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Conserved domains on  [gi|45184658|ref|NP_982376|]
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AAL166Cp [Eremothecium gossypii ATCC 10895]

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. ...
 103-427 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: 541.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   103 SFAEGLVVGQLSVIVVLIFFIKFFIFSDGPAKTGggggssaesrssgftgSPLTSTTSRLLSTLiKRGGKEGTEFAEDSE 182
Cdd:pfam10296   2 SFTQGLILGQLSVVLLLIFFIKFFIFGDAPSKDS----------------RASSSAASRRVRTL-SHGGKDSSESSDDLR 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   183 NERT-RQINAILEKTYYDVETHSPESLDWFNVLIAQTIQKFREEALQKDNIVHSLNDFISrkSSQLPNYLDAVKITELDI 261
Cdd:pfam10296  65 NKPSsLQINSILEKTYYNVDTHQPESLDWFNVLIAQTIAQFREEALLKDNILHSLNDFLN--SSELPDYLDKIKITEIDI 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   262 GDDFPIFSNCRIKYSPPLNKKRLEAKIDIDLSDRLTLGIETRLLMNYPKYLTASLPVKLTVSMLRFQACLTVSL--TTAE 339
Cdd:pfam10296 143 GDDFPIFSNCRIIPSPNSNKGRLEAKIDVDLSDRLTLGIETKLLLNYPKPLTAVLPVALTVSIVRFSGCLTVSLipTTAE 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   340 EFVPTMAATT--DTDAGDSEGHYLVFSFSPDYRMEFDIKSLIGARSKLENIPKISSLVEYQIKKWFMDRCVEPRFQFVKL 417
Cdd:pfam10296 223 EFVSPTSTNSsdEDDAEDNNGTALMFSFLPDYRLEFSVKSLIGSRSKLQDVPKIASLIESRIKKWFDERCVEPRFQVIKL 302

                         330
                  ....*....|
gi 45184658   418 PSMWPRSKNT 427
Cdd:pfam10296 303 PSLWPRSKNT 312
 
Name Accession Description Interval E-value
MMM1 pfam10296
Maintenance of mitochondrial morphology protein 1; MMM1 is conserved from plants to humans. ...
 103-427 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: 541.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   103 SFAEGLVVGQLSVIVVLIFFIKFFIFSDGPAKTGggggssaesrssgftgSPLTSTTSRLLSTLiKRGGKEGTEFAEDSE 182
Cdd:pfam10296   2 SFTQGLILGQLSVVLLLIFFIKFFIFGDAPSKDS----------------RASSSAASRRVRTL-SHGGKDSSESSDDLR 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   183 NERT-RQINAILEKTYYDVETHSPESLDWFNVLIAQTIQKFREEALQKDNIVHSLNDFISrkSSQLPNYLDAVKITELDI 261
Cdd:pfam10296  65 NKPSsLQINSILEKTYYNVDTHQPESLDWFNVLIAQTIAQFREEALLKDNILHSLNDFLN--SSELPDYLDKIKITEIDI 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   262 GDDFPIFSNCRIKYSPPLNKKRLEAKIDIDLSDRLTLGIETRLLMNYPKYLTASLPVKLTVSMLRFQACLTVSL--TTAE 339
Cdd:pfam10296 143 GDDFPIFSNCRIIPSPNSNKGRLEAKIDVDLSDRLTLGIETKLLLNYPKPLTAVLPVALTVSIVRFSGCLTVSLipTTAE 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   340 EFVPTMAATT--DTDAGDSEGHYLVFSFSPDYRMEFDIKSLIGARSKLENIPKISSLVEYQIKKWFMDRCVEPRFQFVKL 417
Cdd:pfam10296 223 EFVSPTSTNSsdEDDAEDNNGTALMFSFLPDYRLEFSVKSLIGSRSKLQDVPKIASLIESRIKKWFDERCVEPRFQVIKL 302

                         330
                  ....*....|
gi 45184658   418 PSMWPRSKNT 427
Cdd:pfam10296 303 PSLWPRSKNT 312
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
 192-423 4.39e-108

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: 318.31  E-value: 4.39e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 192 ILEKTYYDVETHSPESLDWFNVLIAQTIQKFREEALQKDNIVHSLNDFISRKssQLPNYLDAVKITELDIGDDFPIFSNC 271
Cdd:cd21671   5 ILKKTFYDLSEHPPESLDWLNVLLAQILAQYRSDAEGDDNLLRKLEEALNGE--RKPSFLDPIKVTDLDLGDDFPRFSNA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 272 RIKYSPplNKKRLEAKIDIDLSDRLTLGIETRLLMNYPKYLTASLPVKLTVSMLRFQACLTVSLTTAeefvptmaattdt 351
Cdd:cd21671  83 RIRPSD--DSGGLRAEIDIDYSDTISLGIDTSLLLNYPKPRFASLPVSLSVSLVRFSGTLTIELPSP------------- 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45184658 352 dagDSEGHYLVFSFSPDYRMEFDIKSLIGARSKLENIPKISSLVEYQIKKWFMDRCVEPRFQFVKLPSMWPR 423
Cdd:cd21671 148 ---SSPGPTLSFSLLPDFRLDLKVSSLIGSRAKLQDVPKLHSLIESRLRRWFADRCVEPNFWKIVLPSLWPS 216
 
