NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462575676|ref|XP_054199186|]
View 

alsin isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 905-1010 4.20e-64

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: 212.25  E-value: 4.20e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  905 DSLRKPERRLLCESSNRALSLQHAGRFSVNWFILFNDALVHAQFSTHHVFPLATLWAEPLSEEAGGVNGLKITTPEEQFT 984
Cdd:cd13269      1 DSLRSPDRRLIRESSTRPLTLQNAGRFSSHWFILFNDALVHAQFSTHHIFPLATLWVEPIPDEDSGQNALKITTPEESFT 80

                           90       100
                   ....*....|....*....|....*.
gi 2462575676  985 LISSTPQEKTKWLRAISQAVDQALRG 1010
Cdd:cd13269     81 LVASTPQEKAEWLRAINQAIDQALNG 106
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1049-1227 4.56e-34

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 132.39  E-value: 4.56e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1049 YDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNkamnkEDHYVGHWKEGKMCGQGVYSYASGEVFEGCFQ 1128
Cdd:COG4642    104 GGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPN-----GDVYEGEFKNGKPHGQGTLTYADGDRYEGEFK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1129 DNMRHGHGllrsgKLTSSSPSMFIGQWVMDKKAGYGV--FDDitrGEKYMGMWQDDVCQGNGVVVTQFGLYYEGNFHLNK 1206
Cdd:COG4642    179 NGKRHGQG-----TLTYANGDVYEGEFKNGQRHGQGTytYAD---GDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGK 250

                          170       180
                   ....*....|....*....|.
gi 2462575676 1207 MMGNGVLLSEDDTIYEGEFSD 1227
Cdd:COG4642    251 RHGQGTMTYADGSVYEGEWKN 271
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 39-219 4.50e-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: 111.22  E-value: 4.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   39 GGKTVLQAALGVKHGVLLTEDGEVYSFG----------TLPWRSGPVEIcpssPILENalvgqyVITVATGSFHSGAVTD 108
Cdd:COG5184    147 GLSGVVAIAAGGYHTCALKSDGTVWCWGansygqlgdgTTTDRPTPVQV----GGLSG------VVAVAAGGDHSCALKS 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  109 NGVAYMWGENSAGQCAVANQQYVPEPNPVSiadseasplLAVRILQLACGEEHTLALSISREIWAWG--TGCQLGLITTA 186
Cdd:COG5184    217 DGTVWCWGSNSSGQLGDGTTTDRATPVQVA---------GLTGVVAIAAGGSHTCALKSDGTVWCWGdnSYGQLGDGTTT 287

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462575676  187 fPVTKPQKVEHLAGrvVLQVACGAFHSLAL-----VQC 219
Cdd:COG5184    288 -DRSTPVKVPGLSG--VVAVAAGSSHTCALltdgtVWC 322
ATS1 super family cl34932
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 527-683 6.12e-18

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: 86.95  E-value: 6.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  527 EVWTWGKGKEGQLGHGDVLPRLQPlcVKCLDG-KEVIHLEAGGYHSLALTAKSQVYSWGSNTFGQLGHSDFP-TTVPrlA 604
Cdd:COG5184    118 TVWCWGDNSSGQLGDGTTTNRLTP--VQVDAGlSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTdRPTP--V 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  605 KISSENGVWSIAAGRDYSLFLVDTEDfqpgLYYSGR-QDPTEGDNLPENHSgskTPVLLscSKLGYISRVTAGKDSYLAL 683
Cdd:COG5184    194 QVGGLSGVVAVAAGGDHSCALKSDGT----VWCWGSnSSGQLGDGTTTDRA---TPVQV--AGLTGVVAIAAGGSHTCAL 264
RhoGEF super family cl02571
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 695-879 2.19e-07

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: 52.30  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  695 LHELATTERRFYSKLSDIKSQILRPLLSLENLGTTTTVQLLqevasrFSKLCYLIGQHgaslSSFLHGVKEARSL----- 769
Cdd:cd00160      5 IKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVELL------FGNIEEIYEFH----RIFLKSLEERVEEwdksg 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  770 -----VILKHSSLFlDSYTEYCTSITNFLvmggfQLLAKpaidfLNKNQELLQDLSEVNDENTQLMEiLNTLFFLPIRRL 844
Cdd:cd00160     75 prigdVFLKLAPFF-KIYSEYCSNHPDAL-----ELLKK-----LKKFNKFFQEFLEKAESECGRLK-LESLLLKPVQRL 142

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462575676  845 HNYaKVLLK-LATCFEVASPEYQKLQDSSSCYECLA 879
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 ...
 905-1010 4.20e-64

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: 212.25  E-value: 4.20e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  905 DSLRKPERRLLCESSNRALSLQHAGRFSVNWFILFNDALVHAQFSTHHVFPLATLWAEPLSEEAGGVNGLKITTPEEQFT 984
Cdd:cd13269      1 DSLRSPDRRLIRESSTRPLTLQNAGRFSSHWFILFNDALVHAQFSTHHIFPLATLWVEPIPDEDSGQNALKITTPEESFT 80

