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Conserved domains on  [gi|1039793135|ref|XP_017168843|]
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ALS2 C-terminal-like protein isoform X1 [Mus musculus]

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];
358-557 4.31e-32

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 126.22  E-value: 4.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 358 YDGEWCRAKPHGKGTLKWPDGRNHVGTFYQGLEHGfgiclvpqasedkfdcykchwregrmceYGICEYGTDEVYKGYFQ 437
Cdd:COG4642   104 GGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGG----------------------------GGIYTFPNGDVYEGEFK 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 438 AGLRHGFGILESAPQApqpfRYTGHWERGQRSGYGIEEDRDrGERYIGMWQADQRHGPGVVVTQAGVCYQGTFQGDKMAG 517
Cdd:COG4642   156 NGKPHGQGTLTYADGD----RYEGEFKNGKRHGQGTLTYAN-GDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHG 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039793135 518 PGILLCEDDSLYEGTFTRDLtLLGKGKVTFPNGFTLDGSF 557
Cdd:COG4642   231 QGTLTYADGDRYEGEFKNGK-RHGQGTMTYADGSVYEGEW 269
VPS9 super family cl19569
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 835-937 9.05e-15

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.


The actual alignment was detected with superfamily member pfam02204:

Pssm-ID: 473191  Cd Length: 104  Bit Score: 71.09  E-value: 9.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 835 TATECLQKIITTVHPREKLEVLEKTYGEIEATVSR-----------VLGCkyklpmddllplLIYVVSRARIQHLGAEIH 903
Cdd:pfam02204   3 QAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKsnrdeslgaddLLPI------------LIYVLIRANPPNLYSNLQ 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039793135 904 LIRDMMDPVHTGGLHDFLLTALESCYEHIQKEDM 937
Cdd:pfam02204  71 FISEFRDPDLLSGEEGYYLTTLEAALEFIESLDP 104
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 223-321 1.09e-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: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 223 DVLCSPAHRLLQDSQDIPV-VVTPLR--AERVLLFDDSLVLLQGHNTHTFDLKLVWVKPGQD----KCVLHILTPEEEIS 295
Cdd:cd13269     1 DSLRSPDRRLIRESSTRPLtLQNAGRfsSHWFILFNDALVHAQFSTHHIFPLATLWVEPIPDedsgQNALKITTPEESFT 80

                          90       100
                  ....*....|....*....|....*.
gi 1039793135 296 FCTRDPQGQVVWQWKVTQAVCQALCG 321
Cdd:cd13269    81 LVASTPQEKAEWLRAINQAIDQALNG 106
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
358-557 4.31e-32

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 126.22  E-value: 4.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 358 YDGEWCRAKPHGKGTLKWPDGRNHVGTFYQGLEHGfgiclvpqasedkfdcykchwregrmceYGICEYGTDEVYKGYFQ 437
Cdd:COG4642   104 GGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGG----------------------------GGIYTFPNGDVYEGEFK 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 438 AGLRHGFGILESAPQApqpfRYTGHWERGQRSGYGIEEDRDrGERYIGMWQADQRHGPGVVVTQAGVCYQGTFQGDKMAG 517
Cdd:COG4642   156 NGKPHGQGTLTYADGD----RYEGEFKNGKRHGQGTLTYAN-GDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHG 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039793135 518 PGILLCEDDSLYEGTFTRDLtLLGKGKVTFPNGFTLDGSF 557
Cdd:COG4642   231 QGTLTYADGDRYEGEFKNGK-RHGQGTMTYADGSVYEGEW 269
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 835-937 9.05e-15

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: 71.09  E-value: 9.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 835 TATECLQKIITTVHPREKLEVLEKTYGEIEATVSR-----------VLGCkyklpmddllplLIYVVSRARIQHLGAEIH 903
Cdd:pfam02204   3 QAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKsnrdeslgaddLLPI------------LIYVLIRANPPNLYSNLQ 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039793135 904 LIRDMMDPVHTGGLHDFLLTALESCYEHIQKEDM 937
Cdd:pfam02204  71 FISEFRDPDLLSGEEGYYLTTLEAALEFIESLDP 104
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 357-550 4.14e-14

