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Conserved domains on  [gi|2024379311|ref|XP_040507133|]
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heterochromatin protein 1-binding protein 3 isoform X1 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Linker_histone pfam00538
linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin ...
 159-229 2.17e-21

linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures Histone H1 is replaced by histone H5 in some cell types.


:

Pssm-ID: 459846 [Multi-domain]  Cd Length: 71  Bit Score: 87.97  E-value: 2.17e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024379311 159 RPKMDAILTEAIKACFQKSGASVVAIRKYIIHKYPSLELERRGYLLKQALKRELERGIIRQVKGKGASGSF 229
Cdd:pfam00538   1 HPPYSDMIKEAIKALKERKGSSRQAIKKYIKANYKVGDVAKFNSLLKRALKKGVEKGTLVQPKGTGASGSF 71
Linker_histone pfam00538
linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin ...
 343-410 9.97e-21

linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures Histone H1 is replaced by histone H5 in some cell types.


:

Pssm-ID: 459846 [Multi-domain]  Cd Length: 71  Bit Score: 86.04  E-value: 9.97e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024379311 343 MEDAILSAIAAMNEPKTCSTTALKKYILENHPGTNSNFQVHLLKRTLQRCEKNGWLEQISGKGFSGTF 410
Cdd:pfam00538   4 YSDMIKEAIKALKERKGSSRQAIKKYIKANYKVGDVAKFNSLLKRALKKGVEKGTLVQPKGTGASGSF 71
Linker_histone pfam00538
linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin ...
 267-327 2.26e-12

linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures Histone H1 is replaced by histone H5 in some cell types.


:

Pssm-ID: 459846 [Multi-domain]  Cd Length: 71  Bit Score: 62.16  E-value: 2.26e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024379311 267 AFTRLCEPKEASYSLIKKYVSQYYPKLKVDIRPQLLKNALQRAVEKGQLEQITGKGASGTF 327
Cdd:pfam00538  11 AIKALKERKGSSRQAIKKYIKANYKVGDVAKFNSLLKRALKKGVEKGTLVQPKGTGASGSF 71
PHA03378 super family cl33729
EBNA-3B; Provisional
 460-553 3.78e-04

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024379311 460 PPPKKRMQKRPPPKSRSRAPPMKRRESKPKPRKTPAAHQGKAKPPPKVKTPVKKAKPAAPAIKKPSGGSSSKKPTAsGRK 539
Cdd:PHA03378  756 PPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTG-GVK 834

                          90
                  ....*....|....
gi 2024379311 540 EVKPSAKGKSAMRK 553
Cdd:PHA03378  835 RGRPSLKKPAALER 848
LGT super family cl00478
Prolipoprotein diacylglyceryl transferase;
21-138 1.38e-03

Prolipoprotein diacylglyceryl transferase;


The actual alignment was detected with superfamily member PRK13108:

Pssm-ID: 469786 [Multi-domain]  Cd Length: 460  Bit Score: 41.50  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024379311  21 GTQLIHTDKLSEKAEDDTMPIRRSVNSSRETPPKSKPAEGGEEVKADAEATSEESASAGEEQENETLPAAAPSEAEQPKE 100
Cdd:PRK13108  329 VAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEA 408

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2024379311 101 PENEEKGET-KSSVETKKDDKDQSKEKEKKVKKTIPAWA 138
Cdd:PRK13108  409 HDETEPEVPeKAAPIPDPAKPDELAVAGPGDDPAEPDGI 447
 
Name Accession Description Interval E-value
Linker_histone pfam00538
linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin ...
 159-229 2.17e-21

linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures Histone H1 is replaced by histone H5 in some cell types.


Pssm-ID: 459846 [Multi-domain]  Cd Length: 71  Bit Score: 87.97  E-value: 2.17e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024379311 159 RPKMDAILTEAIKACFQKSGASVVAIRKYIIHKYPSLELERRGYLLKQALKRELERGIIRQVKGKGASGSF 229
Cdd:pfam00538   1 HPPYSDMIKEAIKALKERKGSSRQAIKKYIKANYKVGDVAKFNSLLKRALKKGVEKGTLVQPKGTGASGSF 71
H15 cd00073
linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, ...
 156-243 2.84e-21

linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, consisting of an octamer of core histones, two full turns of DNA, a linker histone (H1 or H5) and a variable length of linker DNA; H1/H5 are chromatin-associated proteins that bind to the exterior of nucleosomes and dramatically stabilize the highly condensed states of chromatin fibers; stabilization of higher order folding occurs through electrostatic neutralization of the linker DNA segments, through a highly positively charged carboxy- terminal domain known as the AKP helix (Ala, Lys, Pro); thought to be involved in specific protein-protein and protein-DNA interactions and play a role in suppressing core histone tail domain acetylation in the chromatin fiber