                           90       100
                   ....*....|....*....|....*.
gi 2462575676  985 LISSTPQEKTKWLRAISQAVDQALRG 1010
Cdd:cd13269     81 LVASTPQEKAEWLRAINQAIDQALNG 106
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1049-1227 4.56e-34

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 132.39  E-value: 4.56e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1049 YDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNkamnkEDHYVGHWKEGKMCGQGVYSYASGEVFEGCFQ 1128
Cdd:COG4642    104 GGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPN-----GDVYEGEFKNGKPHGQGTLTYADGDRYEGEFK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1129 DNMRHGHGllrsgKLTSSSPSMFIGQWVMDKKAGYGV--FDDitrGEKYMGMWQDDVCQGNGVVVTQFGLYYEGNFHLNK 1206
Cdd:COG4642    179 NGKRHGQG-----TLTYANGDVYEGEFKNGQRHGQGTytYAD---GDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGK 250

                          170       180
                   ....*....|....*....|.
gi 2462575676 1207 MMGNGVLLSEDDTIYEGEFSD 1227
Cdd:COG4642    251 RHGQGTMTYADGSVYEGEWKN 271
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 39-219 4.50e-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: 111.22  E-value: 4.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   39 GGKTVLQAALGVKHGVLLTEDGEVYSFG----------TLPWRSGPVEIcpssPILENalvgqyVITVATGSFHSGAVTD 108
Cdd:COG5184    147 GLSGVVAIAAGGYHTCALKSDGTVWCWGansygqlgdgTTTDRPTPVQV----GGLSG------VVAVAAGGDHSCALKS 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  109 NGVAYMWGENSAGQCAVANQQYVPEPNPVSiadseasplLAVRILQLACGEEHTLALSISREIWAWG--TGCQLGLITTA 186
Cdd:COG5184    217 DGTVWCWGSNSSGQLGDGTTTDRATPVQVA---------GLTGVVAIAAGGSHTCALKSDGTVWCWGdnSYGQLGDGTTT 287

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462575676  187 fPVTKPQKVEHLAGrvVLQVACGAFHSLAL-----VQC 219
Cdd:COG5184    288 -DRSTPVKVPGLSG--VVAVAAGSSHTCALltdgtVWC 322
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1048-1166 2.39e-19

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 94.13  E-value: 2.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1048 TYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKamnkeDHYVGHWKEGKMCGQGVYSYASGEVFEGCF 1127
Cdd:PLN03185    79 TYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANG-----NVYLGDMKGGKMSGKGTLTWVSGDSYEGQW 153

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462575676 1128 QDNMRHGHGLlrsgkLTSSSPSMFIGQWVMDKKAGYGVF 1166
Cdd:PLN03185   154 LDGMMHGFGV-----YTWSDGGCYVGTWTRGLKDGKGVF 187
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 527-683 6.12e-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: 86.95  E-value: 6.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  527 EVWTWGKGKEGQLGHGDVLPRLQPlcVKCLDG-KEVIHLEAGGYHSLALTAKSQVYSWGSNTFGQLGHSDFP-TTVPrlA 604
Cdd:COG5184    118 TVWCWGDNSSGQLGDGTTTNRLTP--VQVDAGlSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTdRPTP--V 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  605 KISSENGVWSIAAGRDYSLFLVDTEDfqpgLYYSGR-QDPTEGDNLPENHSgskTPVLLscSKLGYISRVTAGKDSYLAL 683
Cdd:COG5184    194 QVGGLSGVVAVAAGGDHSCALKSDGT----VWCWGSnSSGQLGDGTTTDRA---TPVQV--AGLTGVVAIAAGGSHTCAL 264
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
527-574 1.03e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 1.03e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462575676  527 EVWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGKEVIHLEAGGYHSLAL 574
Cdd:pfam00415    3 RVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
170-216 7.17e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 52.90  E-value: 7.17e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462575676  170 EIWAWG--TGCQLGLITTAfPVTKPQKVEHLAGRVVLQVACGAFHSLAL 216
Cdd:pfam00415    3 RVYTWGrnDYGQLGLGTTE-NVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 695-879 2.19e-07

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: 52.30  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  695 LHELATTERRFYSKLSDIKSQILRPLLSLENLGTTTTVQLLqevasrFSKLCYLIGQHgaslSSFLHGVKEARSL----- 769
Cdd:cd00160      5 IKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVELL------FGNIEEIYEFH----RIFLKSLEERVEEwdksg 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  770 -----VILKHSSLFlDSYTEYCTSITNFLvmggfQLLAKpaidfLNKNQELLQDLSEVNDENTQLMEiLNTLFFLPIRRL 844
Cdd:cd00160     75 prigdVFLKLAPFF-KIYSEYCSNHPDAL-----ELLKK-----LKKFNKFFQEFLEKAESECGRLK-LESLLLKPVQRL 142

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462575676  845 HNYaKVLLK-LATCFEVASPEYQKLQDSSSCYECLA 879
Cdd:cd00160    143 TKY-PLLLKeLLKHTPDGHEDREDLKKALEAIKEVA 177
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 695-879 5.53e-07

