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Conserved domains on  [gi|259496078|sp|A3LSW7|]
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RecName: Full=Maintenance of mitochondrial morphology protein 1

Protein Classification

maintenance of mitochondrial morphology protein 1( domain architecture ID 10563307)

maintenance of mitochondrial morphology protein 1 (MMM1) is a component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MMM1 pfam10296
Maintenance of mitochondrial morphology protein 1; MMM1 is conserved from plants to humans. ...
 75-426 0e+00

Maintenance of mitochondrial morphology protein 1; MMM1 is conserved from plants to humans. MMM1 is an integral ER protein. It is N-glycosylated, and forms a complex with Mdm10, Mdm12and Mdm34 to tether the mitochondria to the endoplasmic reticulum.


:

Pssm-ID: 431202  Cd Length: 312  Bit Score: 560.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078   75 WSFTQGLIVGQLSVVFVIVIFIKFFVFAESSPALAKSSITKDASVVIVKRDKKDQSSSDDADPdddsETTASNAKVAAIL 154
Cdd:pfam10296   1 WSFTQGLILGQLSVVLLLIFFIKFFIFGDAPSKDSRASSSAASRRVRTLSHGGKDSSESSDDL----RNKPSSLQINSIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078  155 EKTYYDVDNHSPESLDWFNVLVAQTIAQLRSEALLSDNIYHSLNNFLLKSELPEYLDKINLTEIDIGDDFPIFSNCRIKH 234
Cdd:pfam10296  77 EKTYYNVDTHQPESLDWFNVLIAQTIAQFREEALLKDNILHSLNDFLNSSELPDYLDKIKITEIDIGDDFPIFSNCRIIP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078  235 SKD-GSGRLEAKIDVDLSDTLTLGIETKLLLNHPRPLTAVLPVQLSVSMVRFSGCLTVSLINTADPEFAelsahnspepg 313
Cdd:pfam10296 157 SPNsNKGRLEAKIDVDLSDRLTLGIETKLLLNYPKPLTAVLPVALTVSIVRFSGCLTVSLIPTTAEEFV----------- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078  314 epmsrshsagspggdsshdevistpdSSSHTAQRKHSKDDPNDGTALMFSFSPDYRLEFTVKSLIGARAKLQDVPKISSL 393
Cdd:pfam10296 226 --------------------------SPTSTNSSDEDDAEDNNGTALMFSFLPDYRLEFSVKSLIGSRSKLQDVPKIASL 279

                         330       340       350
                  ....*....|....*....|....*....|...
gi 259496078  394 IENRLRAWFIERCIEPRFQVVRLPSLWPRRKNT 426
Cdd:pfam10296 280 IESRIKKWFDERCVEPRFQVIKLPSLWPRSKNT 312
 
Name Accession Description Interval E-value
MMM1 pfam10296
Maintenance of mitochondrial morphology protein 1; MMM1 is conserved from plants to humans. ...
 75-426 0e+00

Maintenance of mitochondrial morphology protein 1; MMM1 is conserved from plants to humans. MMM1 is an integral ER protein. It is N-glycosylated, and forms a complex with Mdm10, Mdm12and Mdm34 to tether the mitochondria to the endoplasmic reticulum.


Pssm-ID: 431202  Cd Length: 312  Bit Score: 560.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078   75 WSFTQGLIVGQLSVVFVIVIFIKFFVFAESSPALAKSSITKDASVVIVKRDKKDQSSSDDADPdddsETTASNAKVAAIL 154
Cdd:pfam10296   1 WSFTQGLILGQLSVVLLLIFFIKFFIFGDAPSKDSRASSSAASRRVRTLSHGGKDSSESSDDL----RNKPSSLQINSIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078  155 EKTYYDVDNHSPESLDWFNVLVAQTIAQLRSEALLSDNIYHSLNNFLLKSELPEYLDKINLTEIDIGDDFPIFSNCRIKH 234
Cdd:pfam10296  77 EKTYYNVDTHQPESLDWFNVLIAQTIAQFREEALLKDNILHSLNDFLNSSELPDYLDKIKITEIDIGDDFPIFSNCRIIP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078  235 SKD-GSGRLEAKIDVDLSDTLTLGIETKLLLNHPRPLTAVLPVQLSVSMVRFSGCLTVSLINTADPEFAelsahnspepg 313
Cdd:pfam10296 157 SPNsNKGRLEAKIDVDLSDRLTLGIETKLLLNYPKPLTAVLPVALTVSIVRFSGCLTVSLIPTTAEEFV----------- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078  314 epmsrshsagspggdsshdevistpdSSSHTAQRKHSKDDPNDGTALMFSFSPDYRLEFTVKSLIGARAKLQDVPKISSL 393
Cdd:pfam10296 226 --------------------------SPTSTNSSDEDDAEDNNGTALMFSFLPDYRLEFSVKSLIGSRSKLQDVPKIASL 279