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 76.80  E-value: 4.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 357 TYDGEWCRAKPHGKGTLKWPDGRNHVGTFYQGLEHGFGICLVPQASedkfdCYKCHWREGRMCEYGICEYGTDEVYKGYF 436
Cdd:PLN03185   33 MYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGT-----TYKGRWRLNLKHGLGYQRYPNGDVFEGSW 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 437 QAGLRHGFGilesapqapqpfRYTghWERGQrsgygieedrdrgeRYIGMWQADQRHGPGVVVTQAGVCYQGTFQGDKMA 516
Cdd:PLN03185  108 IQGLQEGPG------------KYT--WANGN--------------VYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMH 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1039793135 517 GPGILLCEDDSLYEGTFTRDLTlLGKGkVTFPNG 550
Cdd:PLN03185  160 GFGVYTWSDGGCYVGTWTRGLK-DGKG-VFYPAG 191
PH_alsin cd13269
Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...
 223-321 1.09e-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: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 223 DVLCSPAHRLLQDSQDIPV-VVTPLR--AERVLLFDDSLVLLQGHNTHTFDLKLVWVKPGQD----KCVLHILTPEEEIS 295
Cdd:cd13269     1 DSLRSPDRRLIRESSTRPLtLQNAGRfsSHWFILFNDALVHAQFSTHHIFPLATLWVEPIPDedsgQNALKITTPEESFT 80

                          90       100
                  ....*....|....*....|....*.
gi 1039793135 296 FCTRDPQGQVVWQWKVTQAVCQALCG 321
Cdd:cd13269    81 LVASTPQEKAEWLRAINQAIDQALNG 106
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 358-378 1.81e-03

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: 36.62  E-value: 1.81e-03
                          10        20
                  ....*....|....*....|.
gi 1039793135 358 YDGEWCRAKPHGKGTLKWPDG 378
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
356-377 4.54e-03

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 35.39  E-value: 4.54e-03
                           10        20
                   ....*....|....*....|..
gi 1039793135  356 ATYDGEWCRAKPHGKGTLKWPD 377
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
358-557 4.31e-32

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 126.22  E-value: 4.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 358 YDGEWCRAKPHGKGTLKWPDGRNHVGTFYQGLEHGfgiclvpqasedkfdcykchwregrmceYGICEYGTDEVYKGYFQ 437
Cdd:COG4642   104 GGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGG----------------------------GGIYTFPNGDVYEGEFK 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 438 AGLRHGFGILESAPQApqpfRYTGHWERGQRSGYGIEEDRDrGERYIGMWQADQRHGPGVVVTQAGVCYQGTFQGDKMAG 517
Cdd:COG4642   156 NGKPHGQGTLTYADGD----RYEGEFKNGKRHGQGTLTYAN-GDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHG 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039793135 518 PGILLCEDDSLYEGTFTRDLtLLGKGKVTFPNGFTLDGSF 557
Cdd:COG4642   231 QGTLTYADGDRYEGEFKNGK-RHGQGTMTYADGSVYEGEW 269
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
356-510 3.97e-27

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 111.97  E-value: 3.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 356 ATYDGEWCRAKPHGKGTLKWPDGRNHVGTFYQGLEHGfgiclvpqasedkfdcykchwregrmceYGICEYGTDEVYKGY 435
Cdd:COG4642   148 DVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHG----------------------------QGTLTYANGDVYEGE 199

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039793135 436 FQAGLRHGFGILESapqaPQPFRYTGHWERGQRSGYGIEEDRDrGERYIGMWQADQRHGPGVVVTQAGVCYQGTF 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). ...
 835-937 9.05e-15

