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Conserved domains on  [gi|1039752523|ref|XP_017172698|]
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MLV-related proviral Env polyprotein-like isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TLV_coat super family cl27694
ENV polyprotein (coat polyprotein);
26-561 8.72e-109

ENV polyprotein (coat polyprotein);


The actual alignment was detected with superfamily member pfam00429:

Pssm-ID: 306850  Cd Length: 560  Bit Score: 337.15  E-value: 8.72e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523  26 ILTLLISIGVVQTSPMPHEPHNLTWVITNTatgtvinstshlapigtWFPDLVFDLCALADGTWD--------------- 90
Cdd:pfam00429   2 ILLILLLLGGSAGFGSPHQVYNLTWQVTNT-----------------WWPTLQPDLCDLAGGGQVswsppctppqsvcsg 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523  91 ---------PLGLVWGCQHPAQHSELRRTPFYVCPGEGRSPQQTATCGGPESYFCAYWGCESTGSISWTPPIKDDLIKVQ 161
Cdd:pfam00429  65 cpdlsayltDQSLWPPCVTPPKRTPHANGSFYVCPGECRTRANRRHCGGYSSCYCCSWGCETTGCTYWTPASSWDYITVS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 162 RSPGSESQGWGYGLQpkldandlggpcssnCNPITVQFTPKGKesvgWEKGKTWGLRLYVSGYDYGVMFTIQLSAR---- 237
Cdd:pfam00429 145 WNKTSSTVNCTQEGS---------------CNPLILHFTDCGK----KATTLTWGLRLYVSGYDPLDTFRIRLKITtlne 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 238 ----QGMPLGPNPALPPVgltvtqsqitVPISQELRPRSGPW--DLLKATYLVLNNSKPELTSKCWLCLDAQPPYYEGIA 311
Cdd:pfam00429 206 vlrdQKPPSQPHPLAPPL----------PRPTSPPGPGTGDRllDLLQGAYLTLNATNPSLTQDCWLCLVSGPPYYEGIA 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 312 VPGNYTTSTDNKDCRWQYPGKgrLTLELIQGKGLCFGTIPHTHRHLCNSIQEAPDRDAYIIPPINTWWACTTGLTSCIHT 391
Cdd:pfam00429 276 PNGSVSNHTSAPACSLGPQLA--LTLSEVTGQGCCIGGIPVGHQALCNTTVSTSSGSHYLCAPNGTVWACGTGLTPCLST 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 392 QALNLTNGFCVLVQLAPRILRYSDEMGTRLSPfPAARAKRATVA-------EILGASAFDFQD-------ENYKVLSSAI 457
Cdd:pfam00429 354 ALLNNTTDYCVLAELLPDISYHPGEPIYAIDE-PAGRFRREPVAltlalllGGLGIAAGVGTGttglvstQQFTSLQHAL 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 458 DADLMELGKSLSKSKTSLTSLREATLRNQREQDFQSLQQDGLCKPLEKRCCTFVDNLKHARELLAKVRKRLEDRKREMEQ 537
Cdd:pfam00429 433 ISDIQALESSINDLEDSLTSLAEVVLQNRRGLDLLFLEQGGLCAALQEECCFYADHSGIVRDSIAKLQERLPQRQRLLTD 512
                         570       580       590
                  ....*....|....*....|....*....|....
gi 1039752523 538 GQ----------PVWITVIATLSGFLGLVILIVI 561
Cdd:pfam00429 513 NQlwfeglfglsPWFTTLLSTIMGPLLLLLLILL 546
 
Name Accession Description Interval E-value
TLV_coat pfam00429
ENV polyprotein (coat polyprotein);
26-561 8.72e-109

ENV polyprotein (coat polyprotein);


Pssm-ID: 306850  Cd Length: 560  Bit Score: 337.15  E-value: 8.72e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523  26 ILTLLISIGVVQTSPMPHEPHNLTWVITNTatgtvinstshlapigtWFPDLVFDLCALADGTWD--------------- 90
Cdd:pfam00429   2 ILLILLLLGGSAGFGSPHQVYNLTWQVTNT-----------------WWPTLQPDLCDLAGGGQVswsppctppqsvcsg 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523  91 ---------PLGLVWGCQHPAQHSELRRTPFYVCPGEGRSPQQTATCGGPESYFCAYWGCESTGSISWTPPIKDDLIKVQ 161
Cdd:pfam00429  65 cpdlsayltDQSLWPPCVTPPKRTPHANGSFYVCPGECRTRANRRHCGGYSSCYCCSWGCETTGCTYWTPASSWDYITVS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 162 RSPGSESQGWGYGLQpkldandlggpcssnCNPITVQFTPKGKesvgWEKGKTWGLRLYVSGYDYGVMFTIQLSAR---- 237
Cdd:pfam00429 145 WNKTSSTVNCTQEGS---------------CNPLILHFTDCGK----KATTLTWGLRLYVSGYDPLDTFRIRLKITtlne 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 238 ----QGMPLGPNPALPPVgltvtqsqitVPISQELRPRSGPW--DLLKATYLVLNNSKPELTSKCWLCLDAQPPYYEGIA 311
Cdd:pfam00429 206 vlrdQKPPSQPHPLAPPL----------PRPTSPPGPGTGDRllDLLQGAYLTLNATNPSLTQDCWLCLVSGPPYYEGIA 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 312 VPGNYTTSTDNKDCRWQYPGKgrLTLELIQGKGLCFGTIPHTHRHLCNSIQEAPDRDAYIIPPINTWWACTTGLTSCIHT 391
Cdd:pfam00429 276 PNGSVSNHTSAPACSLGPQLA--LTLSEVTGQGCCIGGIPVGHQALCNTTVSTSSGSHYLCAPNGTVWACGTGLTPCLST 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 392 QALNLTNGFCVLVQLAPRILRYSDEMGTRLSPfPAARAKRATVA-------EILGASAFDFQD-------ENYKVLSSAI 457
Cdd:pfam00429 354 ALLNNTTDYCVLAELLPDISYHPGEPIYAIDE-PAGRFRREPVAltlalllGGLGIAAGVGTGttglvstQQFTSLQHAL 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 458 DADLMELGKSLSKSKTSLTSLREATLRNQREQDFQSLQQDGLCKPLEKRCCTFVDNLKHARELLAKVRKRLEDRKREMEQ 537
Cdd:pfam00429 433 ISDIQALESSINDLEDSLTSLAEVVLQNRRGLDLLFLEQGGLCAALQEECCFYADHSGIVRDSIAKLQERLPQRQRLLTD 512
                         570       580       590
                  ....*....|....*....|....*....|....
gi 1039752523 538 GQ----------PVWITVIATLSGFLGLVILIVI 561
Cdd:pfam00429 513 NQlwfeglfglsPWFTTLLSTIMGPLLLLLLILL 546
HTLV-1-like_HR1-HR2 cd09851
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of human ...
448-525 5.32e-27

heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of human T-cell leukemia virus type 1 (HTLV-1), and related domains; This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane(TM) subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including HTLV-1, HTLV -2, primate Mason-Pfizer monkey virus, Moloney murine leukemia virus, simian T-cell lymphotropic virus, feline leukemia virus (FeLV), bovine leukemia virus, and various human endogenous retroviruses (HERVs), including, HERV-H1_c2q24.3, HERV-H2_3q26, HERV-F(c)1_cXq21.33, HERV-T_19q13.11, Syncytin-1 (HERV-W_c7q21.2/ ERVWE1), Syncytin-2 (HERV-FRD_6p24.1), and related domains. This domain includes an N-terminal heptad repeat, a CKS17-like immunosuppressive region, a CX6C motif that forms an intrasubunit disulfide bond, and a C-terminal heptad repeat. N-terminal to HR1-HR2 region is a fusion peptide (FP), and C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1s helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some modern ERVs, those that integrated into the host genome post-speciation, have a currently active exogenous counterpart, such as FeLV. Some ERVs play specific roles in the host, including placental development, protection of the host from infection by related pathogenic and exogenous retroviruses, and genome plasticity. Syncytin-1 and Syncytin-2 are expressed in the placenta, and are fusogenic, although they have a different cell specificity for fusion. Syncytin-2, but not Syncytin-1, is immunosuppressive; its immunosuppressive domain may protect the fetus from the mother's immune system. Syncytin-1 may participate in the formation of the placental trophoblast; it is also implicated in cell fusions between cancer and host cells and between cancer cell, and in human osteclast fusion. This subfamily also contains a mouse envelope protein encoded by the Fv-4 env gene, that blocks infection by exogenous MuLV.


Pssm-ID: 197368 [Multi-domain]  Cd Length: 78  Bit Score: 104.24  E-value: 5.32e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039752523 448 ENYKVLSSAIDADLMELGKSLSKSKTSLTSLREATLRNQREQDFQSLQQDGLCKPLEKRCCTFVDNLKHARELLAKVR 525
Cdd:cd09851     1 QSYKSLSHALDADIQRLAQSISKLQKQLTSLAEVVLQNRRGLDLLTLEQGGLCAALQEECCFYANQSGLVRDSIAKLR 78
 
Name Accession Description Interval E-value
TLV_coat pfam00429
ENV polyprotein (coat polyprotein);
26-561 8.72e-109

ENV polyprotein (coat polyprotein);


Pssm-ID: 306850  Cd Length: 560  Bit Score: 337.15  E-value: 8.72e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523  26 ILTLLISIGVVQTSPMPHEPHNLTWVITNTatgtvinstshlapigtWFPDLVFDLCALADGTWD--------------- 90
Cdd:pfam00429   2 ILLILLLLGGSAGFGSPHQVYNLTWQVTNT-----------------WWPTLQPDLCDLAGGGQVswsppctppqsvcsg 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523  91 ---------PLGLVWGCQHPAQHSELRRTPFYVCPGEGRSPQQTATCGGPESYFCAYWGCESTGSISWTPPIKDDLIKVQ 161
Cdd:pfam00429  65 cpdlsayltDQSLWPPCVTPPKRTPHANGSFYVCPGECRTRANRRHCGGYSSCYCCSWGCETTGCTYWTPASSWDYITVS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 162 RSPGSESQGWGYGLQpkldandlggpcssnCNPITVQFTPKGKesvgWEKGKTWGLRLYVSGYDYGVMFTIQLSAR---- 237
Cdd:pfam00429 145 WNKTSSTVNCTQEGS---------------CNPLILHFTDCGK----KATTLTWGLRLYVSGYDPLDTFRIRLKITtlne 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 238 ----QGMPLGPNPALPPVgltvtqsqitVPISQELRPRSGPW--DLLKATYLVLNNSKPELTSKCWLCLDAQPPYYEGIA 311
Cdd:pfam00429 206 vlrdQKPPSQPHPLAPPL----------PRPTSPPGPGTGDRllDLLQGAYLTLNATNPSLTQDCWLCLVSGPPYYEGIA 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 312 VPGNYTTSTDNKDCRWQYPGKgrLTLELIQGKGLCFGTIPHTHRHLCNSIQEAPDRDAYIIPPINTWWACTTGLTSCIHT 391
Cdd:pfam00429 276 PNGSVSNHTSAPACSLGPQLA--LTLSEVTGQGCCIGGIPVGHQALCNTTVSTSSGSHYLCAPNGTVWACGTGLTPCLST 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 392 QALNLTNGFCVLVQLAPRILRYSDEMGTRLSPfPAARAKRATVA-------EILGASAFDFQD-------ENYKVLSSAI 457
Cdd:pfam00429 354 ALLNNTTDYCVLAELLPDISYHPGEPIYAIDE-PAGRFRREPVAltlalllGGLGIAAGVGTGttglvstQQFTSLQHAL 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039752523 458 DADLMELGKSLSKSKTSLTSLREATLRNQREQDFQSLQQDGLCKPLEKRCCTFVDNLKHARELLAKVRKRLEDRKREMEQ 537
Cdd:pfam00429 433 ISDIQALESSINDLEDSLTSLAEVVLQNRRGLDLLFLEQGGLCAALQEECCFYADHSGIVRDSIAKLQERLPQRQRLLTD 512
                         570       580       590
                  ....*....|....*....|....*....|....
gi 1039752523 538 GQ----------PVWITVIATLSGFLGLVILIVI 561
Cdd:pfam00429 513 NQlwfeglfglsPWFTTLLSTIMGPLLLLLLILL 546
HTLV-1-like_HR1-HR2 cd09851
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of human ...
448-525 5.32e-27

heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of human T-cell leukemia virus type 1 (HTLV-1), and related domains; This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane(TM) subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including HTLV-1, HTLV -2, primate Mason-Pfizer monkey virus, Moloney murine leukemia virus, simian T-cell lymphotropic virus, feline leukemia virus (FeLV), bovine leukemia virus, and various human endogenous retroviruses (HERVs), including, HERV-H1_c2q24.3, HERV-H2_3q26, HERV-F(c)1_cXq21.33, HERV-T_19q13.11, Syncytin-1 (HERV-W_c7q21.2/ ERVWE1), Syncytin-2 (HERV-FRD_6p24.1), and related domains. This domain includes an N-terminal heptad repeat, a CKS17-like immunosuppressive region, a CX6C motif that forms an intrasubunit disulfide bond, and a C-terminal heptad repeat. N-terminal to HR1-HR2 region is a fusion peptide (FP), and C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1s helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some modern ERVs, those that integrated into the host genome post-speciation, have a currently active exogenous counterpart, such as FeLV. Some ERVs play specific roles in the host, including placental development, protection of the host from infection by related pathogenic and exogenous retroviruses, and genome plasticity. Syncytin-1 and Syncytin-2 are expressed in the placenta, and are fusogenic, although they have a different cell specificity for fusion. Syncytin-2, but not Syncytin-1, is immunosuppressive; its immunosuppressive domain may protect the fetus from the mother's immune system. Syncytin-1 may participate in the formation of the placental trophoblast; it is also implicated in cell fusions between cancer and host cells and between cancer cell, and in human osteclast fusion. This subfamily also contains a mouse envelope protein encoded by the Fv-4 env gene, that blocks infection by exogenous MuLV.


Pssm-ID: 197368 [Multi-domain]  Cd Length: 78  Bit Score: 104.24  E-value: 5.32e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039752523 448 ENYKVLSSAIDADLMELGKSLSKSKTSLTSLREATLRNQREQDFQSLQQDGLCKPLEKRCCTFVDNLKHARELLAKVR 525
Cdd:cd09851     1 QSYKSLSHALDADIQRLAQSISKLQKQLTSLAEVVLQNRRGLDLLTLEQGGLCAALQEECCFYANQSGLVRDSIAKLR 78
Ebola_RSV-like_HR1-HR2 cd09948
heptad repeat 1-heptad repeat 2 region of the transmembrane subunit of various endogenous ...
458-513 1.03e-03