                         330       340       350
                  ....*....|....*....|....*....|...
gi 259496078  394 IENRLRAWFIERCIEPRFQVVRLPSLWPRRKNT 426
Cdd:pfam10296 280 IESRIKKWFDERCVEPRFQVIKLPSLWPRSKNT 312
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
 150-422 1.55e-107

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of mitochondrial morphology protein 1 (Mmm1) and similar proteins; Maintenance of mitochondrial morphology protein 1 (Mmm1), also called mitochondrial outer membrane protein Mmm1, or yeast mitochondrial escape protein 6 (YME6), is a mitochondrial outer membrane protein essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. It is a component of the ER-mitochondrion encounter structure/ mitochondrial distribution and morphology (ERMES/Mdm) complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The Mdm12-Mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The Mdm10-Mdm12-Mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the Mdm12-Mmm1 complex. This model corresponds to the SMP domain of Mmm1, which may be implicated in lipid transport.


Pssm-ID: 439227  Cd Length: 216  Bit Score: 316.77  E-value: 1.55e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 150 VAAILEKTYYDVDNHSPESLDWFNVLVAQTIAQLRSEALLSDNIYHSLNNFLLKSELPEYLDKINLTEIDIGDDFPIFSN 229
Cdd:cd21671    2 LSDILKKTFYDLSEHPPESLDWLNVLLAQILAQYRSDAEGDDNLLRKLEEALNGERKPSFLDPIKVTDLDLGDDFPRFSN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 230 CRIKHSkDGSGRLEAKIDVDLSDTLTLGIETKLLLNHPRPLTAVLPVQLSVSMVRFSGCLTVSLINTadpefaelsahns 309
Cdd:cd21671   82 ARIRPS-DDSGGLRAEIDIDYSDTISLGIDTSLLLNYPKPRFASLPVSLSVSLVRFSGTLTIELPSP------------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 310 pepgepmsrshsagspggdsshdevistpdssshtaqrkhskddPNDGTALMFSFSPDYRLEFTVKSLIGARAKLQDVPK 389
Cdd:cd21671  148 --------------------------------------------SSPGPTLSFSLLPDFRLDLKVSSLIGSRAKLQDVPK 183

                        250       260       270
                 ....*....|....*....|....*....|...
gi 259496078 390 ISSLIENRLRAWFIERCIEPRFQVVRLPSLWPR 422
Cdd:cd21671  184 LHSLIESRLRRWFADRCVEPNFWKIVLPSLWPS 216
 
Name Accession Description Interval E-value
MMM1 pfam10296
Maintenance of mitochondrial morphology protein 1; MMM1 is conserved from plants to humans. ...
 75-426 0e+00

Maintenance of mitochondrial morphology protein 1; MMM1 is conserved from plants to humans. MMM1 is an integral ER protein. It is N-glycosylated, and forms a complex with Mdm10, Mdm12and Mdm34 to tether the mitochondria to the endoplasmic reticulum.


