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Conserved domains on  [gi|33359215|ref|NP_667340|]
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ALS2 C-terminal-like protein isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
357-557 2.86e-32

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 126.61  E-value: 2.86e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 357 TYEGEWCRGRPHGKGTLKWPDGRNHVGNFCQGLEHGFGIRLLPQASE-----DKFDCYKCHWREGSMCGYGICEYSTDEV 431
Cdd:COG4642  70 GGVTAAGGGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGgvlegDDGGGYGGGTADGGRGGGGIYTFPNGDV 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 432 YKGYFQEGLRHGFGVLESGPQApqpfRYTGHWERGQRSGYGIEEDGDrGERYIGMWQAGQRHGPGVMVTQAGVCYQGTFQ 511
Cdd:COG4642 150 YEGEFKNGKPHGQGTLTYADGD----RYEGEFKNGKRHGQGTLTYAN-GDVYEGEFKNGQRHGQGTYTYADGDRYEGEFK 224

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 33359215 512 ADKTVGPGILLSEDDSLYEGTFTRDLtLMGKGKVTFPNGFTLEGSF 557
Cdd:COG4642 225 NGKRHGQGTLTYADGDRYEGEFKNGK-RHGQGTMTYADGSVYEGEW 269
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 836-938 2.26e-18

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: 81.10  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215   836 SATECLQKIMTTVDPREKLEVLERTYGEIEGTVSRvLGREYKLPMDDLLPLLIYVVSRARIQHLGAEIHLIRDMMDPNHT 915
Cdd:pfam02204   3 QAQQELKKLNEAKSPREKLKCLLRTCKLITEALSK-SNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDLL 81

                          90       100
                  ....*....|....*....|...
gi 33359215   916 GGLYDFLLTALESCYEHIQKEDM 938
Cdd:pfam02204  82 SGEEGYYLTTLEAALEFIESLDP 104
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 223-321 1.12e-12

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


The actual alignment was detected with superfamily member cd13269:

Pssm-ID: 473070  Cd Length: 106  Bit Score: 65.11  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 223 DVLCTPAHRLLQDSQDVPVTVAplRAERV-----LLFDDALVLLQGHNVHTFDLKLVWVDPGQDGCT----FHLLTPEEE 293
Cdd:cd13269   1 DSLRSPDRRLIRESSTRPLTLQ--NAGRFsshwfILFNDALVHAQFSTHHIFPLATLWVEPIPDEDSgqnaLKITTPEES 78

                        90       100
                ....*....|....*....|....*...
gi 33359215 294 FSFCAKDSQGQAVWQWKVTWAVHQALHG 321
Cdd:cd13269  79 FTLVASTPQEKAEWLRAINQAIDQALNG 106
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
357-557 2.86e-32

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 126.61  E-value: 2.86e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 357 TYEGEWCRGRPHGKGTLKWPDGRNHVGNFCQGLEHGFGIRLLPQASE-----DKFDCYKCHWREGSMCGYGICEYSTDEV 431
Cdd:COG4642  70 GGVTAAGGGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGgvlegDDGGGYGGGTADGGRGGGGIYTFPNGDV 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 432 YKGYFQEGLRHGFGVLESGPQApqpfRYTGHWERGQRSGYGIEEDGDrGERYIGMWQAGQRHGPGVMVTQAGVCYQGTFQ 511
Cdd:COG4642 150 YEGEFKNGKPHGQGTLTYADGD----RYEGEFKNGKRHGQGTLTYAN-GDVYEGEFKNGQRHGQGTYTYADGDRYEGEFK 224

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 33359215 512 ADKTVGPGILLSEDDSLYEGTFTRDLtLMGKGKVTFPNGFTLEGSF 557
Cdd:COG4642 225 NGKRHGQGTLTYADGDRYEGEFKNGK-RHGQGTMTYADGSVYEGEW 269
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 836-938 2.26e-18

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: 81.10  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215   836 SATECLQKIMTTVDPREKLEVLERTYGEIEGTVSRvLGREYKLPMDDLLPLLIYVVSRARIQHLGAEIHLIRDMMDPNHT 915
Cdd:pfam02204   3 QAQQELKKLNEAKSPREKLKCLLRTCKLITEALSK-SNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDLL 81

                          90       100
                  ....*....|....*....|...
gi 33359215   916 GGLYDFLLTALESCYEHIQKEDM 938
Cdd:pfam02204  82 SGEEGYYLTTLEAALEFIESLDP 104
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 357-510 3.00e-16