heptad repeat 1-heptad repeat 2 region of the transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Ebola virus and Rous sarcoma virus; This domain family spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of endogenous retroviruses (ERVs) and infectious retroviruses, including Ebola virus gp2, Rous sarcoma virus gp37, and the envelope proteins of various ERVs. This domain includes an N-terminal heptad repeat, a CKS17-like immunosuppressive region, a CX6C motif that forms an intra-subunit disulfide bond, and a C-terminal heptad repeat. N-terminal to HR1-HR2 region is a fusion peptide (FP), while C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1s helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some modern ERVs, those that integrated into the host genome post-speciation, have a currently active exogenous counterpart, such as Jaagsiekte sheep retrovirus (JSRV), feline leukemia virus (FeLV), and avian leukemia virus (ALV). Some ERVs play specific roles in the host, including placental development, protection of the host from infection by related pathogenic and exogenous retroviruses, and genome plasticity. Human ERVs (HERVs) belonging to this family include Syncytin-1 (HERV-W_c7q21.2/ ERVWE1), and Syncytin-2 (HERV-FRD_6p24.1) which are expressed in the placenta, and are fusogenic, although they have a different cell specificity for fusion. Syncytin-2, but not Syncytin-1, is immunosuppressive. Its immunosuppressive domain may protect the fetus from the mother's immune system. Syncytin-1 may participate in the formation of the placental trophoblast. It is also implicated in cell fusions between cancer and host cells and between cancer cells, and in human osteclast fusion. This family also contains human HERV-R_c7q21.2 (ERV-3), which is also expressed in the placenta, but is not fusogenic, has an immunosuppressive domain, but lacks a fusion peptide. It is unclear whether ERV-3 has a critical biological role.


Pssm-ID: 197371 [Multi-domain]  Cd Length: 72  Bit Score: 37.83  E-value: 1.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039752523 458 DADLMELGKSLSKSKTSLTSLREATLRNQREQDFQSLQQDGLCKPLEKRCCTFVDN 513
Cdd:cd09948     3 EQDANETTQALQLFLRNVTSLRTVVLQNRRALDFLLAREGGTCHIINEDCCCFLND 58
ENVV1-like_HR1-HR2 cd09950
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of the human ...
465-513 1.05e-03

heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of the human endogenous retrovirus ENVV1, and related domains; This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs), including chicken FET-1 (Female Expressed Transcript 1) protein, and the envelope proteins of the human ERVs (HERVs): ENVV1 (also known as HERV-V2_c19q13.41) and ENVV2 (also known as HERV-V1_c19q13.41 ). This domain belongs to a larger superfamily containing the HR1-HR2 domain of endogenous retroviruses (ERVs) and infectious retroviruses, such as Ebola virus, Rous sarcoma virus and human immunodeficiency virus type 1. This domain includes an N-terminal heptad repeat, a CKS17-like immunosuppressive region, a CX6C motif that forms an intra-subunit disulfide bond, and a C-terminal heptad repeat. N-terminal to HR1-HR2 region is a fusion peptide (FP), and C-terminal, is a membrane-spanning region (MSR). Viral infection involves the formation of a trimer-of-hairpins structure (three HR1 helices, buttressed by three HR2 helices lying in antiparallel orientation). In this structure, the FP (inserted in the host cell membrane) and MSR (inserted in the viral membrane) are in close proximity. ERVs are likely to originate from ancient germ-line infections by active retroviruses. Some ERVs play specific roles in the host, including placental development, protection of the host from infection by related pathogenic and exogenous retroviruses, and genome plasticity. FET-1 may have an ovary-determining role. The FET-1 gene is located on the female specific W chromosome in chickens. During the sex-determining period, the FET-1 transcript is up-regulated in the cortex of the left gonad (the only gonad which develops in female chickens); it is also expressed at a lower level, in neural tissue and waste collection ducts. The genes encoding ENVV1 and ENVV2 proteins are located in tandem on chromosome 19q13.41, and show placenta-specific expression in human and baboon.


Pssm-ID: 197373 [Multi-domain]  Cd Length: 72  Bit Score: 37.95  E-value: 1.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039752523 465 GKSLSKSKTSLTSLREATLRNQREQDFQSLQQDGLCKPLEKRCCTFVDN 513
Cdd:cd09950    10 RDSISALQAEVSSLSNVVLQNRMALDLLLAEQGGVCAVINQSCCAYVNN 58
 
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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