Pssm-ID: 431202  Cd Length: 312  Bit Score: 560.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078   75 WSFTQGLIVGQLSVVFVIVIFIKFFVFAESSPALAKSSITKDASVVIVKRDKKDQSSSDDADPdddsETTASNAKVAAIL 154
Cdd:pfam10296   1 WSFTQGLILGQLSVVLLLIFFIKFFIFGDAPSKDSRASSSAASRRVRTLSHGGKDSSESSDDL----RNKPSSLQINSIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078  155 EKTYYDVDNHSPESLDWFNVLVAQTIAQLRSEALLSDNIYHSLNNFLLKSELPEYLDKINLTEIDIGDDFPIFSNCRIKH 234
Cdd:pfam10296  77 EKTYYNVDTHQPESLDWFNVLIAQTIAQFREEALLKDNILHSLNDFLNSSELPDYLDKIKITEIDIGDDFPIFSNCRIIP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078  235 SKD-GSGRLEAKIDVDLSDTLTLGIETKLLLNHPRPLTAVLPVQLSVSMVRFSGCLTVSLINTADPEFAelsahnspepg 313
Cdd:pfam10296 157 SPNsNKGRLEAKIDVDLSDRLTLGIETKLLLNYPKPLTAVLPVALTVSIVRFSGCLTVSLIPTTAEEFV----------- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078  314 epmsrshsagspggdsshdevistpdSSSHTAQRKHSKDDPNDGTALMFSFSPDYRLEFTVKSLIGARAKLQDVPKISSL 393
Cdd:pfam10296 226 --------------------------SPTSTNSSDEDDAEDNNGTALMFSFLPDYRLEFSVKSLIGSRSKLQDVPKIASL 279

                         330       340       350
                  ....*....|....*....|....*....|...
gi 259496078  394 IENRLRAWFIERCIEPRFQVVRLPSLWPRRKNT 426
Cdd:pfam10296 280 IESRIKKWFDERCVEPRFQVIKLPSLWPRSKNT 312
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
 150-422 1.55e-107

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of mitochondrial morphology protein 1 (Mmm1) and similar proteins; Maintenance of mitochondrial morphology protein 1 (Mmm1), also called mitochondrial outer membrane protein Mmm1, or yeast mitochondrial escape protein 6 (YME6), is a mitochondrial outer membrane protein essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. It is a component of the ER-mitochondrion encounter structure/ mitochondrial distribution and morphology (ERMES/Mdm) complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The Mdm12-Mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The Mdm10-Mdm12-Mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the Mdm12-Mmm1 complex. This model corresponds to the SMP domain of Mmm1, which may be implicated in lipid transport.


Pssm-ID: 439227  Cd Length: 216  Bit Score: 316.77  E-value: 1.55e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 150 VAAILEKTYYDVDNHSPESLDWFNVLVAQTIAQLRSEALLSDNIYHSLNNFLLKSELPEYLDKINLTEIDIGDDFPIFSN 229
Cdd:cd21671    2 LSDILKKTFYDLSEHPPESLDWLNVLLAQILAQYRSDAEGDDNLLRKLEEALNGERKPSFLDPIKVTDLDLGDDFPRFSN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 230 CRIKHSkDGSGRLEAKIDVDLSDTLTLGIETKLLLNHPRPLTAVLPVQLSVSMVRFSGCLTVSLINTadpefaelsahns 309
Cdd:cd21671   82 ARIRPS-DDSGGLRAEIDIDYSDTISLGIDTSLLLNYPKPRFASLPVSLSVSLVRFSGTLTIELPSP------------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 310 pepgepmsrshsagspggdsshdevistpdssshtaqrkhskddPNDGTALMFSFSPDYRLEFTVKSLIGARAKLQDVPK 389
Cdd:cd21671  148 --------------------------------------------SSPGPTLSFSLLPDFRLDLKVSSLIGSRAKLQDVPK 183

                        250       260       270
                 ....*....|....*....|....*....|...
gi 259496078 390 ISSLIENRLRAWFIERCIEPRFQVVRLPSLWPR 422
Cdd:cd21671  184 LHSLIESRLRRWFADRCVEPNFWKIVLPSLWPS 216
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 171-409 1.71e-12

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed protein 2 (TEX2) and similar proteins; testis-expressed protein 2 (TEX2), also called transmembrane protein 96 (TMEM96), is a transmembrane protein with uncharacterized biological function. Diseases associated with TEX2 include Wernicke-Korsakoff Syndrome. This model corresponds to the SMP domain of TEX2, which may be implicated in lipid transport.


