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Conserved domains on  [gi|1994697543|dbj|BCL84862|]
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envelope precursor [Bovine leukemia virus]

Protein Classification

HTLV-1-like_HR1-HR2 domain-containing protein( domain architecture ID 11995389)

HTLV-1-like_HR1-HR2 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TLV_coat pfam00429
ENV polyprotein (coat polyprotein);
20-469 2.43e-117

ENV polyprotein (coat polyprotein);


:

Pssm-ID: 306850  Cd Length: 560  Bit Score: 356.80  E-value: 2.43e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543  20 LTLTLLALCRP-IQTWRCSLSLGNQQWMTAYNQEAKFSISIDQILEAHNQSPF----CAKSPRYTldsVNGYPKIYWPPP 94
Cdd:pfam00429  24 LTWQVTNTWWPtLQPDLCDLAGGGQVSWSPPCTPPQSVCSGCPDLSAYLTDQSlwppCVTPPKRT---PHANGSFYVCPG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543  95 QGRRRFGAR----AMVTYDCEPRCPYVGadrfdCPHWDNASQADQGSFYVNHQ-------------ILFLHLKQCHGIF- 156
Cdd:pfam00429 101 ECRTRANRRhcggYSSCYCCSWGCETTG-----CTYWTPASSWDYITVSWNKTsstvnctqegscnPLILHFTDCGKKAt 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 157 TLTWEIW----GYDPLITFSLH-------------KIPDPPQPDFPQLNS----------DWVPSVRSWA-LLLNQTARA 208
Cdd:pfam00429 176 TLTWGLRlyvsGYDPLDTFRIRlkittlnevlrdqKPPSQPHPLAPPLPRptsppgpgtgDRLLDLLQGAyLTLNATNPS 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 209 FP-DCAICWEPSPPW----APEILVYNKTIS---SSGPGLAL---------------PDAQIFWVNT------------- 252
Cdd:pfam00429 256 LTqDCWLCLVSGPPYyegiAPNGSVSNHTSApacSLGPQLALtlsevtgqgcciggiPVGHQALCNTtvstssgshylca 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 253 ---SSFNTTQGWHHPSQRLLFNVSQG---NALLLPPISLVNLS--TASSAPPTRVRRSPVAaLTLGLALsVGL---TGIN 321
Cdd:pfam00429 336 pngTVWACGTGLTPCLSTALLNNTTDycvLAELLPDISYHPGEpiYAIDEPAGRFRREPVA-LTLALLL-GGLgiaAGVG 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 322 VAVSAL-SHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGfqSLCPTINEPCCFL----RI 396
Cdd:pfam00429 414 TGTTGLvSTQQFTSLQHALISDIQALESSINDLEDSLTSLAEVVLQNRRGLDLLFLEQG--GLCAALQEECCFYadhsGI 491
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1994697543 397 QNDSIIRLGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALFLLFLAPCLIKcltsRLLKLLR 469
Cdd:pfam00429 492 VRDSIAKLQERLPQRQRLLTDNQLWFEGLFGLSPWFTTLLSTIMGPLLLLLLILLFGPCILN----RLVQFIK 560
 
Name Accession Description Interval E-value
TLV_coat pfam00429
ENV polyprotein (coat polyprotein);
20-469 2.43e-117

ENV polyprotein (coat polyprotein);


