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Conserved domains on  [gi|85109618|ref|XP_963005|]
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mitochondrial morphology maintaining protein MMM1 [Neurospora crassa OR74A]

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. ...
 13-339 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: 544.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618    13 LSFTQGLILGQLSVVLLLAAFIKFFIFGDPPSPEVVASIRATDRRSRTLAHKKSILSLRETNalqlvqnpalnkkhvLRP 92
Cdd:pfam10296   1 WSFTQGLILGQLSVVLLLIFFIKFFIFGDAPSKDSRASSSAASRRVRTLSHGGKDSSESSDD---------------LRN 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618    93 GPPILTIGSILSKTYYKVDSHQPESLDWFNVLIAQTIAQFRSDAQHDDAILSSLSKALNGTARPDFLDEIKVTELSLGED 172
Cdd:pfam10296  66 KPSSLQINSILEKTYYNVDTHQPESLDWFNVLIAQTIAQFREEALLKDNILHSLNDFLNSSELPDYLDKIKITEIDIGDD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618   173 FPIFSNCRIIPVdedglsfgtgkafdanmATREGARLQARMDVDLSDMITLAVETKLLLNYPKRLSAVLPVALAVSVVRF 252
Cdd:pfam10296 146 FPIFSNCRIIPS-----------------PNSNKGRLEAKIDVDLSDRLTLGIETKLLLNYPKPLTAVLPVALTVSIVRF 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618   253 SGTLSISFIPSNPS-----------------NNEPAKMIFTFLDDYRLDFSIRSLLGSRSRLQDVPKIAQLVESRLHRWF 315
Cdd:pfam10296 209 SGCLTVSLIPTTAEefvsptstnssdeddaeDNNGTALMFSFLPDYRLEFSVKSLIGSRSKLQDVPKIASLIESRIKKWF 288

                         330       340
                  ....*....|....*....|....
gi 85109618   316 DERCVEPRFQEIALPNMWPRKKNT 339
Cdd:pfam10296 289 DERCVEPRFQVIKLPSLWPRSKNT 312
 
Name Accession Description Interval E-value
MMM1 pfam10296
Maintenance of mitochondrial morphology protein 1; MMM1 is conserved from plants to humans. ...
 13-339 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: 544.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618    13 LSFTQGLILGQLSVVLLLAAFIKFFIFGDPPSPEVVASIRATDRRSRTLAHKKSILSLRETNalqlvqnpalnkkhvLRP 92
Cdd:pfam10296   1 WSFTQGLILGQLSVVLLLIFFIKFFIFGDAPSKDSRASSSAASRRVRTLSHGGKDSSESSDD---------------LRN 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618    93 GPPILTIGSILSKTYYKVDSHQPESLDWFNVLIAQTIAQFRSDAQHDDAILSSLSKALNGTARPDFLDEIKVTELSLGED 172
Cdd:pfam10296  66 KPSSLQINSILEKTYYNVDTHQPESLDWFNVLIAQTIAQFREEALLKDNILHSLNDFLNSSELPDYLDKIKITEIDIGDD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618   173 FPIFSNCRIIPVdedglsfgtgkafdanmATREGARLQARMDVDLSDMITLAVETKLLLNYPKRLSAVLPVALAVSVVRF 252
Cdd:pfam10296 146 FPIFSNCRIIPS-----------------PNSNKGRLEAKIDVDLSDRLTLGIETKLLLNYPKPLTAVLPVALTVSIVRF 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618   253 SGTLSISFIPSNPS-----------------NNEPAKMIFTFLDDYRLDFSIRSLLGSRSRLQDVPKIAQLVESRLHRWF 315
Cdd:pfam10296 209 SGCLTVSLIPTTAEefvsptstnssdeddaeDNNGTALMFSFLPDYRLEFSVKSLIGSRSKLQDVPKIASLIESRIKKWF 288

                         330       340
                  ....*....|....*....|....
gi 85109618   316 DERCVEPRFQEIALPNMWPRKKNT 339
Cdd:pfam10296 289 DERCVEPRFQVIKLPSLWPRSKNT 312
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
 98-335 3.04e-113

