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Conserved domains on  [gi|237757295|ref|NP_082993|]
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alsin isoform 1 [Mus musculus]

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 ...
 899-1004 5.45e-63

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: 209.56  E-value: 5.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  899 DSLRKPERRLLCESSNRALSLQHAGRFSVNWFILFNDALVHAQFSTHHVFPLATLWAEPLSEEAGSVNGLKITTPEEQFT 978
Cdd:cd13269     1 DSLRSPDRRLIRESSTRPLTLQNAGRFSSHWFILFNDALVHAQFSTHHIFPLATLWVEPIPDEDSGQNALKITTPEESFT 80

                          90       100
                  ....*....|....*....|....*.
gi 237757295  979 LISSTPQEKTKWLRAISQAVDQALRG 1004
Cdd:cd13269    81 LVASTPQEKAEWLRAINQAIDQALNG 106
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1012-1243 8.17e-35

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 135.08  E-value: 8.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1012 GGGSSVQRQEPPISRSAKYTFYKDTRLkdaTYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNkalnkE 1091
Cdd:COG4642    76 GGGGGGGGGKGDGGDGGGGEGGFGGGG---GGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPN-----G 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1092 DHYVGHWKEGKMCGQGVYSYASGEVFEGCFQDNMRHGHGllrsgKLTSSSPSMFIGQWVMDKKAGYGVFdditrgekymg 1171
Cdd:COG4642   148 DVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQG-----TLTYANGDVYEGEFKNGQRHGQGTY----------- 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237757295 1172 MWQDdvcqgngvvvtqfGLYYEGNFHLNKMMGNGVLLSEDDTIYEGEFSDDWtLSGKGTLTMPHGDYIEGYF 1243
Cdd:COG4642   212 TYAD-------------GDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGK-RHGQGTMTYADGSVYEGEW 269
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 1546-1650 9.31e-30

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: 114.23  E-value: 9.31e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  1546 FASAVECLQQISTTFTPSDKLKVIQQTFEEISQSVlASLQEDFLWSMDDLFPVFLYVVLRARIRNLGSEVHLIEDLMDPF 1625
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEAL-SKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPD 79

                           90       100
                   ....*....|....*....|....*
gi 237757295  1626 LQHGEQGIMFTTLKACYFQIQREKL 1650
Cdd:pfam02204   80 LLSGEEGYYLTTLEAALEFIESLDP 104
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 18-219 2.20e-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: 112.38  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   18 GLVHVW------QAGSFSLTPERLP---GWGGKTVLQAALGVRHGVLLTEDGEVYSFGTLPWKSESAEICPSSPLLESAL 88
Cdd:COG5184   117 GTVWCWgdnssgQLGDGTTTNRLTPvqvDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVG 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   89 VGHHVITVATGSFHSGAVTESGVVYMWGENAAGQCAVANQQYVPEPSPVsisdsetspSLAVRILQLACGEEHTLALSLS 168
Cdd:COG5184   197 GLSGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQV---------AGLTGVVAIAAGGSHTCALKSD 267

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 237757295  169 REIWAWG--TGCQLGLITTTfPVTKPQKVEHLAGrvVLQVACGAFHSLAL-----VQC 219
Cdd:COG5184   268 GTVWCWGdnSYGQLGDGTTT-DRSTPVKVPGLSG--VVAVAAGSSHTCALltdgtVWC 322
ATS1 super family cl34932
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 521-622 1.04e-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: 86.57  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  521 EVWTWGKGKEGQLGHGDVLPRLQPlcVKCLDGKEVIHLEAGGSHSLALTAKSQVYSWGSNTFGQLGHSefpTTVPRLS-- 598
Cdd:COG5184   219 TVWCWGSNSSGQLGDGTTTDRATP--VQVAGLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDG---TTTDRSTpv 293

                          90       100
                  ....*....|....*....|....
gi 237757295  599 KVSSENGVWSVAAGQDYSLFLVDT 622
Cdd:COG5184   294 KVPGLSGVVAVAAGSSHTCALLTD 317
RhoGEF super family cl02571
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 689-873 2.37e-05

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


The actual alignment was detected with superfamily member cd00160:

Pssm-ID: 470622 [Multi-domain]  Cd Length: 181  Bit Score: 46.91  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  689 LHELASTERRFYSKLSEIKSQILRPLLSLENLGTVTTVQLLqevasrFSKLCYLIGQHgaslSSYLQGMKEASSL----- 763
Cdd:cd00160     5 IKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVELL------FGNIEEIYEFH----RIFLKSLEERVEEwdksg 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  764 -----VIMKHSSLFlDSYTEYCTSVSNFLvmggfQLLAKpaidfLNKNQELLQDLSEVNDENTQLMEiLNMLFFLPIRRL 838
Cdd:cd00160    75 prigdVFLKLAPFF-KIYSEYCSNHPDAL-----ELLKK-----LKKFNKFFQEFLEKAESECGRLK-LESLLLKPVQRL 142

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 237757295  839 HNYaKVLLK-LATCFEVTSPEYQKLQDSSSCYESLA 873
Cdd:cd00160   143 TKY-PLLLKeLLKHTPDGHEDREDLKKALEAIKEVA 177
 
Name Accession Description Interval E-value
PH_alsin cd13269
Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...
 899-1004 5.45e-63

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: 209.56  E-value: 5.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  899 DSLRKPERRLLCESSNRALSLQHAGRFSVNWFILFNDALVHAQFSTHHVFPLATLWAEPLSEEAGSVNGLKITTPEEQFT 978
Cdd:cd13269     1 DSLRSPDRRLIRESSTRPLTLQNAGRFSSHWFILFNDALVHAQFSTHHIFPLATLWVEPIPDEDSGQNALKITTPEESFT 80

                          90       100
                  ....*....|....*....|....*.
gi 237757295  979 LISSTPQEKTKWLRAISQAVDQALRG 1004
Cdd:cd13269    81 LVASTPQEKAEWLRAINQAIDQALNG 106
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1012-1243 8.17e-35

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 135.08  E-value: 8.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1012 GGGSSVQRQEPPISRSAKYTFYKDTRLkdaTYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNkalnkE 1091
Cdd:COG4642    76 GGGGGGGGGKGDGGDGGGGEGGFGGGG---GGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPN-----G 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1092 DHYVGHWKEGKMCGQGVYSYASGEVFEGCFQDNMRHGHGllrsgKLTSSSPSMFIGQWVMDKKAGYGVFdditrgekymg 1171
Cdd:COG4642   148 DVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQG-----TLTYANGDVYEGEFKNGQRHGQGTY----------- 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237757295 1172 MWQDdvcqgngvvvtqfGLYYEGNFHLNKMMGNGVLLSEDDTIYEGEFSDDWtLSGKGTLTMPHGDYIEGYF 1243
Cdd:COG4642   212 TYAD-------------GDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGK-RHGQGTMTYADGSVYEGEW 269
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 1546-1650 9.31e-30

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: 114.23  E-value: 9.31e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  1546 FASAVECLQQISTTFTPSDKLKVIQQTFEEISQSVlASLQEDFLWSMDDLFPVFLYVVLRARIRNLGSEVHLIEDLMDPF 1625
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEAL-SKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPD 79

                           90       100
                   ....*....|....*....|....*
gi 237757295  1626 LQHGEQGIMFTTLKACYFQIQREKL 1650
Cdd:pfam02204   80 LLSGEEGYYLTTLEAALEFIESLDP 104
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 18-219 2.20e-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: 112.38  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   18 GLVHVW------QAGSFSLTPERLP---GWGGKTVLQAALGVRHGVLLTEDGEVYSFGTLPWKSESAEICPSSPLLESAL 88
Cdd:COG5184   117 GTVWCWgdnssgQLGDGTTTNRLTPvqvDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVG 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   89 VGHHVITVATGSFHSGAVTESGVVYMWGENAAGQCAVANQQYVPEPSPVsisdsetspSLAVRILQLACGEEHTLALSLS 168
Cdd:COG5184   197 GLSGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQV---------AGLTGVVAIAAGGSHTCALKSD 267

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 237757295  169 REIWAWG--TGCQLGLITTTfPVTKPQKVEHLAGrvVLQVACGAFHSLAL-----VQC 219
Cdd:COG5184   268 GTVWCWGdnSYGQLGDGTTT-DRSTPVKVPGLSG--VVAVAAGSSHTCALltdgtVWC 322
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1042-1160 4.09e-19

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 94.13  E-value: 4.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1042 TYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKalnkeDHYVGHWKEGKMCGQGVYSYASGEVFEGCF 1121
Cdd:PLN03185   79 TYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANG-----NVYLGDMKGGKMSGKGTLTWVSGDSYEGQW 153

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 237757295 1122 QDNMRHGHGLlrsgkLTSSSPSMFIGQWVMDKKAGYGVF 1160
Cdd:PLN03185  154 LDGMMHGFGV-----YTWSDGGCYVGTWTRGLKDGKGVF 187
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 521-622 1.04e-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: 86.57  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  521 EVWTWGKGKEGQLGHGDVLPRLQPlcVKCLDGKEVIHLEAGGSHSLALTAKSQVYSWGSNTFGQLGHSefpTTVPRLS-- 598
Cdd:COG5184   219 TVWCWGSNSSGQLGDGTTTDRATP--VQVAGLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDG---TTTDRSTpv 293

                          90       100
                  ....*....|....*....|....
gi 237757295  599 KVSSENGVWSVAAGQDYSLFLVDT 622
Cdd:COG5184   294 KVPGLSGVVAVAAGSSHTCALLTD 317
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
521-568 1.38e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 1.38e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 237757295   521 EVWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGKEVIHLEAGGSHSLAL 568
Cdd:pfam00415    3 RVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
170-216 8.41e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 52.90  E-value: 8.41e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 237757295   170 EIWAWG--TGCQLGLiTTTFPVTKPQKVEHLAGRVVLQVACGAFHSLAL 216
Cdd:pfam00415    3 RVYTWGrnDYGQLGL-GTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 1561-1640 4.00e-07

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 50.15  E-value: 4.00e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   1561 TPSDKLKVIQQTFEEISQSVlaSLQEDFLWSMDDLFPVFLYVVLRARIRNLGSEVHLIEDLMDPFLQHGEQGIMFTTLKA 1640
Cdd:smart00167   17 SPSDKIKCLLRACKLIYTLL--ETQSGEVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSLLTGEGGYYLTSLSA 94
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 689-873 2.37e-05

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 46.91  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  689 LHELASTERRFYSKLSEIKSQILRPLLSLENLGTVTTVQLLqevasrFSKLCYLIGQHgaslSSYLQGMKEASSL----- 763
Cdd:cd00160     5 IKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVELL------FGNIEEIYEFH----RIFLKSLEERVEEwdksg 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  764 -----VIMKHSSLFlDSYTEYCTSVSNFLvmggfQLLAKpaidfLNKNQELLQDLSEVNDENTQLMEiLNMLFFLPIRRL 838
Cdd:cd00160    75 prigdVFLKLAPFF-KIYSEYCSNHPDAL-----ELLKK-----LKKFNKFFQEFLEKAESECGRLK-LESLLLKPVQRL 142

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 237757295  839 HNYaKVLLK-LATCFEVTSPEYQKLQDSSSCYESLA 873
Cdd:cd00160   143 TKY-PLLLKeLLKHTPDGHEDREDLKKALEAIKEVA 177
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 1094-1116 8.27e-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: 40.85  E-value: 8.27e-05
                           10        20
                   ....*....|....*....|...
gi 237757295  1094 YVGHWKEGKMCGQGVYSYASGEV 1116
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
1092-1112 1.52e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 40.02  E-value: 1.52e-04
                            10        20
                    ....*....|....*....|.
gi 237757295   1092 DHYVGHWKEGKMCGQGVYSYA 1112
Cdd:smart00698    1 DRYEGEWRNGKRHGRGVYTYA 21
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 689-873 1.89e-04

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 44.21  E-value: 1.89e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295    689 LHELASTERRFYSKLSEIKSQILRPLLSLENLGTVTTVQLLqevasrFSKLCYLIGQHgaslSSYLQGMKEASSL----- 763
Cdd:smart00325    2 LKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNELETL------FGNIEEIYEFH----RDFLDELEERIEEwddsv 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295    764 -----VIMKHSSLFlDSYTEYCTSVSNFLvmggfQLLAKpaidfLNKNQELLQDLSEV-NDENTQLMEiLNMLFFLPIRR 837
Cdd:smart00325   72 erigdVFLKLEEFF-KIYSEYCSNHPDAL-----ELLKK-----LKKNPRFQKFLKEIeSSPQCRRLT-LESLLLKPVQR 139

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 237757295    838 LHNYaKVLLK-LATCFEVTSPEYQKLQDSSSCYESLA 873
Cdd:smart00325  140 LTKY-PLLLKeLLKHTPEDHEDREDLKKALKAIKELA 175
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 929-999 2.94e-03

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: 38.68  E-value: 2.94e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295    929 WFILFNDALV-------HAQFSTHHVFPLATL-WAEPLSEEAGSV-NGLKITTPEEQ-FTLISSTPQEKTKWLRAISQAV 998
Cdd:smart00233   22 YFVLFNSTLLyykskkdKKSYKPKGSIDLSGCtVREAPDPDSSKKpHCFEIKTSDRKtLLLQAESEEEREKWVEALRKAI 101


                    .
gi 237757295    999 D 999
Cdd:smart00233  102 A 102
 
Name Accession Description Interval E-value
PH_alsin cd13269
Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...
 899-1004 5.45e-63

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: 209.56  E-value: 5.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  899 DSLRKPERRLLCESSNRALSLQHAGRFSVNWFILFNDALVHAQFSTHHVFPLATLWAEPLSEEAGSVNGLKITTPEEQFT 978
Cdd:cd13269     1 DSLRSPDRRLIRESSTRPLTLQNAGRFSSHWFILFNDALVHAQFSTHHIFPLATLWVEPIPDEDSGQNALKITTPEESFT 80

                          90       100
                  ....*....|....*....|....*.
gi 237757295  979 LISSTPQEKTKWLRAISQAVDQALRG 1004
Cdd:cd13269    81 LVASTPQEKAEWLRAINQAIDQALNG 106
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1012-1243 8.17e-35

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 135.08  E-value: 8.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1012 GGGSSVQRQEPPISRSAKYTFYKDTRLkdaTYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNkalnkE 1091
Cdd:COG4642    76 GGGGGGGGGKGDGGDGGGGEGGFGGGG---GGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPN-----G 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1092 DHYVGHWKEGKMCGQGVYSYASGEVFEGCFQDNMRHGHGllrsgKLTSSSPSMFIGQWVMDKKAGYGVFdditrgekymg 1171
Cdd:COG4642   148 DVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQG-----TLTYANGDVYEGEFKNGQRHGQGTY----------- 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237757295 1172 MWQDdvcqgngvvvtqfGLYYEGNFHLNKMMGNGVLLSEDDTIYEGEFSDDWtLSGKGTLTMPHGDYIEGYF 1243
Cdd:COG4642   212 TYAD-------------GDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGK-RHGQGTMTYADGSVYEGEW 269
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1011-1175 2.88e-32

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 127.77  E-value: 2.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1011 YGGGSSVQRQEPPISRSAKYTFYKDTRLKDATYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKalnk 1090
Cdd:COG4642   118 VLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANG---- 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1091 eDHYVGHWKEGKMCGQGVYSYASGEVFEGCFQDNMRHGHgllrsGKLTSSSPSMFIGQWVMDKKAGYGVFDDITrGEKYM 1170
Cdd:COG4642   194 -DVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQ-----GTLTYADGDRYEGEFKNGKRHGQGTMTYAD-GSVYE 266


                  ....*
gi 237757295 1171 GMWQD 1175
Cdd:COG4642   267 GEWKN 271
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 1546-1650 9.31e-30

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: 114.23  E-value: 9.31e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  1546 FASAVECLQQISTTFTPSDKLKVIQQTFEEISQSVlASLQEDFLWSMDDLFPVFLYVVLRARIRNLGSEVHLIEDLMDPF 1625
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEAL-SKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPD 79

                           90       100
                   ....*....|....*....|....*
gi 237757295  1626 LQHGEQGIMFTTLKACYFQIQREKL 1650
Cdd:pfam02204   80 LLSGEEGYYLTTLEAALEFIESLDP 104
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 18-219 2.20e-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: 112.38  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   18 GLVHVW------QAGSFSLTPERLP---GWGGKTVLQAALGVRHGVLLTEDGEVYSFGTLPWKSESAEICPSSPLLESAL 88
Cdd:COG5184   117 GTVWCWgdnssgQLGDGTTTNRLTPvqvDAGLSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVG 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   89 VGHHVITVATGSFHSGAVTESGVVYMWGENAAGQCAVANQQYVPEPSPVsisdsetspSLAVRILQLACGEEHTLALSLS 168
Cdd:COG5184   197 GLSGVVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGDGTTTDRATPVQV---------AGLTGVVAIAAGGSHTCALKSD 267

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 237757295  169 REIWAWG--TGCQLGLITTTfPVTKPQKVEHLAGrvVLQVACGAFHSLAL-----VQC 219
Cdd:COG5184   268 GTVWCWGdnSYGQLGDGTTT-DRSTPVKVPGLSG--VVAVAAGSSHTCALltdgtVWC 322
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 15-216 1.61e-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: 109.68  E-value: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   15 KERGLVHVW------QAG----SFSLTPERLPGwgGKTVLQAALGVRHGVLLTEDGEVY-----SFGTLPWKSESAEicp 79
Cdd:COG5184    14 KSDGTVWCWgdnsygQLGdgttTDRSTPVRVPG--LSNVVAVAAGGDHTCALKADGTVWcwgnnSYGQLGDGTTTDR--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   80 SSPLLESALVGhhVITVATGSFHSGAVTESGVVYMWGENAAGQcaVANQQYVPEPSPVSISDSETSpslavrILQLACGE 159
Cdd:COG5184    89 TTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQ--LGDGTTTNRLTPVQVDAGLSG------VVAIAAGG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 237757295  160 EHTLALSLSREIWAWG--TGCQLGLITTTfPVTKPQKVEHLAGrvVLQVACGAFHSLAL 216
Cdd:COG5184   159 YHTCALKSDGTVWCWGanSYGQLGDGTTT-DRPTPVQVGGLSG--VVAVAAGGDHSCAL 214
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 94-216 7.24e-20

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: 93.12  E-value: 7.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   94 ITVATGSFHSGAVTESGVVYMWGENAAGQcaVANQQYVPEPSPVSISDSETspslavrILQLACGEEHTLALSLSREIWA 173
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQ--LGDGTTTDRSTPVRVPGLSN-------VVAVAAGGDHTCALKADGTVWC 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 237757295  174 WGTGC--QLGLITTTFPVTkPQKVEHLAGrvVLQVACGAFHSLAL 216
Cdd:COG5184    72 WGNNSygQLGDGTTTDRTT-PVKVPGLTG--VVAVAAGYYHSCAL 113
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1042-1160 4.09e-19

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 94.13  E-value: 4.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1042 TYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKalnkeDHYVGHWKEGKMCGQGVYSYASGEVFEGCF 1121
Cdd:PLN03185   79 TYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANG-----NVYLGDMKGGKMSGKGTLTWVSGDSYEGQW 153

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 237757295 1122 QDNMRHGHGLlrsgkLTSSSPSMFIGQWVMDKKAGYGVF 1160
Cdd:PLN03185  154 LDGMMHGFGV-----YTWSDGGCYVGTWTRGLKDGKGVF 187
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1042-1196 5.47e-19

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 93.74  E-value: 5.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1042 TYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKALnkedhYVGHWKEGKMCGQGVYSYASGEVFEGCF 1121
Cdd:PLN03185   33 MYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTT-----YKGRWRLNLKHGLGYQRYPNGDVFEGSW 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 237757295 1122 QDNMRHGHgllrsGKLTSSSPSMFIGQWVMDKKAGYGVFdDITRGEKYMGMWQDDVCQGNGVVVTQFGLYYEGNF 1196
Cdd:PLN03185  108 IQGLQEGP-----GKYTWANGNVYLGDMKGGKMSGKGTL-TWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTW 176
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 29-186 4.46e-18

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: 87.72  E-value: 4.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   29 SLTPERLPGWGGktVLQAALGVRHGVLLTEDGEVYSFGTlpwkSESAEICPSSPLLESALV----GHHVITVATGSFHSG 104
Cdd:COG5184   189 RPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGS----NSSGQLGDGTTTDRATPVqvagLTGVVAIAAGGSHTC 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  105 AVTESGVVYMWGENAAGQCAVANQQYVPEPSPVsisdsetsPSLAvRILQLACGEEHTLALSLSREIWAWGTGC--QLGL 182
Cdd:COG5184   263 ALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKV--------PGLS-GVVAVAAGSSHTCALLTDGTVWCWGDNAygQLGD 333


                  ....
gi 237757295  183 ITTT 186
Cdd:COG5184   334 GTTT 337
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 521-622 1.04e-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: 86.57  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  521 EVWTWGKGKEGQLGHGDVLPRLQPlcVKCLDGKEVIHLEAGGSHSLALTAKSQVYSWGSNTFGQLGHSefpTTVPRLS-- 598
Cdd:COG5184   219 TVWCWGSNSSGQLGDGTTTDRATP--VQVAGLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDG---TTTDRSTpv 293

                          90       100
                  ....*....|....*....|....
gi 237757295  599 KVSSENGVWSVAAGQDYSLFLVDT 622
Cdd:COG5184   294 KVPGLSGVVAVAAGSSHTCALLTD 317
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 522-622 1.51e-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: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  522 VWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGkeVIHLEAGGSHSLALTAKSQVYSWGSNTFGQLGHSEF-----PTTVPR 596
Cdd:COG5184    19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTtdrttPVKVPG 96

                          90       100
                  ....*....|....*....|....*.
gi 237757295  597 LSKVSsengvwSVAAGQDYSLFLVDT 622
Cdd:COG5184    97 LTGVV------AVAAGYYHSCALKSD 116
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 521-619 1.89e-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: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  521 EVWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGkeVIHLEAGGSHSLALTAKSQVYSWGSNTFGQLGHsefPTTVPRLS-- 598
Cdd:COG5184   169 TVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGSNSSGQLGD---GTTTDRATpv 243

                          90       100
                  ....*....|....*....|.
gi 237757295  599 KVSSENGVWSVAAGQDYSLFL 619
Cdd:COG5184   244 QVAGLTGVVAIAAGGSHTCAL 264
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1056-1410 3.09e-17

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 87.97  E-value: 3.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1056 GVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKALnkedhYVGHWKEGKMCGQGVYSYASGEVFEGCFQDNMRHGhgllrSG 1135
Cdd:PLN03185    1 GELVLSNGDFYSGSLLGNVPEGPGKYLWSDGCM-----YEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHG-----SG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1136 KLTSSSPSMFIGQWVMDKKAGYGvFDDITRGEKYMGMWQDDVCQGNGVVVTQFGLYYEGNFHLNKMMGNGVLLSEDDTIY 1215
Cdd:PLN03185   71 TYTGTDGTTYKGRWRLNLKHGLG-YQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1216 EGEFSDDwTLSGKGTLTMPHGdyieGYFSGEWGSGIkitgtyfkpslyesdKDKPKAFRKLGNLAVAADEKWRAVFEECW 1295
Cdd:PLN03185  150 EGQWLDG-MMHGFGVYTWSDG----GCYVGTWTRGL---------------KDGKGVFYPAGSRVPAVQEFYLNALRKRG 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1296 RQLGCESPGQGEVWKAWDNIAVALTTNRR-QHKDSPEILSRSQTQTLE-------SLEYIPQHIGAFSVEKYDDIKKYLI 1367
Cdd:PLN03185  210 VLPDLRRQNQVLSSHNSEQLSRGVSSDKLsKGSLLPLEQSRNRNVSLErrwslevSIEKVIGHDYSGSSSAVLDEGSEVE 289

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 237757295 1368 KACDTPL----HPLGRLVETLVAVYRMTYVGVGANRRlLQEAVKEIK 1410
Cdd:PLN03185  290 YKANRPIlereYMQGVLISELVLNNSFSSTSRRAKRR-QKKLVKEIK 335
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 521-619 5.76e-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: 5.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  521 EVWTWGKGKEGQLGHGDVLPRLQPlcVKCLDG-KEVIHLEAGGSHSLALTAKSQVYSWGSNTFGQLGHSefpTTVPRLS- 598
Cdd:COG5184   118 TVWCWGDNSSGQLGDGTTTNRLTP--VQVDAGlSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDG---TTTDRPTp 192

                          90       100
                  ....*....|....*....|..
gi 237757295  599 -KVSSENGVWSVAAGQDYSLFL 619
Cdd:COG5184   193 vQVGGLSGVVAVAAGGDHSCAL 214
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 521-619 1.85e-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: 82.72  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  521 EVWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGkeVIHLEAGGSHSLALTAKSQVYSWGSNTFGQLG-----HSEFPTTV- 594
Cdd:COG5184    68 TVWCWGNNSYGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGdgtttNRLTPVQVd 145

                          90       100
                  ....*....|....*....|....*
gi 237757295  595 PRLSKVSsengvwSVAAGQDYSLFL 619
Cdd:COG5184   146 AGLSGVV------AIAAGGYHTCAL 164
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
521-568 1.38e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 1.38e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 237757295   521 EVWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGKEVIHLEAGGSHSLAL 568
Cdd:pfam00415    3 RVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
PH_Phafin2-like cd01218
Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain; ...
 929-997 7.57e-10

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: 58.42  E-value: 7.57e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237757295  929 WFILFNDALVHA-------QFSTHHVFPLATLWAEPLSEEAGSVNGLKITTPEEQFTLISSTPQEKTKWLRAISQA 997
Cdd:cd01218    48 QFFLFNDILVYGsivinkkKYNKQRIIPLEDVKIEDLEDTGELKNGWQIISPKKSFVVYAATATEKSEWMDHINKC 123
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 556-619 1.17e-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: 61.92  E-value: 1.17e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 237757295  556 IHLEAGGSHSLALTAKSQVYSWGSNTFGQLG-----HSEFPTTVPRLSKVSsengvwSVAAGQDYSLFL 619
Cdd:COG5184     1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGdgtttDRSTPVRVPGLSNVV------AVAAGGDHTCAL 63
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
573-619 6.52e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 53.29  E-value: 6.52e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 237757295   573 QVYSWGSNTFGQLGH-SEFPTTVPRLSKVSSENGVWSVAAGQDYSLFL 619
Cdd:pfam00415    3 RVYTWGRNDYGQLGLgTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
170-216 8.41e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 52.90  E-value: 8.41e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 237757295   170 EIWAWG--TGCQLGLiTTTFPVTKPQKVEHLAGRVVLQVACGAFHSLAL 216
Cdd:pfam00415    3 RVYTWGrnDYGQLGL-GTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
PH1_FGD5_FGD6 cd13389
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal ...
 930-998 5.51e-08

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: 53.04  E-value: 5.51e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237757295  930 FILFNDALVHA-------QFSTHHVFPLATLWAEPLSEEAGSvNGLKITTPEEQFTLISSTPQEKTKWLRAISQAV 998
Cdd:cd13389    33 FFLFNDCLLYTtpvqssgMLKLNNELPLSGMKVKLPEDEEYS-NEFQIISTKRSFTLIASSEEERDEWVKALSRAI 107
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
555-584 3.86e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 47.80  E-value: 3.86e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 237757295   555 VIHLEAGGSHSLALTAKSQVYSWGSNTFGQ 584
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 1561-1640 4.00e-07

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 50.15  E-value: 4.00e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295   1561 TPSDKLKVIQQTFEEISQSVlaSLQEDFLWSMDDLFPVFLYVVLRARIRNLGSEVHLIEDLMDPFLQHGEQGIMFTTLKA 1640
Cdd:smart00167   17 SPSDKIKCLLRACKLIYTLL--ETQSGEVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSLLTGEGGYYLTSLSA 94
PH1_FARP1-like cd01220
FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin ...
 930-1001 8.13e-07

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: 49.24  E-value: 8.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  930 FILFNDALVHA--------QFSTHHVFPLATLWAEPLSEEAGSVNGLKITTPEEQFTLISSTPQEKTKWLRAISQAVDQA 1001
Cdd:cd01220    27 FFLFSDVLLYTsrsptpslQFKVHGQLPLRGLMVEESEPEWGVAHCFTIYGGNRALTVAASSEEEKERWLEDLQRAIDAA 106
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
109-165 2.52e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 45.97  E-value: 2.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 237757295   109 SGVVYMWGENAAGQCAVANQQYVPEPSPVSISDSetspslaVRILQLACGEEHTLAL 165
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEGLSG-------NKVVQVACGGDHTVAL 50
PH1_FGD6 cd15793
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 6, N-terminal Pleckstrin ...
 930-1000 4.43e-06

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 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: 275436  Cd Length: 123  Bit Score: 47.72  E-value: 4.43e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237757295  930 FILFNDALVH------AQFSTHHVFPLATLWAEPLSEEAGSvNGLKITTPEEQFTLISSTPQEKTKWLRAISQAVDQ 1000
Cdd:cd15793    33 FFLFNDALLYttpvqsGMYKLNNMLSLAGMKVSKPSQEAYQ-NELNIESVERSFILSASSATERDEWLEAISRAIEE 108
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
93-122 9.22e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 43.57  E-value: 9.22e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 237757295    93 VITVATGSFHSGAVTESGVVYMWGENAAGQ 122
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
 929-1008 1.51e-05

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. 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: 270095  Cd Length: 106  Bit Score: 45.39  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  929 WFILFNDAL------VHAQFST-HHVFPLAT-LWAEPLSEEAGSVNGLKITTPEEQFTLISSTPQEKTKWLRAISQAVDQ 1000
Cdd:cd13276    19 WFVLKQGKLfwfkepDVTPYSKpRGVIDLSKcLTVKSAEDATNKENAFELSTPEETFYFIADNEKEKEEWIGAIGRAIVK 98


                  ....*...
gi 237757295 1001 ALRGTSDF 1008
Cdd:cd13276    99 HSRSVTDD 106
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
1029-1139 1.66e-05

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


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 46.99  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295 1029 KYTFYKDTRLKDATYDGRWLSGKPHGRGVLKW--PDGKMYS-GMFRNGLEDGYGEYRIPNKALNKEdhyvGHWKEGKMCG 1105
Cdd:COG2849    41 EDSYNEGGKLIKKKLGKGLGKYKKGKLGEWKTyyPNGQLKSeGTYKNGKLEGEWKEYYENGKLKSE----GNYKNGKLHG 116

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 237757295 1106 QGVYSYASGEVF-EGCFQDNMRHGHGLL--RSGKLTS 1139
Cdd:COG2849   117 EWKEYYENGKLKeEGNYKNGKKDGVWKYydENGKLVK 153
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 689-873 2.37e-05

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 46.91  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  689 LHELASTERRFYSKLSEIKSQILRPLLSLENLGTVTTVQLLqevasrFSKLCYLIGQHgaslSSYLQGMKEASSL----- 763
Cdd:cd00160     5 IKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVELL------FGNIEEIYEFH----RIFLKSLEERVEEwdksg 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295  764 -----VIMKHSSLFlDSYTEYCTSVSNFLvmggfQLLAKpaidfLNKNQELLQDLSEVNDENTQLMEiLNMLFFLPIRRL 838
Cdd:cd00160    75 prigdVFLKLAPFF-KIYSEYCSNHPDAL-----ELLKK-----LKKFNKFFQEFLEKAESECGRLK-LESLLLKPVQRL 142

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 237757295  839 HNYaKVLLK-LATCFEVTSPEYQKLQDSSSCYESLA 873
Cdd:cd00160   143 TKY-PLLLKeLLKHTPDGHEDREDLKKALEAIKEVA 177
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 1094-1116 8.27e-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: 40.85  E-value: 8.27e-05
                           10        20
                   ....*....|....*....|...
gi 237757295  1094 YVGHWKEGKMCGQGVYSYASGEV 1116
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
1092-1112 1.52e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 40.02  E-value: 1.52e-04
                            10        20
                    ....*....|....*....|.
gi 237757295   1092 DHYVGHWKEGKMCGQGVYSYA 1112
Cdd:smart00698    1 DRYEGEWRNGKRHGRGVYTYA 21
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 689-873 1.89e-04

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 44.21  E-value: 1.89e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295    689 LHELASTERRFYSKLSEIKSQILRPLLSLENLGTVTTVQLLqevasrFSKLCYLIGQHgaslSSYLQGMKEASSL----- 763
Cdd:smart00325    2 LKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNELETL------FGNIEEIYEFH----RDFLDELEERIEEwddsv 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295    764 -----VIMKHSSLFlDSYTEYCTSVSNFLvmggfQLLAKpaidfLNKNQELLQDLSEV-NDENTQLMEiLNMLFFLPIRR 837
Cdd:smart00325   72 erigdVFLKLEEFF-KIYSEYCSNHPDAL-----ELLKK-----LKKNPRFQKFLKEIeSSPQCRRLT-LESLLLKPVQR 139

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 237757295    838 LHNYaKVLLK-LATCFEVTSPEYQKLQDSSSCYESLA 873
Cdd:smart00325  140 LTKY-PLLLKeLLKHTPEDHEDREDLKKALKAIKELA 175
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 1043-1063 1.96e-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: 39.70  E-value: 1.96e-04
                           10        20
                   ....*....|....*....|.
gi 237757295  1043 YDGRWLSGKPHGRGVLKWPDG 1063
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDG 21
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
1041-1062 3.32e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 39.25  E-value: 3.32e-04
                            10        20
                    ....*....|....*....|..
gi 237757295   1041 ATYDGRWLSGKPHGRGVLKWPD 1062
Cdd:smart00698    1 DRYEGEWRNGKRHGRGVYTYAN 22
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 929-994 1.41e-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: 39.45  E-value: 1.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 237757295  929 WFILFNDALVHAQFST------HHVFPLATLWAEPLSEEAGSVNGLKITTPEEQ-FTLISSTPQEKTKWLRAI 994
Cdd:cd00821    20 WFVLFEGVLLYYKSKKdssykpKGSIPLSGILEVEEVSPKERPHCFELVTPDGRtYYLQADSEEERQEWLKAL 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 929-999 2.94e-03

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: 38.68  E-value: 2.94e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757295    929 WFILFNDALV-------HAQFSTHHVFPLATL-WAEPLSEEAGSV-NGLKITTPEEQ-FTLISSTPQEKTKWLRAISQAV 998
Cdd:smart00233   22 YFVLFNSTLLyykskkdKKSYKPKGSIDLSGCtVREAPDPDSSKKpHCFEIKTSDRKtLLLQAESEEEREKWVEALRKAI 101


                    .
gi 237757295    999 D 999
Cdd:smart00233  102 A 102
 
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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