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Conserved domains on  [gi|1069932289|ref|XP_018268460|]
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uncharacterized protein RHOBADRAFT_55878 [Rhodotorula graminis WP1]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMP_Mdm34 cd21673
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in mitochondrial ...
1-192 5.31e-106

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: 325.33  E-value: 5.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289   1 MSFNFEWPQFSDDFYADAREMLAQALNKGQKPPIIADRIEVKELNMGTIPPELEILEIGDLSTDRFRGIFRLTYSGDAYI 80
Cdd:cd21673     1 MSFKFNWSPFDPSFYEDIKEALTTALNKGPKPPIIADKISVTELDLGTIPPELEILEIGDLSEDRFKGIFKLEYAGDASI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289  81 VLQTKVQANPLNVP-RPSLDILSSPRILFAAAPLVVPMTLRLSNLSLRAIVVLVVSRQKGITLVFKNDPLESVNVSSSFD 159
Cdd:cd21673    81 VLQTKVQANPLNSItSSSPSFLRTPGFLLANKPLVVPLELTLSNIKLDGIVILVFSKNKGITLVFKNDPLESVKVSSTFD 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1069932289 160 GVDSVAGFIQREIENQLREAFRSDLPSVIHRLS 192
Cdd:cd21673   161 EIPSIANFLQREIENQLRELFKEDLPEIIHELS 193
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
688-870 9.12e-04

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 688 ARSAPYSTSASGISSGAARM--APSAPGTGRVALVHGAGAMPGrPGSAPPAQPVKAVRKRlhrIGSARAASPARNSVPPS 765
Cdd:PRK12323  407 AAAPAAAAAARAVAAAPARRspAPEALAAARQASARGPGGAPA-PAPAPAAAPAAAARPA---AAGPRPVAAAAAAAPAR 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 766 PALLSGVASSSSSSGVGAGSGSGYGGYTPAAPGTVPPRRPGAPLTRASLSRATSPLRSSHLAPSAATQSLPAVAARGLGV 845
Cdd:PRK12323  483 AAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVA 562
                         170       180
                  ....*....|....*....|....*
gi 1069932289 846 GGGGGSGGGGAPSELSDYFPTSGAR 870
Cdd:PRK12323  563 PRPPRASASGLPDMFDGDWPALAAR 587
 
Name Accession Description Interval E-value
SMP_Mdm34 cd21673
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in mitochondrial ...
1-192 5.31e-106

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: 325.33  E-value: 5.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289   1 MSFNFEWPQFSDDFYADAREMLAQALNKGQKPPIIADRIEVKELNMGTIPPELEILEIGDLSTDRFRGIFRLTYSGDAYI 80
Cdd:cd21673     1 MSFKFNWSPFDPSFYEDIKEALTTALNKGPKPPIIADKISVTELDLGTIPPELEILEIGDLSEDRFKGIFKLEYAGDASI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289  81 VLQTKVQANPLNVP-RPSLDILSSPRILFAAAPLVVPMTLRLSNLSLRAIVVLVVSRQKGITLVFKNDPLESVNVSSSFD 159
Cdd:cd21673    81 VLQTKVQANPLNSItSSSPSFLRTPGFLLANKPLVVPLELTLSNIKLDGIVILVFSKNKGITLVFKNDPLESVKVSSTFD 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1069932289 160 GVDSVAGFIQREIENQLREAFRSDLPSVIHRLS 192
Cdd:cd21673   161 EIPSIANFLQREIENQLRELFKEDLPEIIHELS 193
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
688-870 9.12e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 688 ARSAPYSTSASGISSGAARM--APSAPGTGRVALVHGAGAMPGrPGSAPPAQPVKAVRKRlhrIGSARAASPARNSVPPS 765
Cdd:PRK12323  407 AAAPAAAAAARAVAAAPARRspAPEALAAARQASARGPGGAPA-PAPAPAAAPAAAARPA---AAGPRPVAAAAAAAPAR 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 766 PALLSGVASSSSSSGVGAGSGSGYGGYTPAAPGTVPPRRPGAPLTRASLSRATSPLRSSHLAPSAATQSLPAVAARGLGV 845
Cdd:PRK12323  483 AAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVA 562
                         170       180
                  ....*....|....*....|....*
gi 1069932289 846 GGGGGSGGGGAPSELSDYFPTSGAR 870
Cdd:PRK12323  563 PRPPRASASGLPDMFDGDWPALAAR 587
 