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: 51.15  E-value: 5.53e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   695 LHELATTERRFYSKLSDIKSQILRPLLSLENLGTTTTVQLLqevasrFSKLCYLIGQHgaslSSFLHGVKEARSL----- 769
Cdd:smart00325    2 LKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNELETL------FGNIEEIYEFH----RDFLDELEERIEEwddsv 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   770 -----VILKHSSLFlDSYTEYCTSITNFLvmggfQLLAKpaidfLNKNQELLQDLSEV-NDENTQLMEiLNTLFFLPIRR 843
Cdd:smart00325   72 erigdVFLKLEEFF-KIYSEYCSNHPDAL-----ELLKK-----LKKNPRFQKFLKEIeSSPQCRRLT-LESLLLKPVQR 139

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 2462575676   844 LHNYaKVLLK-LATCFEVASPEYQKLQDSSSCYECLA 879
Cdd:smart00325  140 LTKY-PLLLKeLLKHTPEDHEDREDLKKALKAIKELA 175
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 1100-1122 6.94e-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: 6.94e-05
                           10        20
                   ....*....|....*....|...
gi 2462575676 1100 YVGHWKEGKMCGQGVYSYASGEV 1122
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
1098-1118 1.25e-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: 1.25e-04
                            10        20
                    ....*....|....*....|.
gi 2462575676  1098 DHYVGHWKEGKMCGQGVYSYA 1118
Cdd:smart00698    1 DRYEGEWRNGKRHGRGVYTYA 21
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 935-1005 1.45e-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: 39.45  E-value: 1.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   935 WFILFNDALV-------HAQFSTHHVFPLATL-WAEPLSEEAGGV-NGLKITTPEEQ-FTLISSTPQEKTKWLRAISQAV 1004
Cdd:smart00233   22 YFVLFNSTLLyykskkdKKSYKPKGSIDLSGCtVREAPDPDSSKKpHCFEIKTSDRKtLLLQAESEEEREKWVEALRKAI 101


                    .
gi 2462575676  1005 D 1005
Cdd:smart00233  102 A 102
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 695-871 5.76e-03

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 39.21  E-value: 5.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  695 LHELATTERRFYSKLSDIKSQILRPLLSLENlgttttvQLLQEVASRFSKLCYLIGQHGaslSSFLHGVKEARSL----- 769
Cdd:pfam00621    2 IKELLQTERSYVRDLEILVEVFLPPNSKPLS-------ESEEEIKTIFSNIEEIYELHR---QLLLEELLKEWISiqrig 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  770 -VILKHSSLFlDSYTEYCTSITNFLvmggfQLLAKpAIDFLNKNQELLQDLSEvNDENTQLMeiLNTLFFLPIRRLHNYa 848
Cdd:pfam00621   72 dIFLKFAPGF-KVYSTYCSNYPKAL-----KLLKK-LLKKNPKFRAFLEELEA-NPECRGLD--LNSFLIKPVQRIPRY- 140

                          170       180
                   ....*....|....*....|....
gi 2462575676  849 KVLLK-LATCFEVASPEYQKLQDS 871
Cdd:pfam00621  141 PLLLKeLLKHTPPDHPDYEDLKKA 164
 
Name Accession Description Interval E-value
PH_alsin cd13269
Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...
 905-1010 4.20e-64

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: 212.25  E-value: 4.20e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  905 DSLRKPERRLLCESSNRALSLQHAGRFSVNWFILFNDALVHAQFSTHHVFPLATLWAEPLSEEAGGVNGLKITTPEEQFT 984
Cdd:cd13269      1 DSLRSPDRRLIRESSTRPLTLQNAGRFSSHWFILFNDALVHAQFSTHHIFPLATLWVEPIPDEDSGQNALKITTPEESFT 80

                           90       100
                   ....*....|....*....|....*.
gi 2462575676  985 LISSTPQEKTKWLRAISQAVDQALRG 1010
Cdd:cd13269     81 LVASTPQEKAEWLRAINQAIDQALNG 106
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1049-1227 4.56e-34

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 132.39  E-value: 4.56e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1049 YDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNkamnkEDHYVGHWKEGKMCGQGVYSYASGEVFEGCFQ 1128
Cdd:COG4642    104 GGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPN-----GDVYEGEFKNGKPHGQGTLTYADGDRYEGEFK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1129 DNMRHGHGllrsgKLTSSSPSMFIGQWVMDKKAGYGV--FDDitrGEKYMGMWQDDVCQGNGVVVTQFGLYYEGNFHLNK 1206
Cdd:COG4642    179 NGKRHGQG-----TLTYANGDVYEGEFKNGQRHGQGTytYAD---GDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGK 250

                          170       180
                   ....*....|....*....|.
gi 2462575676 1207 MMGNGVLLSEDDTIYEGEFSD 1227
Cdd:COG4642    251 RHGQGTMTYADGSVYEGEWKN 271
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1047-1181 4.24e-32

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 126.61  E-value: 4.24e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1047 ATYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKamnkeDHYVGHWKEGKMCGQGVYSYASGEVFEGC 1126
Cdd:COG4642    148 DVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANG-----DVYEGEFKNGQRHGQGTYTYADGDRYEGE 222