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: 71.09  E-value: 9.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 835 TATECLQKIITTVHPREKLEVLEKTYGEIEATVSR-----------VLGCkyklpmddllplLIYVVSRARIQHLGAEIH 903
Cdd:pfam02204   3 QAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKsnrdeslgaddLLPI------------LIYVLIRANPPNLYSNLQ 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039793135 904 LIRDMMDPVHTGGLHDFLLTALESCYEHIQKEDM 937
Cdd:pfam02204  71 FISEFRDPDLLSGEEGYYLTTLEAALEFIESLDP 104
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 357-550 4.14e-14

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 76.80  E-value: 4.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 357 TYDGEWCRAKPHGKGTLKWPDGRNHVGTFYQGLEHGFGICLVPQASedkfdCYKCHWREGRMCEYGICEYGTDEVYKGYF 436
Cdd:PLN03185   33 MYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGT-----TYKGRWRLNLKHGLGYQRYPNGDVFEGSW 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 437 QAGLRHGFGilesapqapqpfRYTghWERGQrsgygieedrdrgeRYIGMWQADQRHGPGVVVTQAGVCYQGTFQGDKMA 516
Cdd:PLN03185  108 IQGLQEGPG------------KYT--WANGN--------------VYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMH 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1039793135 517 GPGILLCEDDSLYEGTFTRDLTlLGKGkVTFPNG 550
Cdd:PLN03185  160 GFGVYTWSDGGCYVGTWTRGLK-DGKG-VFYPAG 191
PH_alsin cd13269
Alsin Pleckstrin homology (PH) domain; The ALS2 gene encodes alsin, a GEF, that has dual ...
 223-321 1.09e-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: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 223 DVLCSPAHRLLQDSQDIPV-VVTPLR--AERVLLFDDSLVLLQGHNTHTFDLKLVWVKPGQD----KCVLHILTPEEEIS 295
Cdd:cd13269     1 DSLRSPDRRLIRESSTRPLtLQNAGRfsSHWFILFNDALVHAQFSTHHIFPLATLWVEPIPDedsgQNALKITTPEESFT 80

                          90       100
                  ....*....|....*....|....*.
gi 1039793135 296 FCTRDPQGQVVWQWKVTQAVCQALCG 321
Cdd:cd13269    81 LVASTPQEKAEWLRAINQAIDQALNG 106
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 356-473 1.97e-06

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 51.76  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 356 ATYDGEWCRAKPHGKGTLKWPDGRNHVGTFYQGLEHGFGICLVPQAseDKFD--------------------CYKCHWRE 415
Cdd:PLN03185   55 ATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNG--DVFEgswiqglqegpgkytwangnVYLGDMKG 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039793135 416 GRMCEYGICEYGTDEVYKGYFQAGLRHGFGILESAPQApqpfRYTGHWERGQRSGYGI 473
Cdd:PLN03185  133 GKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGG----CYVGTWTRGLKDGKGV 186
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 459-564 1.50e-05

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 49.06  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793135 459 YTGHWERGQRSGYG--IEEDrdrGERYIGMWQADQRHGPGVVVTQAGVCYQGTFQGDKMAGPGILLCEDDSLYEGTFTRD 536
Cdd:PLN03185   11 YSGSLLGNVPEGPGkyLWSD---GCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLN 87

                          90       100
                  ....*....|....*....|....*...
gi 1039793135 537 LTLlGKGKVTFPNGFTLDGSFSSGTDKG 564
Cdd:PLN03185   88 LKH-GLGYQRYPNGDVFEGSWIQGLQEG 114
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 358-378 1.81e-03

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: 36.62  E-value: 1.81e-03
                          10        20
                  ....*....|....*....|.
gi 1039793135 358 YDGEWCRAKPHGKGTLKWPDG 378
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
356-377 4.54e-03

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 35.39  E-value: 4.54e-03
                           10        20
                   ....*....|....*....|..
gi 1039793135  356 ATYDGEWCRAKPHGKGTLKWPD 377
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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