Name Accession Description Interval E-value
SMP_Mdm34 cd21673
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in mitochondrial ...
1-192 5.31e-106

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: 325.33  E-value: 5.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289   1 MSFNFEWPQFSDDFYADAREMLAQALNKGQKPPIIADRIEVKELNMGTIPPELEILEIGDLSTDRFRGIFRLTYSGDAYI 80
Cdd:cd21673     1 MSFKFNWSPFDPSFYEDIKEALTTALNKGPKPPIIADKISVTELDLGTIPPELEILEIGDLSEDRFKGIFKLEYAGDASI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289  81 VLQTKVQANPLNVP-RPSLDILSSPRILFAAAPLVVPMTLRLSNLSLRAIVVLVVSRQKGITLVFKNDPLESVNVSSSFD 159
Cdd:cd21673    81 VLQTKVQANPLNSItSSSPSFLRTPGFLLANKPLVVPLELTLSNIKLDGIVILVFSKNKGITLVFKNDPLESVKVSSTFD 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1069932289 160 GVDSVAGFIQREIENQLREAFRSDLPSVIHRLS 192
Cdd:cd21673   161 EIPSIANFLQREIENQLRELFKEDLPEIIHELS 193
SMP_Mdm12 cd21672
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in mitochondrial ...
1-132 2.66e-15

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: 75.56  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289   1 MSFNFEWPQFSDDFYADAREMLAQALNKGQKPPIIADrIEVKELNMGTIPPELEILEIGDLSTDrFRGI---FRLTYSGD 77
Cdd:cd21672     1 MSIDINWEKLDSSLAESLRDFLNRQFQSIPLPSFIGP-IEVTSFDFGSVPPDIEIKDITDPFPE-FYDLqlhLRVSYKGD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1069932289  78 AYIVLQTKVQanpLNVPRPSLDILssprilfaaaplvvPMTLRLSNLSLRAIVVL 132
Cdd:cd21672    79 LRLTLTTELL---LNYPSPSFMSL--------------PIKLSVTGLVFHGLAVV 116
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
18-190 2.88e-06

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: 49.06  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289  18 AREMLAQALNKGQKPPIIaDRIEVKELNMGTIPPELE---ILEIGDLStdRFRGIFRLTYSGDAYIVLQTKVQanpLNVP 94
Cdd:cd21671    45 LLRKLEEALNGERKPSFL-DPIKVTDLDLGDDFPRFSnarIRPSDDSG--GLRAEIDIDYSDTISLGIDTSLL---LNYP 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289  95 RPSldilssprilFAAAPlvVPMTLRLSNLSLRAIVVLVVSRQKGITLvfkndpleSVNVSSSFD---GVDSVAGF---- 167
Cdd:cd21671   119 KPR----------FASLP--VSLSVSLVRFSGTLTIELPSPSSPGPTL--------SFSLLPDFRldlKVSSLIGSrakl 178
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1069932289 168 -----IQREIENQLREAFRS----------DLPSVIHR 190
Cdd:cd21671   179 qdvpkLHSLIESRLRRWFADrcvepnfwkiVLPSLWPS 216
SMP_SF cd21669
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP ...
18-184 9.02e-06

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: 46.93  E-value: 9.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289  18 AREMLAQALNKGQKPPIIaDRIEVKELNMGTIPPELEILEIGDLSTDRFRGIF--RLTYSGDAYIVLQTKVQANPLNvpr 95
Cdd:cd21669     5 IRESLQELLEEVKKPSFI-ESLELTEFTLGSNPPRIKSVRVLDSPSSDLQLVLdlDLEYAGDFSVVLSAKLGGGGLG--- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289  96 psldilssprilfaaaplvVPMTLRLSNLSLRAIVVLVVSR------QKGITLVFKNDPLESVNVSSSFDGVDSVAGFIQ 169
Cdd:cd21669    81 -------------------LPVPVSVSDLSLEGRLRVRLTLlpefpyVGALSISFVEPPDIDFSIRPLGGVDLMELPGLS 141
                         170
                  ....*....|....*
gi 1069932289 170 REIENQLREAFRSDL 184
Cdd:cd21669   142 SWLEKLLTDALVELL 156
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
26-109 1.47e-05

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: 46.72  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289  26 LNKGQKPPIIaDRIEVKELNMGTIPPelEILEIGDLSTDRFRGI---FRLTYSGDAYIVLQTKVqanplNVPRPSLDILS 102
Cdd:cd21675    31 LSKIKLPSFL-GEITVTDLDLGTSVP--VISNPKLPSLDPDGGLwvdLDVSYRGGFSLTLETKL-----NLSKLKKEKVS 102