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462575676 1127 FQDNMRHGHgllrsGKLTSSSPSMFIGQWVMDKKAGYGVFDDITrGEKYMGMWQD 1181
Cdd:COG4642    223 FKNGKRHGQ-----GTLTYADGDRYEGEFKNGKRHGQGTMTYAD-GSVYEGEWKN 271
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1035-1157 5.86e-30

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 120.45  E-value: 5.86e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1035 KYTFYKDPRlkdatYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKamnkeDHYVGHWKEGKMCGQGV 1114
Cdd:COG4642    164 TLTYADGDR-----YEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADG-----DRYEGEFKNGKRHGQGT 233

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2462575676 1115 YSYASGEVFEGCFQDNMRHGHgllrsGKLTSSSPSMFIGQWVM 1157
Cdd:COG4642    234 LTYADGDRYEGEFKNGKRHGQ-----GTMTYADGSVYEGEWKN 271
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 39-219 4.50e-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: 111.22  E-value: 4.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   39 GGKTVLQAALGVKHGVLLTEDGEVYSFG----------TLPWRSGPVEIcpssPILENalvgqyVITVATGSFHSGAVTD 108
Cdd:COG5184    147 GLSGVVAIAAGGYHTCALKSDGTVWCWGansygqlgdgTTTDRPTPVQV----GGLSG------VVAVAAGGDHSCALKS 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  109 NGVAYMWGENSAGQCAVANQQYVPEPNPVSiadseasplLAVRILQLACGEEHTLALSISREIWAWG--TGCQLGLITTA 186
Cdd:COG5184    217 DGTVWCWGSNSSGQLGDGTTTDRATPVQVA---------GLTGVVAIAAGGSHTCALKSDGTVWCWGdnSYGQLGDGTTT 287

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462575676  187 fPVTKPQKVEHLAGrvVLQVACGAFHSLAL-----VQC 219
Cdd:COG5184    288 -DRSTPVKVPGLSG--VVAVAAGSSHTCALltdgtVWC 322
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 31-216 2.84e-23

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: 102.75  E-value: 2.84e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   31 TPERLPGwgGKTVLQAALGVKHGVLLTEDGEVYSFG----------TLPWRSGPVEIcpssPILENalvgqyVITVATGS 100
Cdd:COG5184     40 TPVRVPG--LSNVVAVAAGGDHTCALKADGTVWCWGnnsygqlgdgTTTDRTTPVKV----PGLTG------VVAVAAGY 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  101 FHSGAVTDNGVAYMWGENSAGQcaVANQQYVPEPNPVSIADSeaspllAVRILQLACGEEHTLALSISREIWAWG--TGC 178
Cdd:COG5184    108 YHSCALKSDGTVWCWGDNSSGQ--LGDGTTTNRLTPVQVDAG------LSGVVAIAAGGYHTCALKSDGTVWCWGanSYG 179

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462575676  179 QLGLITTAfPVTKPQKVEHLAGrvVLQVACGAFHSLAL 216
Cdd:COG5184    180 QLGDGTTT-DRPTPVQVGGLSG--VVAVAAGGDHSCAL 214
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 31-219 9.34e-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: 98.13  E-value: 9.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   31 TPERLPGWGGktVLQAALGVKHGVLLTEDGEVYSFG----------TLPWRSGPVEICPSspiLENalvgqyVITVATGS 100
Cdd:COG5184     90 TPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGdnssgqlgdgTTTNRLTPVQVDAG---LSG------VVAIAAGG 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  101 FHSGAVTDNGVAYMWGENSAGQCAVANQQYVPEPNPVSIADSeaspllavrILQLACGEEHTLALSISREIWAWGTG--C 178
Cdd:COG5184    159 YHTCALKSDGTVWCWGANSYGQLGDGTTTDRPTPVQVGGLSG---------VVAVAAGGDHSCALKSDGTVWCWGSNssG 229

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462575676  179 QLGLITTAFPVTkPQKVEHLAGrvVLQVACGAFHSLAL-----VQC 219
Cdd:COG5184    230 QLGDGTTTDRAT-PVQVAGLTG--VVAIAAGGSHTCALksdgtVWC 272
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1034-1234 1.31e-21

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 96.18  E-value: 1.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1034 AKYTFYKDPRLKDATYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNK-------AMNKEDHYVGHWKE 1106
Cdd:COG4642     31 GEGGGGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGGEGGVTAAGGGGGGGGGKGDGGdggggegGFGGGGGGGGGKKG 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1107 GKMCGQGVYSYASGEVFEGCFQDNMRHGHGllrsgKLTSSSPSMFIGQWVMDKKAGYGVFDDiTRGEKYMGMWQDDVCQG 1186
Cdd:COG4642    111 GGGGGGGVLEGDDGGGYGGGTADGGRGGGG-----IYTFPNGDVYEGEFKNGKPHGQGTLTY-ADGDRYEGEFKNGKRHG 184