Pssm-ID: 238028 [Multi-domain]  Cd Length: 88  Bit Score: 88.06  E-value: 2.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024379311 156 ATSRPKMDAILTEAIKACFQKSGASVVAIRKYIIHKYPSLeLERRGYLLKQALKRELERGIIRQVKGKGASGSFVVVSNA 235
Cdd:cd00073     1 PPSHPPYSEMVTEAIKALKERKGSSLQAIKKYIEAKYKVD-DENFNKLLKLALKKGVAKGKLVQVKGTGASGSFKLSKKK 79


                  ....*...
gi 2024379311 236 GKTVQKAR 243
Cdd:cd00073    80 KKKKKPAK 87
Linker_histone pfam00538
linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin ...
 343-410 9.97e-21

linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures Histone H1 is replaced by histone H5 in some cell types.


Pssm-ID: 459846 [Multi-domain]  Cd Length: 71  Bit Score: 86.04  E-value: 9.97e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024379311 343 MEDAILSAIAAMNEPKTCSTTALKKYILENHPGTNSNFQVHLLKRTLQRCEKNGWLEQISGKGFSGTF 410
Cdd:pfam00538   4 YSDMIKEAIKALKERKGSSRQAIKKYIKANYKVGDVAKFNSLLKRALKKGVEKGTLVQPKGTGASGSF 71
H15 smart00526
Domain in histone families 1 and 5;
156-222 5.46e-14

Domain in histone families 1 and 5;


Pssm-ID: 197772 [Multi-domain]  Cd Length: 66  Bit Score: 66.83  E-value: 5.46e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024379311  156 ATSRPKMDAILTEAIKACFQKSGASVVAIRKYIIHKYPSLElERRGYLLKQALKRELERGIIRQVKG 222
Cdd:smart00526   1 PPSHPPYSEMIVEAISALKERKGSSLQAIKKYIEANYKVLP-NNFRKLLKLALKRLVASGKLVQVKG 66
Linker_histone pfam00538
linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin ...
 267-327 2.26e-12

linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures Histone H1 is replaced by histone H5 in some cell types.


Pssm-ID: 459846 [Multi-domain]  Cd Length: 71  Bit Score: 62.16  E-value: 2.26e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024379311 267 AFTRLCEPKEASYSLIKKYVSQYYPKLKVDIRPQLLKNALQRAVEKGQLEQITGKGASGTF 327
Cdd:pfam00538  11 AIKALKERKGSSRQAIKKYIKANYKVGDVAKFNSLLKRALKKGVEKGTLVQPKGTGASGSF 71
H15 smart00526
Domain in histone families 1 and 5;
343-403 1.02e-10

Domain in histone families 1 and 5;


Pssm-ID: 197772 [Multi-domain]  Cd Length: 66  Bit Score: 57.59  E-value: 1.02e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024379311  343 MEDAILSAIAAMNEPKTCSTTALKKYILENHpGTNSNFQVHLLKRTLQRCEKNGWLEQISG 403
Cdd:smart00526   7 YSEMIVEAISALKERKGSSLQAIKKYIEANY-KVLPNNFRKLLKLALKRLVASGKLVQVKG 66
H15 smart00526
Domain in histone families 1 and 5;
259-320 2.79e-10

Domain in histone families 1 and 5;


Pssm-ID: 197772 [Multi-domain]  Cd Length: 66  Bit Score: 56.05  E-value: 2.79e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024379311  259 KLEDILPLAFTRLCEPKEASYSLIKKYVSQYYPKLKVDIRPqLLKNALQRAVEKGQLEQITG 320
Cdd:smart00526   6 PYSEMIVEAISALKERKGSSLQAIKKYIEANYKVLPNNFRK-LLKLALKRLVASGKLVQVKG 66
H15 cd00073
linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, ...
 343-413 7.40e-08

linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, consisting of an octamer of core histones, two full turns of DNA, a linker histone (H1 or H5) and a variable length of linker DNA; H1/H5 are chromatin-associated proteins that bind to the exterior of nucleosomes and dramatically stabilize the highly condensed states of chromatin fibers; stabilization of higher order folding occurs through electrostatic neutralization of the linker DNA segments, through a highly positively charged carboxy- terminal domain known as the AKP helix (Ala, Lys, Pro); thought to be involved in specific protein-protein and protein-DNA interactions and play a role in suppressing core histone tail domain acetylation in the chromatin fiber


