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Conserved domains on  [gi|2030916629|gb|QUM93283|]
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envelope protein [Avian leukosis virus ev/J]

Protein Classification

envelope glycoprotein( domain architecture ID 10264914)

envelope glycoprotein similar to Human immunodeficiency virus envelope glycoprotein gp160, also called surface protein gp120, that attaches the virus to the host lymphoid cell by binding to the primary receptor CD4

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RSV-like_HR1-HR2 cd09949
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of Rous ...
413-484 2.40e-40

heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of Rous sarcoma virus (RSV), and related domains; This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Rous sarcoma virus gp37, Avian leukosis virus subgroup J (ALV-J) envelope protein, and the envelope proteins of various ERVs, including those belonging to the ev/J (or EAV-HP) family of chicken ERVs, such as ev/J 4.1 Rb. ALV-J is a recently emerged avian pathogen, the causative agent of myeloid leukosis in meat-type chicken. ERVs are likely to originate from ancient germ-line infections by active retroviruses. ALV-J may have emerged from a recombination event between an unknown ALV and an EAV-HP ERV. 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.


:

Pssm-ID: 197372  Cd Length: 72  Bit Score: 140.79  E-value: 2.40e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030916629 413 WSVKQANLTSLILNAILEDTNSIRHAVLQNRAAIDFLLLAQGHGCQDVEGMCCFNLSDHSESIHKALQAMKE 484
Cdd:cd09949     1 WSVKQANATSLALNDLLEDIGSIRHAVLQNRAAIDFLLLAHGHGCEDFEGLCCFNLSDHSEIIHKILQAMKE 72
Avian_gp85 super family cl04221
Avian retrovirus envelope protein, gp85; Family of a vain specific viral glycoproteins that ...
1-366 1.37e-25

Avian retrovirus envelope protein, gp85; Family of a vain specific viral glycoproteins that forms a receptor-binding gp85 polypeptide that is linked through disulfide to a membrane-spanning gp37 spike. Gp85 confers a high degree of subgroup specificity for interaction with distinct cell receptors.


The actual alignment was detected with superfamily member pfam03708:

Pssm-ID: 461019  Cd Length: 246  Bit Score: 105.55  E-value: 1.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629   1 MEAVIKAFLTGHPGKVSKKDSKKKPPA-----PEKTPLLPSRGYFFFqtiLACVVIISVVPGV-GGVHLLQQPGNVWVTW 74
Cdd:pfam03708   1 LEASIKAELHELPGKGSKKDPKEKNIAqikgdPEGCPGFPPQGNPIL---IGGSLQEAERFGLrADSFLKEQEGFLVITA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629  75 ANMTGRTDFCLSLQSATSPFRTCLIGIPqyplntfegyvTNVTACDNnadlasqtacliqalnttlpwdpqeldilgsqm 154
Cdd:pfam03708  78 ANHNGFMDFCLCGASATRFFNMCLCGIP-----------GPISECDF--------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629 155 iKNGTTRTCVTFGSmcykennrsrvchnfdgnfngtggaeaelrdfiakwksdDPRIRPYVNQSwtmvSPINAESFSISS 234
Cdd:pfam03708 114 -AGSPRDGCPEIGC---------------------------------------DRLGGKADFQG----GEDNESELFSFK 149
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629 235 RYCGFTSnetryyrRNRSSWCSSKGGEWSAGYSNGTECSSNTRgcggnctaewnyyaygftfgkqpevlwnngtAKALPP 314
Cdd:pfam03708 150 VNCLALK-------LGNAMGCCGHAGQILGGKSLDNIQGIAQI-------------------------------PGALGG 191
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2030916629 315 GIFLICGDRAWQGIPRNALGGPCYLGQLTMLSPN--FTTWMTYGPNITGHRRSR 366
Cdd:pfam03708 192 AIFFICGDRAWQGGPSRPEAGPCLLGHLSFLAPKepDILKTADNHNLFGGREKC 245
 
