185434 1123 TFWYASGE-VYEGSFRENMRH 1142
Cdd:COG2849    143 KYYDENGKlVKEEEYKNGKKV 163
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1057-1103 6.73e-07

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 54.45  E-value: 6.73e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1207185434 1057 KYEGRWLSGKPHGKGNLKWPDGTMYCGTFKSGLEDGFGDFMTPSTTF 1103
Cdd:PLN03185   148 SYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVFYPAGSRV 194
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
563-592 2.15e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 45.49  E-value: 2.15e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207185434  563 VVKITAGANHSLALTAQCQVYSWGSEKFGQ 592
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
581-627 6.46e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 44.82  E-value: 6.46e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1207185434  581 QVYSWGSEKFGQLGRMN-SPSTVPNLTTVSDGIRVWDVAAGQTHTLLL 627
Cdd:pfam00415    3 RVYTWGRNDYGQLGLGTtENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
1108-1127 7.79e-06

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 43.87  E-value: 7.79e-06
                            10        20
                    ....*....|....*....|
gi 1207185434  1108 RYQGHWKEGKMHGFGTFWYA 1127
Cdd:smart00698    2 RYEGEWRNGKRHGRGVYTYA 21
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 1109-1131 1.64e-05

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 42.78  E-value: 1.64e-05
                           10        20
                   ....*....|....*....|...
gi 1207185434 1109 YQGHWKEGKMHGFGTFWYASGEV 1131
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
PH1_FARP1-like cd01220
FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin ...
 938-1015 1.33e-04

FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin Homology (PH) domain, repeat 1; Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FARP6 (also called Zinc finger FYVE domain-containing protein 24). They are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. Little is known about FARP1 and FARP6, though FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. FARP1 and FARP2 are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. FARP6 is composed of Dbl-homology (DH), and two C-terminal PH domains separated by a FYVE domain. This hierarchy contains the first PH repeat. 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: 269928  Cd Length: 109  Bit Score: 42.69  E-value: 1.33e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207185434  938 FILFNDVLVHAQGSIPSKKLFSSHYVYPLATLWVEPISDESLGLLGLKLTTPEDSFVVLATSPLEKGKWLRAINQAID 1015
Cdd:cd01220     27 FFLFSDVLLYTSRSPTPSLQFKVHGQLPLRGLMVEESEPEWGVAHCFTIYGGNRALTVAASSEEEKERWLEDLQRAID 104
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 1058-1080 3.59e-04

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 39.31  E-value: 3.59e-04
                           10        20
                   ....*....|....*....|...
gi 1207185434 1058 YEGRWLSGKPHGKGNLKWPDGTM 1080
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
149-173 5.13e-04

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 38.94  E-value: 5.13e-04
                           10        20
                   ....*....|....*....|....*
gi 1207185434  149 VLNVACGAQHTLALSNKHEVWAWGS 173
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGD 25
PH1_FGD5_FGD6 cd13389
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal ...
 938-1016 5.23e-04

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal Pleckstrin Homology (PH) domain; FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH 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: 275424  Cd Length: 124  Bit Score: 41.49  E-value: 5.23e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207185434  938 FILFNDVLVHAQgSIPSKKLFSSHYVYPLATLWVEPISDESLGLLGLKLTTpEDSFVVLATSPLEKGKWLRAINQAIDE 1016
Cdd:cd13389     33 FFLFNDCLLYTT-PVQSSGMLKLNNELPLSGMKVKLPEDEEYSNEFQIIST-KRSFTLIASSEEERDEWVKALSRAIEE 109
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 1604-1656 3.74e-03

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


Pssm-ID: 128469  Cd Length: 117  Bit Score: 38.98  E-value: 3.74e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1207185434  1604 DDLFPIFLYVVLRARIRNLGSEVSLIEDLTDSNLQLGQLGFMLTTLKACYNQI 1656
Cdd:smart00167   47 DDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSLLTGEGGYYLTSLSAALALI 99
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
1056-1077 8.18e-03

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 35.39  E-value: 8.18e-03
                            10        20
                    ....*....|....*....|..
gi 1207185434  1056 AKYEGRWLSGKPHGKGNLKWPD 1077
Cdd:smart00698    1 DRYEGEWRNGKRHGRGVYTYAN 22
 
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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