Pssm-ID: 439231  Cd Length: 186  Bit Score: 65.59  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 171 WFNVLVAQTIAQLRSEALLSDNIYHSLNNFLLKSELPEYLDKINLTEIDIGDDFPIFSNCRIKHSkDGSGRLEAKIDVDL 250
Cdd:cd21675    1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSL-DPDGGLWVDLDVSY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 251 SDTLTLGIETKLLLN-HPRPLTAVLPVQLSVSMVRFSGCLTVslintadpefaelsahNSPEPgePMSRshsagspggds 329
Cdd:cd21675   80 RGGFSLTLETKLNLSkLKKEKVSNVPLVLAVEVKSLSGTLRL----------------NIKPP--PSNR----------- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 330 shdevistpdssshtaqrkhskddpndgtaLMFSFSPDYRLEFTVKSLIGARAKlqDVPKISSLIENRLRAWFIERCIEP 409
Cdd:cd21675  131 ------------------------------LWYGFREMPKLELEIEPVVGERQV--TLPHVTNWIEKKLKEEIKESLVLP 178
SMP_SF cd21669
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP ...
 189-414 6.75e-12

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP domain is a lipid transport domain found in phospholipid transfer proteins such as synaptotagmin family proteins, tricalbin (TCB) family proteins, maintenance of mitochondrial morphology protein 1 (MMM1), mitochondrial distribution and morphology protein 12 (MDM12), mitochondrial distribution and morphology protein 34 (MDM34), PDZ domain-containing protein 8 (PDZD8), testis-expressed protein 2 (TEX2), meiotically up-regulated gene 190 protein (Mug190), C2 domain-containing protein 2 (C2CD2) and C2 domain-containing protein 2-like (C2CD2L). The SMP domain belongs to a superfamily of lipid/hydrophobic ligand-binding domains called TULIP (tubular lipid-binding proteins). It adopts a TULIP fold with two alpha helices and a highly curved antiparallel beta sheet forming a cornucopia-like structure.


Pssm-ID: 439225  Cd Length: 165  Bit Score: 63.49  E-value: 6.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 189 LSDNIYHSLNNFLLKSELPEYLDKINLTEIDIGDDFPIFSNCRIKHSKDGSGRLEAKIDVDLSDTLTLGIETKLLLNhpr 268
Cdd:cd21669    1 LEQLIRESLQELLEEVKKPSFIESLELTEFTLGSNPPRIKSVRVLDSPSSDLQLVLDLDLEYAGDFSVVLSAKLGGG--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 269 plTAVLPVQLSVSMVRFSGCLTVSLINTADPEFaelsahnspepgepmsrshsagspggdsshdevistpdssshtaqrk 348
Cdd:cd21669   78 --GLGLPVPVSVSDLSLEGRLRVRLTLLPEFPY----------------------------------------------- 108

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259496078 349 hskddpndGTALMFSFSPDYRLEFTVKSLIGARakLQDVPKISSLIENRLRAWFIERCIEPRFQVV 414
Cdd:cd21669  109 --------VGALSISFVEPPDIDFSIRPLGGVD--LMELPGLSSWLEKLLTDALVELLVEPNRIVI 164
SMP_Mdm12 cd21672
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in mitochondrial ...
 189-295 1.28e-08

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in mitochondrial distribution and morphology protein 12 (Mdm12) and similar proteins; Mitochondrial distribution and morphology protein 12 (Mdm12), also called mitochondrial inheritance component Mdm12, acts as a component of the endoplasmic reticulum-mitochondria encounter structure (ERMES)/Mdm complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the endoplasmic reticulum (ER) and mitochondria. Mdm12 is required for the interaction of the ER-resident membrane protein Mmm1 and the outer mitochondrial membrane-resident beta-barrel protein Mdm10. The Mdm12-Mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The Mdm10-Mdm12-Mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the Mdm12-Mmm1 complex. This model corresponds to the SMP domain of Mdm12, which adopts a head-to-head and tail-to-tail dimer configuration rather than existing solely as a monomer. It may be implicated in lipid transport.