Name Accession Description Interval E-value
RSV-like_HR1-HR2 cd09949
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of Rous ...
413-484 2.40e-40

heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of Rous sarcoma virus (RSV), and related domains; This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Rous sarcoma virus gp37, Avian leukosis virus subgroup J (ALV-J) envelope protein, and the envelope proteins of various ERVs, including those belonging to the ev/J (or EAV-HP) family of chicken ERVs, such as ev/J 4.1 Rb. ALV-J is a recently emerged avian pathogen, the causative agent of myeloid leukosis in meat-type chicken. ERVs are likely to originate from ancient germ-line infections by active retroviruses. ALV-J may have emerged from a recombination event between an unknown ALV and an EAV-HP ERV. 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.


Pssm-ID: 197372  Cd Length: 72  Bit Score: 140.79  E-value: 2.40e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030916629 413 WSVKQANLTSLILNAILEDTNSIRHAVLQNRAAIDFLLLAQGHGCQDVEGMCCFNLSDHSESIHKALQAMKE 484
Cdd:cd09949     1 WSVKQANATSLALNDLLEDIGSIRHAVLQNRAAIDFLLLAHGHGCEDFEGLCCFNLSDHSEIIHKILQAMKE 72
Avian_gp85 pfam03708
Avian retrovirus envelope protein, gp85; Family of a vain specific viral glycoproteins that ...
1-366 1.37e-25

Avian retrovirus envelope protein, gp85; Family of a vain specific viral glycoproteins that forms a receptor-binding gp85 polypeptide that is linked through disulfide to a membrane-spanning gp37 spike. Gp85 confers a high degree of subgroup specificity for interaction with distinct cell receptors.


Pssm-ID: 461019  Cd Length: 246  Bit Score: 105.55  E-value: 1.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629   1 MEAVIKAFLTGHPGKVSKKDSKKKPPA-----PEKTPLLPSRGYFFFqtiLACVVIISVVPGV-GGVHLLQQPGNVWVTW 74
Cdd:pfam03708   1 LEASIKAELHELPGKGSKKDPKEKNIAqikgdPEGCPGFPPQGNPIL---IGGSLQEAERFGLrADSFLKEQEGFLVITA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629  75 ANMTGRTDFCLSLQSATSPFRTCLIGIPqyplntfegyvTNVTACDNnadlasqtacliqalnttlpwdpqeldilgsqm 154
Cdd:pfam03708  78 ANHNGFMDFCLCGASATRFFNMCLCGIP-----------GPISECDF--------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629 155 iKNGTTRTCVTFGSmcykennrsrvchnfdgnfngtggaeaelrdfiakwksdDPRIRPYVNQSwtmvSPINAESFSISS 234
Cdd:pfam03708 114 -AGSPRDGCPEIGC---------------------------------------DRLGGKADFQG----GEDNESELFSFK 149
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629 235 RYCGFTSnetryyrRNRSSWCSSKGGEWSAGYSNGTECSSNTRgcggnctaewnyyaygftfgkqpevlwnngtAKALPP 314
Cdd:pfam03708 150 VNCLALK-------LGNAMGCCGHAGQILGGKSLDNIQGIAQI-------------------------------PGALGG 191
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2030916629 315 GIFLICGDRAWQGIPRNALGGPCYLGQLTMLSPN--FTTWMTYGPNITGHRRSR 366
Cdd:pfam03708 192 AIFFICGDRAWQGGPSRPEAGPCLLGHLSFLAPKepDILKTADNHNLFGGREKC 245
TLV_coat pfam00429
ENV polyprotein (coat polyprotein);
414-537 4.45e-05

ENV polyprotein (coat polyprotein);


Pssm-ID: 306850  Cd Length: 560  Bit Score: 46.33  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629 414 SVKQANLTSLILNAI-----LEDT--------NSIRHAVLQNRAAIDFLLLAQGHGCQDVEGMCCFnLSDHSESIHKALQ 480
Cdd:pfam00429 419 LVSTQQFTSLQHALIsdiqaLESSindledslTSLAEVVLQNRRGLDLLFLEQGGLCAALQEECCF-YADHSGIVRDSIA 497
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2030916629 481 AMKEHTEKIRVEDDPIGDWFTRTFgGLGGWLAKGVKTLLFALLVIVCLLAIIPCIIK 537
Cdd:pfam00429 498 KLQERLPQRQRLLTDNQLWFEGLF-GLSPWFTTLLSTIMGPLLLLLLILLFGPCILN 553
 
Name Accession Description Interval E-value
RSV-like_HR1-HR2 cd09949
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of Rous ...
413-484 2.40e-40

heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of Rous sarcoma virus (RSV), and related domains; This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Rous sarcoma virus gp37, Avian leukosis virus subgroup J (ALV-J) envelope protein, and the envelope proteins of various ERVs, including those belonging to the ev/J (or EAV-HP) family of chicken ERVs, such as ev/J 4.1 Rb. ALV-J is a recently emerged avian pathogen, the causative agent of myeloid leukosis in meat-type chicken. ERVs are likely to originate from ancient germ-line infections by active retroviruses. ALV-J may have emerged from a recombination event between an unknown ALV and an EAV-HP ERV. 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.


Pssm-ID: 197372  Cd Length: 72  Bit Score: 140.79  E-value: 2.40e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030916629 413 WSVKQANLTSLILNAILEDTNSIRHAVLQNRAAIDFLLLAQGHGCQDVEGMCCFNLSDHSESIHKALQAMKE 484
Cdd:cd09949     1 WSVKQANATSLALNDLLEDIGSIRHAVLQNRAAIDFLLLAHGHGCEDFEGLCCFNLSDHSEIIHKILQAMKE 72
Avian_gp85 pfam03708
Avian retrovirus envelope protein, gp85; Family of a vain specific viral glycoproteins that ...
1-366 1.37e-25

Avian retrovirus envelope protein, gp85; Family of a vain specific viral glycoproteins that forms a receptor-binding gp85 polypeptide that is linked through disulfide to a membrane-spanning gp37 spike. Gp85 confers a high degree of subgroup specificity for interaction with distinct cell receptors.


Pssm-ID: 461019  Cd Length: 246  Bit Score: 105.55  E-value: 1.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629   1 MEAVIKAFLTGHPGKVSKKDSKKKPPA-----PEKTPLLPSRGYFFFqtiLACVVIISVVPGV-GGVHLLQQPGNVWVTW 74
Cdd:pfam03708   1 LEASIKAELHELPGKGSKKDPKEKNIAqikgdPEGCPGFPPQGNPIL---IGGSLQEAERFGLrADSFLKEQEGFLVITA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629  75 ANMTGRTDFCLSLQSATSPFRTCLIGIPqyplntfegyvTNVTACDNnadlasqtacliqalnttlpwdpqeldilgsqm 154
Cdd:pfam03708  78 ANHNGFMDFCLCGASATRFFNMCLCGIP-----------GPISECDF--------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629 155 iKNGTTRTCVTFGSmcykennrsrvchnfdgnfngtggaeaelrdfiakwksdDPRIRPYVNQSwtmvSPINAESFSISS 234
Cdd:pfam03708 114 -AGSPRDGCPEIGC---------------------------------------DRLGGKADFQG----GEDNESELFSFK 149
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629 235 RYCGFTSnetryyrRNRSSWCSSKGGEWSAGYSNGTECSSNTRgcggnctaewnyyaygftfgkqpevlwnngtAKALPP 314
Cdd:pfam03708 150 VNCLALK-------LGNAMGCCGHAGQILGGKSLDNIQGIAQI-------------------------------PGALGG 191
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2030916629 315 GIFLICGDRAWQGIPRNALGGPCYLGQLTMLSPN--FTTWMTYGPNITGHRRSR 366
Cdd:pfam03708 192 AIFFICGDRAWQGGPSRPEAGPCLLGHLSFLAPKepDILKTADNHNLFGGREKC 245
Ebola_RSV-like_HR1-HR2 cd09948
heptad repeat 1-heptad repeat 2 region of the transmembrane subunit of various endogenous ...
413-484 7.47e-22

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: 89.45  E-value: 7.47e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030916629 413 WSVKQANLTSLILNAILEDTNSIRHAVLQNRAAIDFLLLAQGHGCQDVEGMCCFNLSDHSESIHKALQAMKE 484
Cdd:cd09948     1 GLEQDANETTQALQLFLRNVTSLRTVVLQNRRALDFLLAREGGTCHIINEDCCCFLNDQSRITDKIDQLIEQ 72
Ebola-like_HR1-HR2 cd09850
heptad repeat 1-heptad repeat 2 region of the transmembrane subunit of Filoviridae viruses, ...
418-489 1.31e-06

heptad repeat 1-heptad repeat 2 region of the transmembrane subunit of Filoviridae viruses, Ebola virus and Marburg virus, and related domains; This domain subfamily spans both heptad repeats of the glycoprotein (gp)/transmembrane subunit of various endogenous retroviruses (ERVs) and infectious retroviruses, including Ebola virus gp2, Marburg virus gp, and the envelope proteins of various ERVs, including human HERV-R_c7q21.2 (ERV-3). 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 ERVs play specific roles in the host. However, it is unclear whether ERV-3 has a critical biological role: it is expressed in the placenta, but is not fusogenic, has an immunosuppressive domain, but lacks a fusion peptide. Filoviridae, the family of viruses including Ebola and Marburg, may have acquired this domain via horizontal transfer from retroviruses.


Pssm-ID: 197367  Cd Length: 77  Bit Score: 46.33  E-value: 1.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2030916629 418 ANLTSLILNAILEDTNSIRHAVLQNRAAIDFLLLAQGHGCQDV-EGMCCFNLSDHSESIhkalqamKEHTEKI 489
Cdd:cd09850     6 ANETAQALELLLRQTTEMRTFSYQNRLALDYLLAREGGVCGKFnPDNCCIEIDDWGEVI-------KNITDKI 71
TLV_coat pfam00429
ENV polyprotein (coat polyprotein);
414-537 4.45e-05

ENV polyprotein (coat polyprotein);


Pssm-ID: 306850  Cd Length: 560  Bit Score: 46.33  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030916629 414 SVKQANLTSLILNAI-----LEDT--------NSIRHAVLQNRAAIDFLLLAQGHGCQDVEGMCCFnLSDHSESIHKALQ 480
Cdd:pfam00429 419 LVSTQQFTSLQHALIsdiqaLESSindledslTSLAEVVLQNRRGLDLLFLEQGGLCAALQEECCF-YADHSGIVRDSIA 497
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2030916629 481 AMKEHTEKIRVEDDPIGDWFTRTFgGLGGWLAKGVKTLLFALLVIVCLLAIIPCIIK 537
Cdd:pfam00429 498 KLQERLPQRQRLLTDNQLWFEGLF-GLSPWFTTLLSTIMGPLLLLLLILLFGPCILN 553
ENVV1-like_HR1-HR2 cd09950
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of the human ...
418-484 9.67e-05

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: 40.65  E-value: 9.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2030916629 418 ANLTSLILNAILEDTNSIRHAVLQNRAAIDFLLLAQGHGCQDVEGMCCFNLsDHSESIHKALQAMKE 484
Cdd:cd09950     6 ANSTRDSISALQAEVSSLSNVVLQNRMALDLLLAEQGGVCAVINQSCCAYV-NNSGRIETDIKKIYD 71
HTLV-1-like_HR1-HR2 cd09851
heptad repeat 1-heptad repeat 2 region (ectodomain) of the transmembrane subunit of human ...
417-480 9.67e-04

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: 37.99  E-value: 9.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030916629 417 QANLTSLI--LNAILEDTNSIRHAVLQNRAAIDFLLLAQGHGCQDVEGMCCFnLSDHSESIHKALQ 480
Cdd:cd09851    11 DADIQRLAqsISKLQKQLTSLAEVVLQNRRGLDLLTLEQGGLCAALQEECCF-YANQSGLVRDSIA 75
 
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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