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462575676 1187 NGVVVTQFGLYYEGNFHLNKMMGNGVLLSEDDTIYEGEFSDDwTLSGK 1234
Cdd:COG4642    185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNG-KRHGQ 231
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 45-216 2.62e-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: 93.89  E-value: 2.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   45 QAALGVKHGVLLTEDGEVYSFG----------TLPWRSGPVEIcpssPILENalvgqyVITVATGSFHSGAVTDNGVAYM 114
Cdd:COG5184      2 QVAAGGSHSCALKSDGTVWCWGdnsygqlgdgTTTDRSTPVRV----PGLSN------VVAVAAGGDHTCALKADGTVWC 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  115 WGENSAGQCAVANQQYVPEPNPVSIADSeaspllavrILQLACGEEHTLALSISREIWAWGTGC--QLGLITTAfPVTKP 192
Cdd:COG5184     72 WGNNSYGQLGDGTTTDRTTPVKVPGLTG---------VVAVAAGYYHSCALKSDGTVWCWGDNSsgQLGDGTTT-NRLTP 141

                          170       180
                   ....*....|....*....|....
gi 2462575676  193 QKVEHLAGRVVlQVACGAFHSLAL 216
Cdd:COG5184    142 VQVDAGLSGVV-AIAAGGYHTCAL 164
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1048-1166 2.39e-19

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 94.13  E-value: 2.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1048 TYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKamnkeDHYVGHWKEGKMCGQGVYSYASGEVFEGCF 1127
Cdd:PLN03185    79 TYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANG-----NVYLGDMKGGKMSGKGTLTWVSGDSYEGQW 153

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462575676 1128 QDNMRHGHGLlrsgkLTSSSPSMFIGQWVMDKKAGYGVF 1166
Cdd:PLN03185   154 LDGMMHGFGV-----YTWSDGGCYVGTWTRGLKDGKGVF 187
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1048-1202 2.86e-19

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 94.13  E-value: 2.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1048 TYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKAMnkedhYVGHWKEGKMCGQGVYSYASGEVFEGCF 1127
Cdd:PLN03185    33 MYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTT-----YKGRWRLNLKHGLGYQRYPNGDVFEGSW 107

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462575676 1128 QDNMRHGHgllrsGKLTSSSPSMFIGQWVMDKKAGYGVFdDITRGEKYMGMWQDDVCQGNGVVVTQFGLYYEGNF 1202
Cdd:PLN03185   108 IQGLQEGP-----GKYTWANGNVYLGDMKGGKMSGKGTL-TWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTW 176
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 527-683 6.12e-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: 86.95  E-value: 6.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  527 EVWTWGKGKEGQLGHGDVLPRLQPlcVKCLDG-KEVIHLEAGGYHSLALTAKSQVYSWGSNTFGQLGHSDFP-TTVPrlA 604
Cdd:COG5184    118 TVWCWGDNSSGQLGDGTTTNRLTP--VQVDAGlSGVVAIAAGGYHTCALKSDGTVWCWGANSYGQLGDGTTTdRPTP--V 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  605 KISSENGVWSIAAGRDYSLFLVDTEDfqpgLYYSGR-QDPTEGDNLPENHSgskTPVLLscSKLGYISRVTAGKDSYLAL 683
Cdd:COG5184    194 QVGGLSGVVAVAAGGDHSCALKSDGT----VWCWGSnSSGQLGDGTTTDRA---TPVQV--AGLTGVVAIAAGGSHTCAL 264
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 94-216 1.45e-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: 1.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   94 ITVATGSFHSGAVTDNGVAYMWGENSAGQcaVANQQYVPEPNPVSIADSEaspllavRILQLACGEEHTLALSISREIWA 173
Cdd:COG5184      1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQ--LGDGTTTDRSTPVRVPGLS-------NVVAVAAGGDHTCALKADGTVWC 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462575676  174 WGTGC--QLGLITTAFPVTkPQKVEHLAGrvVLQVACGAFHSLAL 216
Cdd:COG5184     72 WGNNSygQLGDGTTTDRTT-PVKVPGLTG--VVAVAAGYYHSCAL 113
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 31-189 1.54e-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: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   31 TPERLPGWGGktVLQAALGVKHGVLLTEDGEVYSFG----------TLPWRSGPVEICPSSPilenalvgqyVITVATGS 100
Cdd:COG5184    191 TPVQVGGLSG--VVAVAAGGDHSCALKSDGTVWCWGsnssgqlgdgTTTDRATPVQVAGLTG----------VVAIAAGG 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  101 FHSGAVTDNGVAYMWGENSAGQCAVANQQYVPEPNPVSIADseaspllavRILQLACGEEHTLALSISREIWAWGTGC-- 178
Cdd:COG5184    259 SHTCALKSDGTVWCWGDNSYGQLGDGTTTDRSTPVKVPGLS---------GVVAVAAGSSHTCALLTDGTVWCWGDNAyg 329

                          170
                   ....*....|....
gi 2462575676  179 QLGLITT---AFPV 189
Cdd:COG5184    330 QLGDGTTtdrSTPV 343
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 527-628 4.03e-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: 4.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  527 EVWTWGKGKEGQLGHGDVLPRLQPlcVKCLDGKEVIHLEAGGYHSLALTAKSQVYSWGSNTFGQLGHSdfpTTVPRLA-- 604
Cdd:COG5184    219 TVWCWGSNSSGQLGDGTTTDRATP--VQVAGLTGVVAIAAGGSHTCALKSDGTVWCWGDNSYGQLGDG---TTTDRSTpv 293