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 83.73  E-value: 3.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215  357 TYEGEWCRGRPHGKGTLKWPDGRNHVGNFCQGLEHGFGIRLLPQASedkfdCYKCHWREGSMCGYGICEYSTDEVYKGYF 436
Cdd:PLN03185  33 MYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGT-----TYKGRWRLNLKHGLGYQRYPNGDVFEGSW 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33359215  437 QEGLRHGFG--VLESGPQapqpfrYTGHWERGQRSGYGIEEdGDRGERYIGMWQAGQRHGPGVMVTQAGVCYQGTF 510
Cdd:PLN03185 108 IQGLQEGPGkyTWANGNV------YLGDMKGGKMSGKGTLT-WVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTW 176
PH_alsin cd13269
Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...
 223-321 1.12e-12

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: 65.11  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 223 DVLCTPAHRLLQDSQDVPVTVAplRAERV-----LLFDDALVLLQGHNVHTFDLKLVWVDPGQDGCT----FHLLTPEEE 293
Cdd:cd13269   1 DSLRSPDRRLIRESSTRPLTLQ--NAGRFsshwfILFNDALVHAQFSTHHIFPLATLWVEPIPDEDSgqnaLKITTPEES 78

                        90       100
                ....*....|....*....|....*...
gi 33359215 294 FSFCAKDSQGQAVWQWKVTWAVHQALHG 321
Cdd:cd13269  79 FTLVASTPQEKAEWLRAINQAIDQALNG 106
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 358-378 4.81e-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: 4.81e-05
                          10        20
                  ....*....|....*....|.
gi 33359215   358 YEGEWCRGRPHGKGTLKWPDG 378
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
356-377 3.35e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 38.48  E-value: 3.35e-04
                           10        20
                   ....*....|....*....|..
gi 33359215    356 ATYEGEWCRGRPHGKGTLKWPD 377
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
357-557 2.86e-32

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 126.61  E-value: 2.86e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 357 TYEGEWCRGRPHGKGTLKWPDGRNHVGNFCQGLEHGFGIRLLPQASE-----DKFDCYKCHWREGSMCGYGICEYSTDEV 431
Cdd:COG4642  70 GGVTAAGGGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGgvlegDDGGGYGGGTADGGRGGGGIYTFPNGDV 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 432 YKGYFQEGLRHGFGVLESGPQApqpfRYTGHWERGQRSGYGIEEDGDrGERYIGMWQAGQRHGPGVMVTQAGVCYQGTFQ 511
Cdd:COG4642 150 YEGEFKNGKPHGQGTLTYADGD----RYEGEFKNGKRHGQGTLTYAN-GDVYEGEFKNGQRHGQGTYTYADGDRYEGEFK 224

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 33359215 512 ADKTVGPGILLSEDDSLYEGTFTRDLtLMGKGKVTFPNGFTLEGSF 557
Cdd:COG4642 225 NGKRHGQGTLTYADGDRYEGEFKNGK-RHGQGTMTYADGSVYEGEW 269
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
356-510 4.07e-30

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 120.45  E-value: 4.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 356 ATYEGEWCRGRPHGKGTLKWPDGrnhvgnfcqglehgfgirllpqasedkfDCYKCHWREGSMCGYGICEYSTDEVYKGY 435
Cdd:COG4642 148 DVYEGEFKNGKPHGQGTLTYADG----------------------------DRYEGEFKNGKRHGQGTLTYANGDVYEGE 199

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33359215 436 FQEGLRHGFGVLESgpqaPQPFRYTGHWERGQRSGYGIEEDGDrGERYIGMWQAGQRHGPGVMVTQAGVCYQGTF 510
Cdd:COG4642 200 FKNGQRHGQGTYTY----ADGDRYEGEFKNGKRHGQGTLTYAD-GDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 836-938 2.26e-18

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: 81.10  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215   836 SATECLQKIMTTVDPREKLEVLERTYGEIEGTVSRvLGREYKLPMDDLLPLLIYVVSRARIQHLGAEIHLIRDMMDPNHT 915
Cdd:pfam02204   3 QAQQELKKLNEAKSPREKLKCLLRTCKLITEALSK-SNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDLL 81

                          90       100
                  ....*....|....*....|...
gi 33359215   916 GGLYDFLLTALESCYEHIQKEDM 938
Cdd:pfam02204  82 SGEEGYYLTTLEAALEFIESLDP 104
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 357-510 3.00e-16

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 83.73  E-value: 3.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215  357 TYEGEWCRGRPHGKGTLKWPDGRNHVGNFCQGLEHGFGIRLLPQASedkfdCYKCHWREGSMCGYGICEYSTDEVYKGYF 436
Cdd:PLN03185  33 MYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGT-----TYKGRWRLNLKHGLGYQRYPNGDVFEGSW 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33359215  437 QEGLRHGFG--VLESGPQapqpfrYTGHWERGQRSGYGIEEdGDRGERYIGMWQAGQRHGPGVMVTQAGVCYQGTF 510
Cdd:PLN03185 108 IQGLQEGPGkyTWANGNV------YLGDMKGGKMSGKGTLT-WVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTW 176
PH_alsin cd13269
Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...
 223-321 1.12e-12