Pssm-ID: 238028 [Multi-domain]  Cd Length: 88  Bit Score: 49.93  E-value: 7.40e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024379311 343 MEDAILSAIAAMNEPKTCSTTALKKYILENHPGTNSNFQVHlLKRTLQRCEKNGWLEQISGKGFSGTFQLC 413
Cdd:cd00073     7 YSEMVTEAIKALKERKGSSLQAIKKYIEAKYKVDDENFNKL-LKLALKKGVAKGKLVQVKGTGASGSFKLS 76
PHA03378 PHA03378
EBNA-3B; Provisional
 460-553 3.78e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024379311 460 PPPKKRMQKRPPPKSRSRAPPMKRRESKPKPRKTPAAHQGKAKPPPKVKTPVKKAKPAAPAIKKPSGGSSSKKPTAsGRK 539
Cdd:PHA03378  756 PPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTG-GVK 834

                          90
                  ....*....|....
gi 2024379311 540 EVKPSAKGKSAMRK 553
Cdd:PHA03378  835 RGRPSLKKPAALER 848
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 21-138 1.38e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 41.50  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024379311  21 GTQLIHTDKLSEKAEDDTMPIRRSVNSSRETPPKSKPAEGGEEVKADAEATSEESASAGEEQENETLPAAAPSEAEQPKE 100
Cdd:PRK13108  329 VAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEA 408

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2024379311 101 PENEEKGET-KSSVETKKDDKDQSKEKEKKVKKTIPAWA 138
Cdd:PRK13108  409 HDETEPEVPeKAAPIPDPAKPDELAVAGPGDDPAEPDGI 447
 
Name Accession Description Interval E-value
Linker_histone pfam00538
linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin ...
 159-229 2.17e-21

linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures Histone H1 is replaced by histone H5 in some cell types.


Pssm-ID: 459846 [Multi-domain]  Cd Length: 71  Bit Score: 87.97  E-value: 2.17e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024379311 159 RPKMDAILTEAIKACFQKSGASVVAIRKYIIHKYPSLELERRGYLLKQALKRELERGIIRQVKGKGASGSF 229
Cdd:pfam00538   1 HPPYSDMIKEAIKALKERKGSSRQAIKKYIKANYKVGDVAKFNSLLKRALKKGVEKGTLVQPKGTGASGSF 71
H15 cd00073
linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, ...
 156-243 2.84e-21

linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, consisting of an octamer of core histones, two full turns of DNA, a linker histone (H1 or H5) and a variable length of linker DNA; H1/H5 are chromatin-associated proteins that bind to the exterior of nucleosomes and dramatically stabilize the highly condensed states of chromatin fibers; stabilization of higher order folding occurs through electrostatic neutralization of the linker DNA segments, through a highly positively charged carboxy- terminal domain known as the AKP helix (Ala, Lys, Pro); thought to be involved in specific protein-protein and protein-DNA interactions and play a role in suppressing core histone tail domain acetylation in the chromatin fiber


Pssm-ID: 238028 [Multi-domain]  Cd Length: 88  Bit Score: 88.06  E-value: 2.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024379311 156 ATSRPKMDAILTEAIKACFQKSGASVVAIRKYIIHKYPSLeLERRGYLLKQALKRELERGIIRQVKGKGASGSFVVVSNA 235
Cdd:cd00073     1 PPSHPPYSEMVTEAIKALKERKGSSLQAIKKYIEAKYKVD-DENFNKLLKLALKKGVAKGKLVQVKGTGASGSFKLSKKK 79


                  ....*...
gi 2024379311 236 GKTVQKAR 243
Cdd:cd00073    80 KKKKKPAK 87
Linker_histone pfam00538
linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin ...
 343-410 9.97e-21

linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures Histone H1 is replaced by histone H5 in some cell types.