                           90       100
                   ....*....|....*....|....
gi 2462575676  605 KISSENGVWSIAAGRDYSLFLVDT 628
Cdd:COG5184    294 KVPGLSGVVAVAAGSSHTCALLTD 317
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 528-628 5.99e-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: 83.87  E-value: 5.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  528 VWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGkeVIHLEAGGYHSLALTAKSQVYSWGSNTFGQLGHSDF-----PTTVPR 602
Cdd:COG5184     19 VWCWGDNSYGQLGDGTTTDRSTPVRVPGLSN--VVAVAAGGDHTCALKADGTVWCWGNNSYGQLGDGTTtdrttPVKVPG 96

                           90       100
                   ....*....|....*....|....*.
gi 2462575676  603 LAKISsengvwSIAAGRDYSLFLVDT 628
Cdd:COG5184     97 LTGVV------AVAAGYYHSCALKSD 116
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 527-625 1.10e-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: 1.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  527 EVWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGkeVIHLEAGGYHSLALTAKSQVYSWGSNTFGQLGHSDF-PTTVPRLAK 605
Cdd:COG5184     68 TVWCWGNNSYGQLGDGTTTDRTTPVKVPGLTG--VVAVAAGYYHSCALKSDGTVWCWGDNSSGQLGDGTTtNRLTPVQVD 145

                           90       100
                   ....*....|....*....|
gi 2462575676  606 ISSENGVwSIAAGRDYSLFL 625
Cdd:COG5184    146 AGLSGVV-AIAAGGYHTCAL 164
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1049-1238 1.55e-16

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 85.27  E-value: 1.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1049 YDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKAMnkedhYVGHWKEGKMCGQGVYSYASGEVFEGCFQ 1128
Cdd:PLN03185    11 YSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGAT-----YEGEFSGGYMHGSGTYTGTDGTTYKGRWR 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1129 DNMRHGHGLLRsgkltSSSPSMFIGQWVMDKKAGYGVFdDITRGEKYMGMWQDDVCQGNGVVVTQFGLYYEGNFhLNKMM 1208
Cdd:PLN03185    86 LNLKHGLGYQR-----YPNGDVFEGSWIQGLQEGPGKY-TWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQW-LDGMM 158

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462575676 1209 -GNGVLLSEDDTIYEGefsdDWTLSGKDNSG 1238
Cdd:PLN03185   159 hGFGVYTWSDGGCYVG----TWTRGLKDGKG 185
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1062-1227 1.20e-14

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 79.11  E-value: 1.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1062 GVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKAMnkedhYVGHWKEGKMCGQGVYSYASGEVFEGCFQDNMRHGhgllrSG 1141
Cdd:PLN03185     1 GELVLSNGDFYSGSLLGNVPEGPGKYLWSDGCM-----YEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHG-----SG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1142 KLTSSSPSMFIGQWVMDKKAGYGvFDDITRGEKYMGMWQDDVCQGNGVVVTQFGLYYEGNFHLNKMMGNGVLLSEDDTIY 1221
Cdd:PLN03185    71 TYTGTDGTTYKGRWRLNLKHGLG-YQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSY 149


                   ....*.
gi 2462575676 1222 EGEFSD 1227
Cdd:PLN03185   150 EGQWLD 155
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 528-592 1.82e-13

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: 73.09  E-value: 1.82e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462575676  528 VWTWGKGKEGQLGHGDVLPRLQPlcVKCLDGKEVIHLEAGGYHSLALTAKSQVYSWGSNTFGQLG 592
Cdd:COG5184    270 VWCWGDNSYGQLGDGTTTDRSTP--VKVPGLSGVVAVAAGSSHTCALLTDGTVWCWGDNAYGQLG 332
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
527-574 1.03e-11

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 60.61  E-value: 1.03e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462575676  527 EVWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGKEVIHLEAGGYHSLAL 574
Cdd:pfam00415    3 RVYTWGRNDYGQLGLGTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
PH_Phafin2-like cd01218
Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain; ...
 935-1003 8.04e-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: 57.65  E-value: 8.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575676  935 WFILFNDALVHA-------QFSTHHVFPLATLWAEPLSEEAGGVNGLKITTPEEQFTLISSTPQEKTKWLRAISQA 1003
Cdd:cd01218     48 QFFLFNDILVYGsivinkkKYNKQRIIPLEDVKIEDLEDTGELKNGWQIISPKKSFVVYAATATEKSEWMDHINKC 123
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
579-625 6.07e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 52.90  E-value: 6.07e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462575676  579 QVYSWGSNTFGQLGH-SDFPTTVPRLAKISSENGVWSIAAGRDYSLFL 625
Cdd:pfam00415    3 RVYTWGRNDYGQLGLgTTENVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
170-216 7.17e-09