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: 65.11  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 223 DVLCTPAHRLLQDSQDVPVTVAplRAERV-----LLFDDALVLLQGHNVHTFDLKLVWVDPGQDGCT----FHLLTPEEE 293
Cdd:cd13269   1 DSLRSPDRRLIRESSTRPLTLQ--NAGRFsshwfILFNDALVHAQFSTHHIFPLATLWVEPIPDEDSgqnaLKITTPEES 78

                        90       100
                ....*....|....*....|....*...
gi 33359215 294 FSFCAKDSQGQAVWQWKVTWAVHQALHG 321
Cdd:cd13269  79 FTLVASTPQEKAEWLRAINQAIDQALNG 106
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 358-550 5.73e-11

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 66.40  E-value: 5.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215  358 YEGEWCRGRPHGKGTLKWPDGRNHVGNFCQGLEHGFGIRLLPQ--ASEDKFDCykchwreGSMCGYGICEYSTDEVYKGY 435
Cdd:PLN03185  11 YSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSgaTYEGEFSG-------GYMHGSGTYTGTDGTTYKGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215  436 FQEGLRHGFGVlesgPQAPQPFRYTGHWERGQRSGYGiEEDGDRGERYIGMWQAGQRHGPGVMVTQAGVCYQGTFQADKT 515
Cdd:PLN03185  84 WRLNLKHGLGY----QRYPNGDVFEGSWIQGLQEGPG-KYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMM 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 33359215  516 VGPGILLSEDDSLYEGTFTRDLTlMGKGkVTFPNG 550
Cdd:PLN03185 159 HGFGVYTWSDGGCYVGTWTRGLK-DGKG-VFYPAG 191
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 356-497 2.31e-10

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 64.47  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215  356 ATYEGEWCRGRPHGKGTLKWPDGRNHVGNFCQGLEHGFGIRLLPQAsedkfDCYKCHWREGSMCGYGICEYSTDEVYKGY 435
Cdd:PLN03185  55 ATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNG-----DVFEGSWIQGLQEGPGKYTWANGNVYLGD 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33359215  436 FQEGLRHGFGVLE--SGPqapqpfRYTGHWERGQRSGYGIEEDGDrGERYIGMWQAGQRHGPGV 497
Cdd:PLN03185 130 MKGGKMSGKGTLTwvSGD------SYEGQWLDGMMHGFGVYTWSD-GGCYVGTWTRGLKDGKGV 186
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 407-567 4.25e-06

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 50.60  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215  407 DCYKCHWREGSMCGYGICEYSTDEVYKGYFQEGLRHGFGVLesgpQAPQPFRYTGHWERGQRSGYGIEEDGDrGERYIGM 486
Cdd:PLN03185   9 DFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKI----SWPSGATYEGEFSGGYMHGSGTYTGTD-GTTYKGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215  487 WQAGQRHGPGVMVTQAGVCYQGTFQADKTVGPGILLSEDDSLYEGTFtRDLTLMGKGKVTFPNGFTLEGSFGSGA--GRG 564
Cdd:PLN03185  84 WRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDM-KGGKMSGKGTLTWVSGDSYEGQWLDGMmhGFG 162


                 ...
gi 33359215  565 LHT 567
Cdd:PLN03185 163 VYT 165
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 358-378 4.81e-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: 4.81e-05
                          10        20
                  ....*....|....*....|.
gi 33359215   358 YEGEWCRGRPHGKGTLKWPDG 378
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
356-377 3.35e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 38.48  E-value: 3.35e-04
                           10        20
                   ....*....|....*....|..
gi 33359215    356 ATYEGEWCRGRPHGKGTLKWPD 377
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 503-567 7.61e-04

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 43.28  E-value: 7.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33359215  503 GVCYQGTFQADKTVGPGILLSEDDSLYEGTFTRDLTlMGKGKVTFPNGFTLEGSFGSGAGRGLHT 567
Cdd:PLN03185   8 GDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMR-HGNGKISWPSGATYEGEFSGGYMHGSGT 71
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
445-564 1.33e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 41.87  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33359215 445 GVLESGPQAPQPFRYTGHWERGQRSGYGIEEDGDRGErYIGMWQAGQRHGPGVMVTQAGVCYQGTFQAD----------- 513
Cdd:COG4642  32 EGGGGLGTLPGGGGYGGGADGGGGGGGGTGVAGGGGG-EGGVTAAGGGGGGGGGKGDGGDGGGGEGGFGggggggggkkg 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 33359215 514 -KTVGPGILLSEDDSLYEGTFTRDLTlMGKGKVTFPNGFTLEGSFGSG--AGRG 564
Cdd:COG4642 111 gGGGGGGVLEGDDGGGYGGGTADGGR-GGGGIYTFPNGDVYEGEFKNGkpHGQG 163
 
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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