Name Accession Description Interval E-value
MMM1 pfam10296
Maintenance of mitochondrial morphology protein 1; MMM1 is conserved from plants to humans. ...
 103-427 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: 541.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   103 SFAEGLVVGQLSVIVVLIFFIKFFIFSDGPAKTGggggssaesrssgftgSPLTSTTSRLLSTLiKRGGKEGTEFAEDSE 182
Cdd:pfam10296   2 SFTQGLILGQLSVVLLLIFFIKFFIFGDAPSKDS----------------RASSSAASRRVRTL-SHGGKDSSESSDDLR 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   183 NERT-RQINAILEKTYYDVETHSPESLDWFNVLIAQTIQKFREEALQKDNIVHSLNDFISrkSSQLPNYLDAVKITELDI 261
Cdd:pfam10296  65 NKPSsLQINSILEKTYYNVDTHQPESLDWFNVLIAQTIAQFREEALLKDNILHSLNDFLN--SSELPDYLDKIKITEIDI 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   262 GDDFPIFSNCRIKYSPPLNKKRLEAKIDIDLSDRLTLGIETRLLMNYPKYLTASLPVKLTVSMLRFQACLTVSL--TTAE 339
Cdd:pfam10296 143 GDDFPIFSNCRIIPSPNSNKGRLEAKIDVDLSDRLTLGIETKLLLNYPKPLTAVLPVALTVSIVRFSGCLTVSLipTTAE 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658   340 EFVPTMAATT--DTDAGDSEGHYLVFSFSPDYRMEFDIKSLIGARSKLENIPKISSLVEYQIKKWFMDRCVEPRFQFVKL 417
Cdd:pfam10296 223 EFVSPTSTNSsdEDDAEDNNGTALMFSFLPDYRLEFSVKSLIGSRSKLQDVPKIASLIESRIKKWFDERCVEPRFQVIKL 302

                         330
                  ....*....|
gi 45184658   418 PSMWPRSKNT 427
Cdd:pfam10296 303 PSLWPRSKNT 312
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
 192-423 4.39e-108

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: 318.31  E-value: 4.39e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 192 ILEKTYYDVETHSPESLDWFNVLIAQTIQKFREEALQKDNIVHSLNDFISRKssQLPNYLDAVKITELDIGDDFPIFSNC 271
Cdd:cd21671   5 ILKKTFYDLSEHPPESLDWLNVLLAQILAQYRSDAEGDDNLLRKLEEALNGE--RKPSFLDPIKVTDLDLGDDFPRFSNA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 272 RIKYSPplNKKRLEAKIDIDLSDRLTLGIETRLLMNYPKYLTASLPVKLTVSMLRFQACLTVSLTTAeefvptmaattdt 351
Cdd:cd21671  83 RIRPSD--DSGGLRAEIDIDYSDTISLGIDTSLLLNYPKPRFASLPVSLSVSLVRFSGTLTIELPSP------------- 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45184658 352 dagDSEGHYLVFSFSPDYRMEFDIKSLIGARSKLENIPKISSLVEYQIKKWFMDRCVEPRFQFVKLPSMWPR 423
Cdd:cd21671 148 ---SSPGPTLSFSLLPDFRLDLKVSSLIGSRAKLQDVPKLHSLIESRLRRWFADRCVEPNFWKIVLPSLWPS 216
SMP_SF cd21669
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP ...
 229-415 3.36e-18

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: 81.60  E-value: 3.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 229 KDNIVHSLNDFISRKssQLPNYLDAVKITELDIGDDFPIFSNCRIkYSPPLNKKRLEAKIDIDLSDRLTLGIETRLLMNy 308
Cdd:cd21669   2 EQLIRESLQELLEEV--KKPSFIESLELTEFTLGSNPPRIKSVRV-LDSPSSDLQLVLDLDLEYAGDFSVVLSAKLGGG- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 309 pkylTASLPVKLTVSMLRFQACLTVSLTTAEEFvPTMAAttdtdagdseghyLVFSFSPDYRMEFDIKSLIGarSKLENI 388
Cdd:cd21669  78 ----GLGLPVPVSVSDLSLEGRLRVRLTLLPEF-PYVGA-------------LSISFVEPPDIDFSIRPLGG--VDLMEL 137

                       170       180
                ....*....|....*....|....*..
gi 45184658 389 PKISSLVEYQIKKWFMDRCVEPRFQFV 415
Cdd:cd21669 138 PGLSSWLEKLLTDALVELLVEPNRIVI 164
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 210-410 3.23e-14

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: 70.60  E-value: 3.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 210 WFNVLIAqtiqkfR--EEALQKDNIVHSLNDFISRKSS--QLPNYLDAVKITELDIGDDFPIFSNCRIkysPPLNKKRlE 285
Cdd:cd21675   1 WLNALLG------RlfFDFLRTKYWKEFIKEKIQKKLSkiKLPSFLGEITVTDLDLGTSVPVISNPKL---PSLDPDG-G 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 286 AKIDIDLSDR--LTLGIETRL-LMNYPKYLTASLPVKLTVSMLRFQACLTVSLttaeefvptmaattdtdaGDSEGHYLV 362
Cdd:cd21675  71 LWVDLDVSYRggFSLTLETKLnLSKLKKEKVSNVPLVLAVEVKSLSGTLRLNI------------------KPPPSNRLW 132

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 45184658 363 FSFSPDYRMEFDIKSLIGARSKleNIPKISSLVEYQIKKWFMDRCVEP 410
Cdd:cd21675 133 YGFREMPKLELEIEPVVGERQV--TLPHVTNWIEKKLKEEIKESLVLP 178
SMP_PDZD8 cd21674
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ ...
 206-402 1.49e-11

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: 62.95  E-value: 1.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 206 ESLDWFNVLIAQTIQKFREEALQKDNIVHSLN----DFISRKSSQlpNYLDAVKITELDIGDDFPIFSNCRIKySPPLNK 281
Cdd:cd21674   1 ESCVWLNLLFQFLFQELRDTKRVRRWVTKKLNvefeELLKTKTAG--KFLESITVRDLSLGTSFPVIKNVTVI-NVKLSE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 282 -----KRLEAKIDIDLSDRLTLGIETRLLMNYPKYLtaSLPVKLTVSMLRFQacltvsLTTAEEfvPTMAattdtdagds 356
Cdd:cd21674  78 dedvpEELDLALDLEYSGGFQLAIDVDLVFGKSAYL--SIKVVKLSGRLRLQ------FSRLPY--THWS---------- 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 45184658 357 eghylvFSFSPDYRMEFDIKSLIGARSklenIPKISSLVEYQIKKW 402
Cdd:cd21674 138 ------FSFYEEPIIEFDVESRFEGRQ----LPQLTSLIINQIRRV 173
SMP_Mdm12 cd21672
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in mitochondrial ...
 230-413 1.83e-11

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: 63.24  E-value: 1.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 230 DNIVHSLNDFISrkSSQLPNYLDAVKITEL------------DIGDDFPIFSN----CRIKYSpplnkkrleakididlS 293
Cdd:cd21672  16 ESLRDFLNRQFQ--SIPLPSFIGPIEVTSFdfgsvppdieikDITDPFPEFYDlqlhLRVSYK----------------G 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 294 DrLTLGIETRLLMNYPKYLTASLPVKLTVSMLRFQACLTVSLttaEE------FVPTMAATTDTDAGDSEGHYLVFSFSP 367
Cdd:cd21672  78 D-LRLTLTTELLLNYPSPSFMSLPIKLSVTGLVFHGLAVVAY---IGkrvhfcFLEDEDDEAPAGDDSSGPTRSAKPLPE 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 45184658 368 DYRM--EFDIKSLIGARSK--LENIPKISSLVEYQIKKWFMDRCVEPRFQ 413
Cdd:cd21672 154 GISLlpDIKIESEIGEADKhvLKNVGKVEKFILEQLRKILEDELVFPSFI 203
SMP_ESyt cd21670
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain of the extended ...
 206-301 2.44e-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: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45184658 206 ESLDWFNVLIAQ---TIQKFREEALqKDNIVHSLNDfisrkssQLPNYLDAVKITELDIGDDFPIFSNCRIkYSPPLNKK 282
Cdd:cd21670   1 ERAEWLNKIIKQlwpYINEYVEKLL-KEKIEPSIRA-------LLPGPLKSFRFEKIDLGDKPPRIGGVKV-YTDNVDRD 71

                        90       100
                ....*....|....*....|....*....
gi 45184658 283 RL----------EAKIDIDLSDRLTLGIE 301
Cdd:cd21670  72 EIildldisydgDADIEVSVGTGIKAGIK 100
 
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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