                  ....*..
gi 1069932289 103 SPRILFA 109
Cdd:cd21675   103 NVPLVLA 109
SMP_SYT cd21677
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in the synaptotagmin ...
7-130 2.47e-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: 42.92  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289   7 WPQFSDDFYADAREMLAQALNKgQKPPIIAdRIEVKELNMGTIPPeleileigdlstdRFRGIfRLTYSGDAYIVLQTKV 86
Cdd:cd21677    23 WPYLDKAASKLVKESVEPLLEQ-YKPSFIS-SIKFKKLTLGTVPP-------------RIEGV-KVVESDEDEVILDVDF 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1069932289  87 Q--ANPlnvprpslDIlssprILFAAAPLVVPMTLRLSNLSLRAIV 130
Cdd:cd21677    87 RwaGDP--------DI-----VLAVKLLPGLSLPVQVKDLQLSGTV 119
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
688-870 9.12e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 688 ARSAPYSTSASGISSGAARM--APSAPGTGRVALVHGAGAMPGrPGSAPPAQPVKAVRKRlhrIGSARAASPARNSVPPS 765
Cdd:PRK12323  407 AAAPAAAAAARAVAAAPARRspAPEALAAARQASARGPGGAPA-PAPAPAAAPAAAARPA---AAGPRPVAAAAAAAPAR 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 766 PALLSGVASSSSSSGVGAGSGSGYGGYTPAAPGTVPPRRPGAPLTRASLSRATSPLRSSHLAPSAATQSLPAVAARGLGV 845
Cdd:PRK12323  483 AAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVA 562
                         170       180
                  ....*....|....*....|....*
gi 1069932289 846 GGGGGSGGGGAPSELSDYFPTSGAR 870
Cdd:PRK12323  563 PRPPRASASGLPDMFDGDWPALAAR 587
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
686-839 1.95e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 686 VTARSAPYSTSASGISSGAARMAPSAPGTGRVALVHGAGAMPGRPGSAPPAQPVKAVrkrlhriGSARAASPARNSVPPS 765
Cdd:PRK07003  362 VTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAA-------AATRAEAPPAAPAPPA 434
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069932289 766 PALLSGVASSSSSSGVGAGSGSGYGGYTPAAPGTVPPRRPGAPLTRASLSRATSPLRSSHLAPSAATQSLPAVA 839
Cdd:PRK07003  435 TADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVP 508
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
706-858 5.20e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.63  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 706 RMAPSAPGTGrvalvhGAGAMPGRPGSAPPAQPVKAVRkrlhrigSARAASPARNSVPPSPALlsgvassssssgvgags 785
Cdd:PRK12323  359 RMLAFRPGQS------GGGAGPATAAAAPVAQPAPAAA-------APAAAAPAPAAPPAAPAA----------------- 408
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1069932289 786 gSGYGGYTPAAPGTVPPRRPGAPLTRASLSRATSPLRSSHLAPSAATQSLPAVAARGLGVGGGGGSGGGGAPS 858
Cdd:PRK12323  409 -APAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAP 480
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
691-871 8.59e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 691 APYSTSASGISSGAARMAPSAPGTGRVALVHGAGAMPGRPGSAPPAQPVKAVRKRlhrigSARAASPARNSVPP---SPA 767
Cdd:PRK07003  359 EPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPK-----AAAAAAATRAEAPPaapAPP 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 768 LLSGVASSSSSSGVGAGSGSGYGGYTPAAPGTVPPRRPGAPLTRASLSRATSPLRSSHLAPSAAtQSLPAVAARGLGVGG 847
Cdd:PRK07003  434 ATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAA-APSAATPAAVPDARA 512
                         170       180
                  ....*....|....*....|....
gi 1069932289 848 GGGSGGGGAPSELSDYFPTSGARE 871
Cdd:PRK07003  513 PAAASREDAPAAAAPPAPEARPPT 536
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
684-814 8.59e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.70  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069932289 684 AHVTARSAPYSTSASGISSGAARMAPSAPGTGRVALVHGAGAMPGRPGSAPPAQPVKAVRKRLHRIGSARAASPARNSVP 763
Cdd:PRK14951  369 AAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALA 448
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1069932289 764 PSPallsgvASSSSSSGVGAGSGSGYGGYTPAAPGTVPPRRPGAPLTRASL 814
Cdd:PRK14951  449 PAP------PAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
 
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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