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 52.90  E-value: 7.17e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462575676  170 EIWAWG--TGCQLGLITTAfPVTKPQKVEHLAGRVVLQVACGAFHSLAL 216
Cdd:pfam00415    3 RVYTWGrnDYGQLGLGTTE-NVLVPQKVEGLSGNKVVQVACGGDHTVAL 50
ATS1 COG5184
Alpha-tubulin suppressor ATS1 and related RCC1 domain-containing proteins [Cell cycle control, ...
 562-625 9.65e-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: 58.83  E-value: 9.65e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462575676  562 IHLEAGGYHSLALTAKSQVYSWGSNTFGQLG-----HSDFPTTVPRLAKISsengvwSIAAGRDYSLFL 625
Cdd:COG5184      1 TQVAAGGSHSCALKSDGTVWCWGDNSYGQLGdgtttDRSTPVRVPGLSNVV------AVAAGGDHTCAL 63
PH1_FGD5_FGD6 cd13389
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal ...
 936-1004 7.74e-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: 52.27  E-value: 7.74e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575676  936 FILFNDALVHA-------QFSTHHVFPLATLWAEPLSEEAGgVNGLKITTPEEQFTLISSTPQEKTKWLRAISQAV 1004
Cdd:cd13389     33 FFLFNDCLLYTtpvqssgMLKLNNELPLSGMKVKLPEDEEY-SNEFQIISTKRSFTLIASSEEERDEWVKALSRAI 107
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
561-590 1.68e-07

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 48.19  E-value: 1.68e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575676  561 VIHLEAGGYHSLALTAKSQVYSWGSNTFGQ 590
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 695-879 2.19e-07

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: 52.30  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  695 LHELATTERRFYSKLSDIKSQILRPLLSLENLGTTTTVQLLqevasrFSKLCYLIGQHgaslSSFLHGVKEARSL----- 769
Cdd:cd00160      5 IKELLQTERNYVRDLKLLVEVFLKPLDKELLPLSPEEVELL------FGNIEEIYEFH----RIFLKSLEERVEEwdksg 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  770 -----VILKHSSLFlDSYTEYCTSITNFLvmggfQLLAKpaidfLNKNQELLQDLSEVNDENTQLMEiLNTLFFLPIRRL 844
Cdd:cd00160     75 prigdVFLKLAPFF-KIYSEYCSNHPDAL-----ELLKK-----LKKFNKFFQEFLEKAESECGRLK-LESLLLKPVQRL 142

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462575676  845 HNYaKVLLK-LATCFEVASPEYQKLQDSSSCYECLA 879
Cdd:cd00160    143 TKY-PLLLKeLLKHTPDGHEDREDLKKALEAIKEVA 177
PH1_FARP1-like cd01220
FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin ...
 936-1007 2.89e-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: 50.01  E-value: 2.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  936 FILFNDALVHA--------QFSTHHVFPLATLWAEPLSEEAGGVNGLKITTPEEQFTLISSTPQEKTKWLRAISQAVDQA 1007
Cdd:cd01220     27 FFLFSDVLLYTsrsptpslQFKVHGQLPLRGLMVEESEPEWGVAHCFTIYGGNRALTVAASSEEEKERWLEDLQRAIDAA 106
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 695-879 5.53e-07

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: 51.15  E-value: 5.53e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   695 LHELATTERRFYSKLSDIKSQILRPLLSLENLGTTTTVQLLqevasrFSKLCYLIGQHgaslSSFLHGVKEARSL----- 769
Cdd:smart00325    2 LKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNELETL------FGNIEEIYEFH----RDFLDELEERIEEwddsv 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   770 -----VILKHSSLFlDSYTEYCTSITNFLvmggfQLLAKpaidfLNKNQELLQDLSEV-NDENTQLMEiLNTLFFLPIRR 843
Cdd:smart00325   72 erigdVFLKLEEFF-KIYSEYCSNHPDAL-----ELLKK-----LKKNPRFQKFLKEIeSSPQCRRLT-LESLLLKPVQR 139

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 2462575676   844 LHNYaKVLLK-LATCFEVASPEYQKLQDSSSCYECLA 879
Cdd:smart00325  140 LTKY-PLLLKeLLKHTPEDHEDREDLKKALKAIKELA 175
PH1_FGD6 cd15793
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 6, N-terminal Pleckstrin ...
 936-1006 5.98e-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: 46.95  E-value: 5.98e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575676  936 FILFNDALVH------AQFSTHHVFPLATLWAEPLSEEAGGvNGLKITTPEEQFTLISSTPQEKTKWLRAISQAVDQ 1006
Cdd:cd15793     33 FFLFNDALLYttpvqsGMYKLNNMLSLAGMKVSKPSQEAYQ-NELNIESVERSFILSASSATERDEWLEAISRAIEE 108
RCC1_2 pfam13540
Regulator of chromosome condensation (RCC1) repeat;
93-122 8.86e-06