Pssm-ID: 306850  Cd Length: 560  Bit Score: 356.80  E-value: 2.43e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543  20 LTLTLLALCRP-IQTWRCSLSLGNQQWMTAYNQEAKFSISIDQILEAHNQSPF----CAKSPRYTldsVNGYPKIYWPPP 94
Cdd:pfam00429  24 LTWQVTNTWWPtLQPDLCDLAGGGQVSWSPPCTPPQSVCSGCPDLSAYLTDQSlwppCVTPPKRT---PHANGSFYVCPG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543  95 QGRRRFGAR----AMVTYDCEPRCPYVGadrfdCPHWDNASQADQGSFYVNHQ-------------ILFLHLKQCHGIF- 156
Cdd:pfam00429 101 ECRTRANRRhcggYSSCYCCSWGCETTG-----CTYWTPASSWDYITVSWNKTsstvnctqegscnPLILHFTDCGKKAt 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 157 TLTWEIW----GYDPLITFSLH-------------KIPDPPQPDFPQLNS----------DWVPSVRSWA-LLLNQTARA 208
Cdd:pfam00429 176 TLTWGLRlyvsGYDPLDTFRIRlkittlnevlrdqKPPSQPHPLAPPLPRptsppgpgtgDRLLDLLQGAyLTLNATNPS 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 209 FP-DCAICWEPSPPW----APEILVYNKTIS---SSGPGLAL---------------PDAQIFWVNT------------- 252
Cdd:pfam00429 256 LTqDCWLCLVSGPPYyegiAPNGSVSNHTSApacSLGPQLALtlsevtgqgcciggiPVGHQALCNTtvstssgshylca 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 253 ---SSFNTTQGWHHPSQRLLFNVSQG---NALLLPPISLVNLS--TASSAPPTRVRRSPVAaLTLGLALsVGL---TGIN 321
Cdd:pfam00429 336 pngTVWACGTGLTPCLSTALLNNTTDycvLAELLPDISYHPGEpiYAIDEPAGRFRREPVA-LTLALLL-GGLgiaAGVG 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 322 VAVSAL-SHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGfqSLCPTINEPCCFL----RI 396
Cdd:pfam00429 414 TGTTGLvSTQQFTSLQHALISDIQALESSINDLEDSLTSLAEVVLQNRRGLDLLFLEQG--GLCAALQEECCFYadhsGI 491
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1994697543 397 QNDSIIRLGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALFLLFLAPCLIKcltsRLLKLLR 469
Cdd:pfam00429 492 VRDSIAKLQERLPQRQRLLTDNQLWFEGLFGLSPWFTTLLSTIMGPLLLLLLILLFGPCILN----RLVQFIK 560
HTLV-1-like_HR1-HR2 cd09851
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of human ...
330-404 1.53e-24

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: 96.93  E-value: 1.53e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994697543 330 QRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRlgFQSLCPTINEPCCFLRIQN----DSIIRL 404
Cdd:cd09851     1 QSYKSLSHALDADIQRLAQSISKLQKQLTSLAEVVLQNRRGLDLLTLE--QGGLCAALQEECCFYANQSglvrDSIAKL 77
 
Name Accession Description Interval E-value
TLV_coat pfam00429
ENV polyprotein (coat polyprotein);
20-469 2.43e-117

ENV polyprotein (coat polyprotein);