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: 330.25  E-value: 3.04e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618  98 TIGSILSKTYYKVDSHQPESLDWFNVLIAQTIAQFRSDAQHDDAILSSLSKALNGTARPDFLDEIKVTELSLGEDFPIFS 177
Cdd:cd21671   1 LLSDILKKTFYDLSEHPPESLDWLNVLLAQILAQYRSDAEGDDNLLRKLEEALNGERKPSFLDPIKVTDLDLGDDFPRFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 178 NCRIIPVDEDGlsfgtgkafdanmatregaRLQARMDVDLSDMITLAVETKLLLNYPKRLSAVLPVALAVSVVRFSGTLS 257
Cdd:cd21671  81 NARIRPSDDSG-------------------GLRAEIDIDYSDTISLGIDTSLLLNYPKPRFASLPVSLSVSLVRFSGTLT 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85109618 258 ISFIPSNPSNNEpakMIFTFLDDYRLDFSIRSLLGSRSRLQDVPKIAQLVESRLHRWFDERCVEPRFQEIALPNMWPR 335
Cdd:cd21671 142 IELPSPSSPGPT---LSFSLLPDFRLDLKVSSLIGSRAKLQDVPKLHSLIESRLRRWFADRCVEPNFWKIVLPSLWPS 216
 
Name Accession Description Interval E-value
MMM1 pfam10296
Maintenance of mitochondrial morphology protein 1; MMM1 is conserved from plants to humans. ...
 13-339 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: 544.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618    13 LSFTQGLILGQLSVVLLLAAFIKFFIFGDPPSPEVVASIRATDRRSRTLAHKKSILSLRETNalqlvqnpalnkkhvLRP 92
Cdd:pfam10296   1 WSFTQGLILGQLSVVLLLIFFIKFFIFGDAPSKDSRASSSAASRRVRTLSHGGKDSSESSDD---------------LRN 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618    93 GPPILTIGSILSKTYYKVDSHQPESLDWFNVLIAQTIAQFRSDAQHDDAILSSLSKALNGTARPDFLDEIKVTELSLGED 172
Cdd:pfam10296  66 KPSSLQINSILEKTYYNVDTHQPESLDWFNVLIAQTIAQFREEALLKDNILHSLNDFLNSSELPDYLDKIKITEIDIGDD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618   173 FPIFSNCRIIPVdedglsfgtgkafdanmATREGARLQARMDVDLSDMITLAVETKLLLNYPKRLSAVLPVALAVSVVRF 252
Cdd:pfam10296 146 FPIFSNCRIIPS-----------------PNSNKGRLEAKIDVDLSDRLTLGIETKLLLNYPKPLTAVLPVALTVSIVRF 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618   253 SGTLSISFIPSNPS-----------------NNEPAKMIFTFLDDYRLDFSIRSLLGSRSRLQDVPKIAQLVESRLHRWF 315
Cdd:pfam10296 209 SGCLTVSLIPTTAEefvsptstnssdeddaeDNNGTALMFSFLPDYRLEFSVKSLIGSRSKLQDVPKIASLIESRIKKWF 288

                         330       340
                  ....*....|....*....|....
gi 85109618   316 DERCVEPRFQEIALPNMWPRKKNT 339
Cdd:pfam10296 289 DERCVEPRFQVIKLPSLWPRSKNT 312
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
 98-335 3.04e-113

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: 330.25  E-value: 3.04e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618  98 TIGSILSKTYYKVDSHQPESLDWFNVLIAQTIAQFRSDAQHDDAILSSLSKALNGTARPDFLDEIKVTELSLGEDFPIFS 177
Cdd:cd21671   1 LLSDILKKTFYDLSEHPPESLDWLNVLLAQILAQYRSDAEGDDNLLRKLEEALNGERKPSFLDPIKVTDLDLGDDFPRFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 178 NCRIIPVDEDGlsfgtgkafdanmatregaRLQARMDVDLSDMITLAVETKLLLNYPKRLSAVLPVALAVSVVRFSGTLS 257
Cdd:cd21671  81 NARIRPSDDSG-------------------GLRAEIDIDYSDTISLGIDTSLLLNYPKPRFASLPVSLSVSLVRFSGTLT 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85109618 258 ISFIPSNPSNNEpakMIFTFLDDYRLDFSIRSLLGSRSRLQDVPKIAQLVESRLHRWFDERCVEPRFQEIALPNMWPR 335
Cdd:cd21671 142 IELPSPSSPGPT---LSFSLLPDFRLDLKVSSLIGSRAKLQDVPKLHSLIESRLRRWFADRCVEPNFWKIVLPSLWPS 216
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 120-332 1.02e-21

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: 91.79  E-value: 1.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 120 WFNVLIAQTIAQFRSDAQHDDAILSSLSKALNGTARPDFLDEIKVTELSLGEDFPIFSNCRIIPVDEDGlsfgtGKAFDA 199
Cdd:cd21675   1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSLDPDG-----GLWVDL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 200 NMATREGarlqarmdvdlsdmITLAVETKLLLNYPKRLSAV-LPVALAVSVVRFSGTLSISfIPSNPSNnepaKMIFTFL 278
Cdd:cd21675  76 DVSYRGG--------------FSLTLETKLNLSKLKKEKVSnVPLVLAVEVKSLSGTLRLN-IKPPPSN----RLWYGFR 136

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 85109618 279 DDYRLDFSIRSLLGSRSRlqDVPKIAQLVESRLHRWFDERCVeprfqeiaLPNM 332
Cdd:cd21675 137 EMPKLELEIEPVVGERQV--TLPHVTNWIEKKLKEEIKESLV--------LPNM 180
SMP_SF cd21669
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP ...
 140-327 1.71e-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: 81.98  E-value: 1.71e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 140 DAILSSLSKALNGTARPDFLDEIKVTELSLGEDFPIFSNCRIIPVDEDGLsfgtgkafdanmatregaRLQARMDVDLSD 219
Cdd:cd21669   3 QLIRESLQELLEEVKKPSFIESLELTEFTLGSNPPRIKSVRVLDSPSSDL------------------QLVLDLDLEYAG 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 220 MITLAVETKLLLNYPKrlsavLPVALAVSVVRFSGTLSISFIPSNPSNNePAKMIFTFLDDYRLDFSIRSLLGsrSRLQD 299
Cdd:cd21669  65 DFSVVLSAKLGGGGLG-----LPVPVSVSDLSLEGRLRVRLTLLPEFPY-VGALSISFVEPPDIDFSIRPLGG--VDLME 136

                       170       180
                ....*....|....*....|....*...
gi 85109618 300 VPKIAQLVESRLHRWFDERCVEPRFQEI 327
Cdd:cd21669 137 LPGLSSWLEKLLTDALVELLVEPNRIVI 164
SMP_PDZD8 cd21674
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ ...
 116-314 7.76e-08

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: 52.17  E-value: 7.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 116 ESLDWFNvLIAQTIaqFRsDAQHDDAILSSLSKALNG--------TARPDFLDEIKVTELSLGEDFPIFSNCRII--PVD 185
Cdd:cd21674   1 ESCVWLN-LLFQFL--FQ-ELRDTKRVRRWVTKKLNVefeellktKTAGKFLESITVRDLSLGTSFPVIKNVTVInvKLS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 186 EDGLSFGTgkafdanmatregarLQARMDVDLSDMITLAVETKLLLNYpkrlsavlPVALAVSVVRFSGTLSISFipsnp 265
Cdd:cd21674  77 EDEDVPEE---------------LDLALDLEYSGGFQLAIDVDLVFGK--------SAYLSIKVVKLSGRLRLQF----- 128

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 85109618 266 sNNEP-AKMIFTFLDDYRLDFSIRSLLGSRSrlqdVPKIAQLVESRLHRW 314
Cdd:cd21674 129 -SRLPyTHWSFSFYEEPIIEFDVESRFEGRQ----LPQLTSLIINQIRRV 173
SMP_Mdm12 cd21672
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in mitochondrial ...
 135-280 2.70e-07

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: 50.91  E-value: 2.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 135 DAQHDDAILSSLSKALNGTARPDFLDEIKVTELSLGED------------FPIFSNcriipvdedglsfgtgkafdanma 202
Cdd:cd21672  11 DSSLAESLRDFLNRQFQSIPLPSFIGPIEVTSFDFGSVppdieikditdpFPEFYD------------------------ 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 203 tregarLQARMDVD-LSDM-ITLAVEtkLLLNYPKRLSAVLPVALAVSVVRFSGTLSISFIPSnpsnnepaKMIFTFLDD 280
Cdd:cd21672  67 ------LQLHLRVSyKGDLrLTLTTE--LLLNYPSPSFMSLPIKLSVTGLVFHGLAVVAYIGK--------RVHFCFLED 130
SMP_SYT cd21677
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in the synaptotagmin ...
 116-312 3.16e-04

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in the synaptotagmin family, mostly plants; The synaptotagmin family includes Arabidopsis thaliana synaptotagmins (AtSYT1-5) and similar proteins. AtSYT1, also called NTMC2T1.1, or synaptotagmin A (SYTA), plays an important role in maintaining plasma membrane integrity during freezing and osmotic stresses. It may function in membrane resealing during calcium-dependent freezing tolerance. It regulates endocytosis and endosome recycling at the plasma membrane and cell-to-cell trafficking of cabbage leaf curl virus (CaLCuV) and tobacco mosaic virus (TMV) movement proteins via plasmodesmata. AtSYT2, also called NTMC2T1.2, or synaptotagmin B (SYTB), may play an important role in regulating an unconventional protein trafficking from the cytosol to the extracellular matrix. AtSYT3 (also called NTMC2T1.3, or synaptotagmin C, or SYTC), AtSYT4 (also called NTMC2T2.2, or synaptotagmin D, or SYTD) and AtSYT5 (also called NTMC2T2.1, or synaptotagmin E, or SYTE) may also be involved in membrane trafficking. This model corresponds to the SMP domain of SYT family proteins, which may be implicated in lipid transport.


Pssm-ID: 439233  Cd Length: 189  Bit Score: 41.38  E-value: 3.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 116 ESLDWFNVLIAQ---TIAQFRSDAqhddaILSSLSKALNgTARPDFLDEIKVTELSLGEDFPIFSNCRIIPVDEDGLSfg 192
Cdd:cd21677  10 ERVDWLNKLLEKlwpYLDKAASKL-----VKESVEPLLE-QYKPSFISSIKFKKLTLGTVPPRIEGVKVVESDEDEVI-- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 193 tgkafdanmatregarlqarMDVDL---SDM-ITLAVETKLLlnypkrlsavLPVALAVSVVRFSGTLSISFipsNPSNN 268
Cdd:cd21677  82 --------------------LDVDFrwaGDPdIVLAVKLLPG----------LSLPVQVKDLQLSGTVRITL---KPLVD 128

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 85109618 269 E-P--AKMIFTFLDDYRLDFSIRSLLGSrsrLQDVPKIAQLVESRLH 312
Cdd:cd21677 129 ElPcfGAVSVSLVEKPVVDFDLKLLGGD---DMALPGLKSWLDSFIR 172
SMP_Mdm34 cd21673
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in mitochondrial ...
 140-312 2.23e-03

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in mitochondrial distribution and morphology protein 34 (Mdm34) and similar proteins; Mitochondrial distribution and morphology protein 34 (Mdm34), also called mitochondrial outer membrane protein 2 (Mmm2), is a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids. It is a component of the ERMES/Mdm complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) 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. Mdm34 is essential for the interaction of the ER-resident membrane protein Mmm1 and the outer mitochondrial membrane-resident beta-barrel protein Mdm10. This model corresponds to the SMP domain of Mdm34, which may be implicated in lipid transport.


Pssm-ID: 439229  Cd Length: 193  Bit Score: 39.13  E-value: 2.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 140 DAILSSLSKALNGTARPDFL-DEIKVTELSLGEDFPIFSNCRIIPVDEDGL--SFGTGKAFDANMATRegARLQAR---- 212
Cdd:cd21673  16 EDIKEALTTALNKGPKPPIIaDKISVTELDLGTIPPELEILEIGDLSEDRFkgIFKLEYAGDASIVLQ--TKVQANplns 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85109618 213 MDVDLSDMITLAveTKLLLNYPkrlsAVLPVALAVSVVRFSGTLSISFipsnpSNNEpaKMIFTFLDDYRLDFSIRSLLG 292
Cdd:cd21673  94 ITSSSPSFLRTP--GFLLANKP----LVVPLELTLSNIKLDGIVILVF-----SKNK--GITLVFKNDPLESVKVSSTFD 160

                       170       180
                ....*....|....*....|
gi 85109618 293 SRSRLQDvpKIAQLVESRLH 312
Cdd:cd21673 161 EIPSIAN--FLQREIENQLR 178
 
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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