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 463914 [Multi-domain]  Cd Length: 30  Bit Score: 43.57  E-value: 8.86e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575676   93 VITVATGSFHSGAVTDNGVAYMWGENSAGQ 122
Cdd:pfam13540    1 VVSVAAGDNHTLALTSDGRVYCWGDNSYGQ 30
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
 935-1013 1.52e-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: 45.00  E-value: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  935 WFILFNDAL------VHAQFST-HHVFPLAT-LWAEPLSEEAGGVNGLKITTPEEQFTLISSTPQEKTKWLRAISQAVDQ 1006
Cdd:cd13276     19 WFVLKQGKLfwfkepDVTPYSKpRGVIDLSKcLTVKSAEDATNKENAFELSTPEETFYFIADNEKEKEEWIGAIGRAIVK 98


                   ....*..
gi 2462575676 1007 ALRGMSD 1013
Cdd:cd13276     99 HSRSVTD 105
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
1035-1145 3.76e-05

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


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 45.44  E-value: 3.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676 1035 KYTFYKDPRLKDATYDGRWLSGKPHGRGVLKW--PDGKMYS-GMFRNGLEDGYGEYRIPNKAMNKEdhyvGHWKEGKMCG 1111
Cdd:COG2849     41 EDSYNEGGKLIKKKLGKGLGKYKKGKLGEWKTyyPNGQLKSeGTYKNGKLEGEWKEYYENGKLKSE----GNYKNGKLHG 116

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575676 1112 QGVYSYASGEVF-EGCFQDNMRHGHGLL--RSGKLTS 1145
Cdd:COG2849    117 EWKEYYENGKLKeEGNYKNGKKDGVWKYydENGKLVK 153
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 1100-1122 6.94e-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: 6.94e-05
                           10        20
                   ....*....|....*....|...
gi 2462575676 1100 YVGHWKEGKMCGQGVYSYASGEV 1122
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
RCC1 pfam00415
Regulator of chromosome condensation (RCC1) repeat;
109-165 6.96e-05

Regulator of chromosome condensation (RCC1) repeat;


Pssm-ID: 395335 [Multi-domain]  Cd Length: 50  Bit Score: 41.35  E-value: 6.96e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575676  109 NGVAYMWGENSAGQCAVANQQYVPEPNPVSIadseaspLLAVRILQLACGEEHTLAL 165
Cdd:pfam00415    1 DGRVYTWGRNDYGQLGLGTTENVLVPQKVEG-------LSGNKVVQVACGGDHTVAL 50
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
1098-1118 1.25e-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: 1.25e-04
                            10        20
                    ....*....|....*....|.
gi 2462575676  1098 DHYVGHWKEGKMCGQGVYSYA 1118
Cdd:smart00698    1 DRYEGEWRNGKRHGRGVYTYA 21
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 1049-1069 1.69e-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: 1.69e-04
                           10        20
                   ....*....|....*....|.
gi 2462575676 1049 YDGRWLSGKPHGRGVLKWPDG 1069
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDG 21
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
1047-1068 2.68e-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: 2.68e-04
                            10        20
                    ....*....|....*....|..
gi 2462575676  1047 ATYDGRWLSGKPHGRGVLKWPD 1068
Cdd:smart00698    1 DRYEGEWRNGKRHGRGVYTYAN 22
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 935-1000 6.72e-04

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: 40.22  E-value: 6.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462575676  935 WFILFNDALVHAQFST------HHVFPLATLWAEPLSEEAGGVNGLKITTPEEQ-FTLISSTPQEKTKWLRAI 1000
Cdd:cd00821     20 WFVLFEGVLLYYKSKKdssykpKGSIPLSGILEVEEVSPKERPHCFELVTPDGRtYYLQADSEEERQEWLKAL 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 935-1005 1.45e-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: 39.45  E-value: 1.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676   935 WFILFNDALV-------HAQFSTHHVFPLATL-WAEPLSEEAGGV-NGLKITTPEEQ-FTLISSTPQEKTKWLRAISQAV 1004
Cdd:smart00233   22 YFVLFNSTLLyykskkdKKSYKPKGSIDLSGCtVREAPDPDSSKKpHCFEIKTSDRKtLLLQAESEEEREKWVEALRKAI 101


                    .
gi 2462575676  1005 D 1005
Cdd:smart00233  102 A 102
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 695-871 5.76e-03

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 39.21  E-value: 5.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  695 LHELATTERRFYSKLSDIKSQILRPLLSLENlgttttvQLLQEVASRFSKLCYLIGQHGaslSSFLHGVKEARSL----- 769
Cdd:pfam00621    2 IKELLQTERSYVRDLEILVEVFLPPNSKPLS-------ESEEEIKTIFSNIEEIYELHR---QLLLEELLKEWISiqrig 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575676  770 -VILKHSSLFlDSYTEYCTSITNFLvmggfQLLAKpAIDFLNKNQELLQDLSEvNDENTQLMeiLNTLFFLPIRRLHNYa 848
Cdd:pfam00621   72 dIFLKFAPGF-KVYSTYCSNYPKAL-----KLLKK-LLKKNPKFRAFLEELEA-NPECRGLD--LNSFLIKPVQRIPRY- 140

                          170       180
                   ....*....|....*....|....
gi 2462575676  849 KVLLK-LATCFEVASPEYQKLQDS 871
Cdd:pfam00621  141 PLLLKeLLKHTPPDHPDYEDLKKA 164
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH