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Conserved domains on  [gi|120873|sp|P10258|]
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RecName: Full=Gag polyprotein; Contains: RecName: Full=Matrix protein p10; Contains: RecName: Full=Phosphorylated protein pp21; Contains: RecName: Full=Protein p3; Contains: RecName: Full=Protein p8; Contains: RecName: Full=Protein n; Contains: RecName: Full=Capsid protein p27; Contains: RecName: Full=Nucleocapsid protein p14

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gag_p24 pfam00607
gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ...
 284-409 1.58e-45

gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro.


:

Pssm-ID: 459864  Cd Length: 128  Bit Score: 157.06  E-value: 1.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120873     284 VWEPLPLKTLKELQSAVRTMGPSAPYTLQVVD-MVASQWLTPSDWHQTARATLSPGDYVLWRTEYEEKSKEMVQK--AAG 360
Cdd:pfam00607   1 VWEPLDFKLLKELKKAVKQYGPNSPYTMQLLEaLASSNALTPYDWRTLAKAVLSPGQYLLWKAEWQELAQEQARRnqRAG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 120873     361 KRKGkVSLDMLLGTGQFLSPSSQIKLSKDVLKDVTTNAVLAWRAIPPPG 409
Cdd:pfam00607  81 PDRG-ITLDMLTGTGQYATPQAQAQLPPEVLEQIKALALRAWKKLPPPG 128
Gag_p10 pfam02337
Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins ...
 8-92 4.30e-39

Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins and encompasses the p10 region producing the p10 protein upon proteolytic cleavage of GAG by retroviral protease. The p10 or matrix protein (MA) is associated with the virus envelope glycoproteins in most mammalian retroviruses and may be involved in virus particle assembly, transport and budding. Some of the GAG polyproteins have alternate cleavage sites leading to the production of alternative and longer cleavage products (e.g. p19) the alignment of this family only covers the approximately N-terminal (GAG) 100 amino acid region of homology to p10.


:

Pssm-ID: 426727  Cd Length: 85  Bit Score: 137.86  E-value: 4.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120873       8 GQKLFVSVLQRLLSERGLHVKESSAIEFYQFLIKVSPWFPEEGGLNLQDWKRVGREMKRYAAEHGTDSIPKQAYPIWLQL 87
Cdd:pfam02337   1 SKQLFLTALQALLKERGLKVSKSSLIKFLQFVEEVCPWFPEEGTLNLETWKKVGRELKTQATEHGPKNIPVDTWPIWALI 80


                  ....*
gi 120873      88 REILT 92
Cdd:pfam02337  81 RAVLD 85
Gag_p24_C pfam19317
Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ...
 409-482 6.88e-35

Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro.


:

Pssm-ID: 466038  Cd Length: 74  Bit Score: 126.05  E-value: 6.88e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 120873     409 GVKKTVLAGLKQGNEESYETFISRLEEAVYRMMPRGEGSDILIKQLAWENANSLCQDLIRPIRKTGTIQDYIRA 482
Cdd:pfam19317   1 GYKPTSLADIRQGPKEPYQDFVARLYDALRKEMPDGKAKDVITKQLAYENANPECQDLLKPLGKTGTLSDMIRA 74
zf-CCHC_5 pfam14787
GAG-polyprotein viral zinc-finger;
550-584 1.68e-16

GAG-polyprotein viral zinc-finger;


:

Pssm-ID: 373297  Cd Length: 36  Bit Score: 72.97  E-value: 1.68e-16
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 120873     550 PPGLCPRCKKGYHWKSECKSKFDKDGNPLPPLETN 584
Cdd:pfam14787   1 PPGLCPRCKKGKHWARDCHSKFDKNGNPLSPNEGN 35
AIR1 super family cl34894
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ...
 525-567 1.21e-05

Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


The actual alignment was detected with superfamily member COG5082:

Pssm-ID: 227414 [Multi-domain]  Cd Length: 190  Bit Score: 46.38  E-value: 1.21e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 120873   525 PVCFSCGKTGHIRKDCkdekgskraPPGLCPRCKKGYHWKSEC 567
Cdd:COG5082  61 PVCFNCGQNGHLRRDC---------PHSICYNCSWDGHRSNHC 94
 
Name Accession Description Interval E-value
Gag_p24 pfam00607
gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ...
 284-409 1.58e-45

gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro.


Pssm-ID: 459864  Cd Length: 128  Bit Score: 157.06  E-value: 1.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120873     284 VWEPLPLKTLKELQSAVRTMGPSAPYTLQVVD-MVASQWLTPSDWHQTARATLSPGDYVLWRTEYEEKSKEMVQK--AAG 360
Cdd:pfam00607   1 VWEPLDFKLLKELKKAVKQYGPNSPYTMQLLEaLASSNALTPYDWRTLAKAVLSPGQYLLWKAEWQELAQEQARRnqRAG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 120873     361 KRKGkVSLDMLLGTGQFLSPSSQIKLSKDVLKDVTTNAVLAWRAIPPPG 409
Cdd:pfam00607  81 PDRG-ITLDMLTGTGQYATPQAQAQLPPEVLEQIKALALRAWKKLPPPG 128
Gag_p10 pfam02337
Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins ...
 8-92 4.30e-39

Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins and encompasses the p10 region producing the p10 protein upon proteolytic cleavage of GAG by retroviral protease. The p10 or matrix protein (MA) is associated with the virus envelope glycoproteins in most mammalian retroviruses and may be involved in virus particle assembly, transport and budding. Some of the GAG polyproteins have alternate cleavage sites leading to the production of alternative and longer cleavage products (e.g. p19) the alignment of this family only covers the approximately N-terminal (GAG) 100 amino acid region of homology to p10.


Pssm-ID: 426727  Cd Length: 85  Bit Score: 137.86  E-value: 4.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120873       8 GQKLFVSVLQRLLSERGLHVKESSAIEFYQFLIKVSPWFPEEGGLNLQDWKRVGREMKRYAAEHGTDSIPKQAYPIWLQL 87
Cdd:pfam02337   1 SKQLFLTALQALLKERGLKVSKSSLIKFLQFVEEVCPWFPEEGTLNLETWKKVGRELKTQATEHGPKNIPVDTWPIWALI 80


                  ....*
gi 120873      88 REILT 92
Cdd:pfam02337  81 RAVLD 85
Gag_p24_C pfam19317
Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ...
 409-482 6.88e-35

Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro.


Pssm-ID: 466038  Cd Length: 74  Bit Score: 126.05  E-value: 6.88e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 120873     409 GVKKTVLAGLKQGNEESYETFISRLEEAVYRMMPRGEGSDILIKQLAWENANSLCQDLIRPIRKTGTIQDYIRA 482
Cdd:pfam19317   1 GYKPTSLADIRQGPKEPYQDFVARLYDALRKEMPDGKAKDVITKQLAYENANPECQDLLKPLGKTGTLSDMIRA 74
zf-CCHC_5 pfam14787
GAG-polyprotein viral zinc-finger;
550-584 1.68e-16

GAG-polyprotein viral zinc-finger;


Pssm-ID: 373297  Cd Length: 36  Bit Score: 72.97  E-value: 1.68e-16
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 120873     550 PPGLCPRCKKGYHWKSECKSKFDKDGNPLPPLETN 584
Cdd:pfam14787   1 PPGLCPRCKKGKHWARDCHSKFDKNGNPLSPNEGN 35
AIR1 COG5082
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ...
 525-567 1.21e-05

Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227414 [Multi-domain]  Cd Length: 190  Bit Score: 46.38  E-value: 1.21e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 120873   525 PVCFSCGKTGHIRKDCkdekgskraPPGLCPRCKKGYHWKSEC 567
Cdd:COG5082  61 PVCFNCGQNGHLRRDC---------PHSICYNCSWDGHRSNHC 94
ZnF_C2HC smart00343
zinc finger;
526-541 3.96e-04

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 37.81  E-value: 3.96e-04
                           10
                   ....*....|....*.
gi 120873      526 VCFSCGKTGHIRKDCK 541
Cdd:smart00343   1 KCYNCGKEGHIARDCP 16
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 527-570 4.51e-04

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 40.95  E-value: 4.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 120873    527 CFSCGKTGHIRKDCKDEKGSKRAPPgLCPRCKKGYHWKSECKSK 570
Cdd:PTZ00368 106 CYNCGGEGHISRDCPNAGKRPGGDK-TCYNCGQTGHLSRDCPDK 148
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 525-541 1.04e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 36.74  E-value: 1.04e-03
                          10
                  ....*....|....*..
gi 120873     525 PVCFSCGKTGHIRKDCK 541
Cdd:pfam00098   1 GKCYNCGEPGHIARDCP 17
CE4_SpCDA1 cd10980
Putative catalytic domain of Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and ...
 248-355 7.13e-03

Putative catalytic domain of Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and similar proteins; This family is represented by Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), encoded by the cda1 gene. The general function of chitin deacetylase (CDA) is the synthesis of chitosan from chitin, a polymer of N-acetyl glucosamine, to build up the proper ascospore wall. The actual function of SpCDA1 might be involved in allantoin hydrolysis. It is likely an ortholog to bacterial PuuE allantoinase, whereas it is more distantly related to the CDAs found in other fungi, such as Saccharomyces cerevisiae and Mucor rouxii. Those CDAs are similar with rizobial NodB protein and are not included in this family.


Pssm-ID: 200602 [Multi-domain]  Cd Length: 297  Bit Score: 38.68  E-value: 7.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120873   248 PPVGFAGAMAEAREKGDLTFTF-----PVVFMGESDEDDTPVWEPLPLKTLKELQSAVRTMgpsaPYTLQVVDM---VAS 319
Cdd:cd10980 142 APRGWYYGRASLRSRSLVAQVYkelglPLLWYSDAYNDDLPYWVPYPGGSKPEDDKGLLIV----PYTLDTNDYknaGYQ 217

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 120873   320 QWLTPSDWHQTARATLSpgdyVLWRtEYEEKSKEMV 355
Cdd:cd10980 218 GFINSDDFYTYLRDAFD----VLYE-EGLEGAPKMM 248
 
Name Accession Description Interval E-value
Gag_p24 pfam00607
gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ...
 284-409 1.58e-45

gag protein p24 N-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro.


Pssm-ID: 459864  Cd Length: 128  Bit Score: 157.06  E-value: 1.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120873     284 VWEPLPLKTLKELQSAVRTMGPSAPYTLQVVD-MVASQWLTPSDWHQTARATLSPGDYVLWRTEYEEKSKEMVQK--AAG 360
Cdd:pfam00607   1 VWEPLDFKLLKELKKAVKQYGPNSPYTMQLLEaLASSNALTPYDWRTLAKAVLSPGQYLLWKAEWQELAQEQARRnqRAG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 120873     361 KRKGkVSLDMLLGTGQFLSPSSQIKLSKDVLKDVTTNAVLAWRAIPPPG 409
Cdd:pfam00607  81 PDRG-ITLDMLTGTGQYATPQAQAQLPPEVLEQIKALALRAWKKLPPPG 128
Gag_p10 pfam02337
Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins ...
 8-92 4.30e-39

Retroviral GAG p10 protein; This family consists of various retroviral GAG (core) polyproteins and encompasses the p10 region producing the p10 protein upon proteolytic cleavage of GAG by retroviral protease. The p10 or matrix protein (MA) is associated with the virus envelope glycoproteins in most mammalian retroviruses and may be involved in virus particle assembly, transport and budding. Some of the GAG polyproteins have alternate cleavage sites leading to the production of alternative and longer cleavage products (e.g. p19) the alignment of this family only covers the approximately N-terminal (GAG) 100 amino acid region of homology to p10.


Pssm-ID: 426727  Cd Length: 85  Bit Score: 137.86  E-value: 4.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120873       8 GQKLFVSVLQRLLSERGLHVKESSAIEFYQFLIKVSPWFPEEGGLNLQDWKRVGREMKRYAAEHGTDSIPKQAYPIWLQL 87
Cdd:pfam02337   1 SKQLFLTALQALLKERGLKVSKSSLIKFLQFVEEVCPWFPEEGTLNLETWKKVGRELKTQATEHGPKNIPVDTWPIWALI 80


                  ....*
gi 120873      88 REILT 92
Cdd:pfam02337  81 RAVLD 85
Gag_p24_C pfam19317
Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA ...
 409-482 6.88e-35

Gag protein p24 C-terminal domain; p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro.


Pssm-ID: 466038  Cd Length: 74  Bit Score: 126.05  E-value: 6.88e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 120873     409 GVKKTVLAGLKQGNEESYETFISRLEEAVYRMMPRGEGSDILIKQLAWENANSLCQDLIRPIRKTGTIQDYIRA 482
Cdd:pfam19317   1 GYKPTSLADIRQGPKEPYQDFVARLYDALRKEMPDGKAKDVITKQLAYENANPECQDLLKPLGKTGTLSDMIRA 74
zf-CCHC_5 pfam14787
GAG-polyprotein viral zinc-finger;
550-584 1.68e-16

GAG-polyprotein viral zinc-finger;


Pssm-ID: 373297  Cd Length: 36  Bit Score: 72.97  E-value: 1.68e-16
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 120873     550 PPGLCPRCKKGYHWKSECKSKFDKDGNPLPPLETN 584
Cdd:pfam14787   1 PPGLCPRCKKGKHWARDCHSKFDKNGNPLSPNEGN 35
AIR1 COG5082
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ...
 525-567 1.21e-05

Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227414 [Multi-domain]  Cd Length: 190  Bit Score: 46.38  E-value: 1.21e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 120873   525 PVCFSCGKTGHIRKDCkdekgskraPPGLCPRCKKGYHWKSEC 567
Cdd:COG5082  61 PVCFNCGQNGHLRRDC---------PHSICYNCSWDGHRSNHC 94
ZnF_C2HC smart00343
zinc finger;
526-541 3.96e-04

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 37.81  E-value: 3.96e-04
                           10
                   ....*....|....*.
gi 120873      526 VCFSCGKTGHIRKDCK 541
Cdd:smart00343   1 KCYNCGKEGHIARDCP 16
AIR1 COG5082
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ...
 526-569 4.08e-04

Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227414 [Multi-domain]  Cd Length: 190  Bit Score: 41.76  E-value: 4.08e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 120873   526 VCFSCGKTGHIRKDCkDEKGSKRAPpglCPRCKKGYHWKSECKS 569
Cdd:COG5082  99 KCYNCGETGHLSRDC-NPSKDQQKS---CFDCNSTRHSSEDCPS 138
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 527-570 4.51e-04

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 40.95  E-value: 4.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 120873    527 CFSCGKTGHIRKDCKDEKGSKRAPPgLCPRCKKGYHWKSECKSK 570
Cdd:PTZ00368 106 CYNCGGEGHISRDCPNAGKRPGGDK-TCYNCGQTGHLSRDCPDK 148
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 525-541 1.04e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 36.74  E-value: 1.04e-03
                          10
                  ....*....|....*..
gi 120873     525 PVCFSCGKTGHIRKDCK 541
Cdd:pfam00098   1 GKCYNCGEPGHIARDCP 17
CE4_SpCDA1 cd10980
Putative catalytic domain of Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and ...
 248-355 7.13e-03

Putative catalytic domain of Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and similar proteins; This family is represented by Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), encoded by the cda1 gene. The general function of chitin deacetylase (CDA) is the synthesis of chitosan from chitin, a polymer of N-acetyl glucosamine, to build up the proper ascospore wall. The actual function of SpCDA1 might be involved in allantoin hydrolysis. It is likely an ortholog to bacterial PuuE allantoinase, whereas it is more distantly related to the CDAs found in other fungi, such as Saccharomyces cerevisiae and Mucor rouxii. Those CDAs are similar with rizobial NodB protein and are not included in this family.


Pssm-ID: 200602 [Multi-domain]  Cd Length: 297  Bit Score: 38.68  E-value: 7.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120873   248 PPVGFAGAMAEAREKGDLTFTF-----PVVFMGESDEDDTPVWEPLPLKTLKELQSAVRTMgpsaPYTLQVVDM---VAS 319
Cdd:cd10980 142 APRGWYYGRASLRSRSLVAQVYkelglPLLWYSDAYNDDLPYWVPYPGGSKPEDDKGLLIV----PYTLDTNDYknaGYQ 217

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 120873   320 QWLTPSDWHQTARATLSpgdyVLWRtEYEEKSKEMV 355
Cdd:cd10980 218 GFINSDDFYTYLRDAFD----VLYE-EGLEGAPKMM 248
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 527-567 9.05e-03

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 37.09  E-value: 9.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 120873    527 CFSCGKTGHIRKDCKDEKGSKRapPGLCPRCKKGYHWKSEC 567
Cdd:PTZ00368  55 CYNCGKTGHLSRECPEAPPGSG--PRSCYNCGQTGHISREC 93
 
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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