Pssm-ID: 439228  Cd Length: 206  Bit Score: 54.76  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 189 LSDNIYHSLNNFLLKSELPEYLDKINLTE------------IDIGDDFPIFSN----CRIKHSKDgsgrleakidvdlsd 252
Cdd:cd21672   14 LAESLRDFLNRQFQSIPLPSFIGPIEVTSfdfgsvppdieiKDITDPFPEFYDlqlhLRVSYKGD--------------- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 259496078 253 tLTLGIETKLLLNHPRPLTAVLPVQLSVSMVRFSGCLTVSLIN 295
Cdd:cd21672   79 -LRLTLTTELLLNYPSPSFMSLPIKLSVTGLVFHGLAVVAYIG 120
SMP_PDZD8 cd21674
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ ...
 167-401 5.91e-06

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZ domain-containing protein 8 (PDZD8), also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondria membranes. PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for ER-mitochondria Ca(2+) transfer. In neurons, PDZD8 is involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons. It plays an indirect role in the regulation of cell morphology and cytoskeletal organization. PDZD8 is also a novel Gag-interacting factor that promotes retroviral infection. It may act as a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1 (HSV1). This model corresponds to the SMP domain of PDZD8, which may be implicated in lipid transport.


Pssm-ID: 439230  Cd Length: 191  Bit Score: 46.77  E-value: 5.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 167 ESLDWFNVLVAQTIAQLRSEALLSDNIYHSLN---NFLLK-SELPEYLDKINLTEIDIGDDFPIFSNCRIKHSK-----D 237
Cdd:cd21674    1 ESCVWLNLLFQFLFQELRDTKRVRRWVTKKLNvefEELLKtKTAGKFLESITVRDLSLGTSFPVIKNVTVINVKlsedeD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 238 GSGRLEAKIDVDLSDTLTLGIETKLLLNHprpltavlPVQLSVSMVRFSGCLTVSLinTADPEfaelsAHNSpepgepms 317
Cdd:cd21674   81 VPEELDLALDLEYSGGFQLAIDVDLVFGK--------SAYLSIKVVKLSGRLRLQF--SRLPY-----THWS-------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 318 rshsagspggdsshdevistpdssshtaqrkhskddpndgtalmFSFSPDYRLEFTVKSLIGARAklqdVPKISSLIENR 397
Cdd:cd21674  138 --------------------------------------------FSFYEEPIIEFDVESRFEGRQ----LPQLTSLIINQ 169


                 ....
gi 259496078 398 LRAW 401
Cdd:cd21674  170 IRRV 173
SMP_ESyt cd21670
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain of the extended ...
 167-301 2.23e-04

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain of the extended synaptotagmin (E-Syt) family; The extended synaptotagmin (E-Syt) family includes a group of Ca2+-regulated intrinsic membrane proteins, such as E-Syt1, E-Syt2 and E-Syt3. They are composed of an N-terminal endoplasmic reticulum (ER)-membrane anchor, a central SMP-domain, and five (E-Syt1) or three C-terminal cytoplasmic C2-domains (E-Syt2 and E-Syt3). The ER-membrane anchor and C2 domains are required for tethering, while the SMP domain is a lipid-binding domain that links the ER with other lipid bilayer-membranes within the cell. This model corresponds to the SMP domain, which has a beta-barrel structure like protein modules in the tubular-lipid-binding (TULIP) superfamily. It dimerizes to form an approximately 90-Angstrom-long cylinder traversed by a channel lined entirely with hydrophobic residues. The following two C2 domains then form arched structures flexibly linked to the SMP domain.


Pssm-ID: 439226  Cd Length: 177  Bit Score: 41.77  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259496078 167 ESLDWFNVLVAQTIAQLRS--EALLSDNIYHSLNnfllkSELPEYLDKINLTEIDIGDDFPIFSNcrIKHSKDGSGRLEA 244
Cdd:cd21670    1 ERAEWLNKIIKQLWPYINEyvEKLLKEKIEPSIR-----ALLPGPLKSFRFEKIDLGDKPPRIGG--VKVYTDNVDRDEI 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259496078 245 KIDVDLS------------DTLTLGIE-------TKLLLnhpRPLTAVLPvqlsvsmvrFSGCLTVSLINTADPEF 301
Cdd:cd21670   74 ILDLDISydgdadievsvgTGIKAGIKdiqlrgtLRIVL---KPLLSELP---------LVGGVQIFFLNPPEIDF 137
 
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.
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