Pssm-ID: 306850  Cd Length: 560  Bit Score: 356.80  E-value: 2.43e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543  20 LTLTLLALCRP-IQTWRCSLSLGNQQWMTAYNQEAKFSISIDQILEAHNQSPF----CAKSPRYTldsVNGYPKIYWPPP 94
Cdd:pfam00429  24 LTWQVTNTWWPtLQPDLCDLAGGGQVSWSPPCTPPQSVCSGCPDLSAYLTDQSlwppCVTPPKRT---PHANGSFYVCPG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543  95 QGRRRFGAR----AMVTYDCEPRCPYVGadrfdCPHWDNASQADQGSFYVNHQ-------------ILFLHLKQCHGIF- 156
Cdd:pfam00429 101 ECRTRANRRhcggYSSCYCCSWGCETTG-----CTYWTPASSWDYITVSWNKTsstvnctqegscnPLILHFTDCGKKAt 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 157 TLTWEIW----GYDPLITFSLH-------------KIPDPPQPDFPQLNS----------DWVPSVRSWA-LLLNQTARA 208
Cdd:pfam00429 176 TLTWGLRlyvsGYDPLDTFRIRlkittlnevlrdqKPPSQPHPLAPPLPRptsppgpgtgDRLLDLLQGAyLTLNATNPS 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 209 FP-DCAICWEPSPPW----APEILVYNKTIS---SSGPGLAL---------------PDAQIFWVNT------------- 252
Cdd:pfam00429 256 LTqDCWLCLVSGPPYyegiAPNGSVSNHTSApacSLGPQLALtlsevtgqgcciggiPVGHQALCNTtvstssgshylca 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 253 ---SSFNTTQGWHHPSQRLLFNVSQG---NALLLPPISLVNLS--TASSAPPTRVRRSPVAaLTLGLALsVGL---TGIN 321
Cdd:pfam00429 336 pngTVWACGTGLTPCLSTALLNNTTDycvLAELLPDISYHPGEpiYAIDEPAGRFRREPVA-LTLALLL-GGLgiaAGVG 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994697543 322 VAVSAL-SHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGfqSLCPTINEPCCFL----RI 396
Cdd:pfam00429 414 TGTTGLvSTQQFTSLQHALISDIQALESSINDLEDSLTSLAEVVLQNRRGLDLLFLEQG--GLCAALQEECCFYadhsGI 491
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1994697543 397 QNDSIIRLGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALFLLFLAPCLIKcltsRLLKLLR 469
Cdd:pfam00429 492 VRDSIAKLQERLPQRQRLLTDNQLWFEGLFGLSPWFTTLLSTIMGPLLLLLLILLFGPCILN----RLVQFIK 560
HTLV-1-like_HR1-HR2 cd09851
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of human ...
330-404 1.53e-24

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: 96.93  E-value: 1.53e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994697543 330 QRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRlgFQSLCPTINEPCCFLRIQN----DSIIRL 404
Cdd:cd09851     1 QSYKSLSHALDADIQRLAQSISKLQKQLTSLAEVVLQNRRGLDLLTLE--QGGLCAALQEECCFYANQSglvrDSIAKL 77
Ebola_RSV-like_HR1-HR2 cd09948
heptad repeat 1-heptad repeat 2 region of the transmembrane subunit of various endogenous ...
338-407 4.33e-23

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: 92.53  E-value: 4.33e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994697543 338 VLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRlgFQSLCPTINEPCC-FLRIQN---DSIIRLGDL 407
Cdd:cd09948     1 GLEQDANETTQALQLFLRNVTSLRTVVLQNRRALDFLLAR--EGGTCHIINEDCCcFLNDQSritDKIDQLIEQ 72
Ebola_HIV-1-like_HR1-HR2 cd09947
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of various ...
338-407 1.03e-18

heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Ebola virus and human immunodeficiency virus type 1 (HIV-1); This domain superfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Ebola virus gp2, Rous sarcoma virus gp37, human immunodeficiency virus type 1 (HIV-1) gp41, and the envelope proteins of various ERVs. In the HR1-HR2 region of Ebola virus and RSV, the linker region between the two repeats includes a CKS17-like immunosuppressive region and a CX6C motif that forms an intra-subunit disulfide bond; MMTV, HIV-1, HERV-K endogenous retroviruses and related sequences lack a canonical CSK17-like sequence, and CX6C motif. N-terminal to the 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 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 superfamily 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 cell, and in human osteclast fusion. This superfamily also contains human HERV-R_c7q21.2 (ERV-3), which is also expressed in the placenta, but is not fusogenic, and has an immunosuppressive domain, but lacks a fusion peptide. It is unclear whether ERV-3 has a critical biological role. Included in this superfamily are ERVs from domestic sheep that are related to JSRV, the agent of transmissible lung cancer in sheep; for example, enJSRV-26 that retains an intact genome. These endogenous JSRVs protect the sheep against JSRV infection and are required for sheep placental development.


Pssm-ID: 197370  Cd Length: 73  Bit Score: 80.35  E-value: 1.03e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994697543 338 VLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGFQslCPTINEPCC-FLRIQN----DSIIRLGDL 407
Cdd:cd09947     1 RLQQLLRLTTQAIKNLHTNLTAIAKYLAQNRRGLDWLAARRGGT--CVALTEVCCpFLSITNkwwqDWIRKLDFL 73
 
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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