Pssm-ID: 459846 [Multi-domain]  Cd Length: 71  Bit Score: 86.04  E-value: 9.97e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024379311 343 MEDAILSAIAAMNEPKTCSTTALKKYILENHPGTNSNFQVHLLKRTLQRCEKNGWLEQISGKGFSGTF 410
Cdd:pfam00538   4 YSDMIKEAIKALKERKGSSRQAIKKYIKANYKVGDVAKFNSLLKRALKKGVEKGTLVQPKGTGASGSF 71
H15 smart00526
Domain in histone families 1 and 5;
156-222 5.46e-14

Domain in histone families 1 and 5;


Pssm-ID: 197772 [Multi-domain]  Cd Length: 66  Bit Score: 66.83  E-value: 5.46e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024379311  156 ATSRPKMDAILTEAIKACFQKSGASVVAIRKYIIHKYPSLElERRGYLLKQALKRELERGIIRQVKG 222
Cdd:smart00526   1 PPSHPPYSEMIVEAISALKERKGSSLQAIKKYIEANYKVLP-NNFRKLLKLALKRLVASGKLVQVKG 66
Linker_histone pfam00538
linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin ...
 267-327 2.26e-12

linker histone H1 and H5 family; Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures Histone H1 is replaced by histone H5 in some cell types.


Pssm-ID: 459846 [Multi-domain]  Cd Length: 71  Bit Score: 62.16  E-value: 2.26e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024379311 267 AFTRLCEPKEASYSLIKKYVSQYYPKLKVDIRPQLLKNALQRAVEKGQLEQITGKGASGTF 327
Cdd:pfam00538  11 AIKALKERKGSSRQAIKKYIKANYKVGDVAKFNSLLKRALKKGVEKGTLVQPKGTGASGSF 71
H15 smart00526
Domain in histone families 1 and 5;
343-403 1.02e-10

Domain in histone families 1 and 5;


Pssm-ID: 197772 [Multi-domain]  Cd Length: 66  Bit Score: 57.59  E-value: 1.02e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024379311  343 MEDAILSAIAAMNEPKTCSTTALKKYILENHpGTNSNFQVHLLKRTLQRCEKNGWLEQISG 403
Cdd:smart00526   7 YSEMIVEAISALKERKGSSLQAIKKYIEANY-KVLPNNFRKLLKLALKRLVASGKLVQVKG 66
H15 smart00526
Domain in histone families 1 and 5;
259-320 2.79e-10

Domain in histone families 1 and 5;


Pssm-ID: 197772 [Multi-domain]  Cd Length: 66  Bit Score: 56.05  E-value: 2.79e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024379311  259 KLEDILPLAFTRLCEPKEASYSLIKKYVSQYYPKLKVDIRPqLLKNALQRAVEKGQLEQITG 320
Cdd:smart00526   6 PYSEMIVEAISALKERKGSSLQAIKKYIEANYKVLPNNFRK-LLKLALKRLVASGKLVQVKG 66
H15 cd00073
linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, ...
 343-413 7.40e-08

linker histone 1 and histone 5 domains; the basic subunit of chromatin is the nucleosome, consisting of an octamer of core histones, two full turns of DNA, a linker histone (H1 or H5) and a variable length of linker DNA; H1/H5 are chromatin-associated proteins that bind to the exterior of nucleosomes and dramatically stabilize the highly condensed states of chromatin fibers; stabilization of higher order folding occurs through electrostatic neutralization of the linker DNA segments, through a highly positively charged carboxy- terminal domain known as the AKP helix (Ala, Lys, Pro); thought to be involved in specific protein-protein and protein-DNA interactions and play a role in suppressing core histone tail domain acetylation in the chromatin fiber


Pssm-ID: 238028 [Multi-domain]  Cd Length: 88  Bit Score: 49.93  E-value: 7.40e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024379311 343 MEDAILSAIAAMNEPKTCSTTALKKYILENHPGTNSNFQVHlLKRTLQRCEKNGWLEQISGKGFSGTFQLC 413
Cdd:cd00073     7 YSEMVTEAIKALKERKGSSLQAIKKYIEAKYKVDDENFNKL-LKLALKKGVAKGKLVQVKGTGASGSFKLS 76
PHA03378 PHA03378
EBNA-3B; Provisional
 460-553 3.78e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024379311 460 PPPKKRMQKRPPPKSRSRAPPMKRRESKPKPRKTPAAHQGKAKPPPKVKTPVKKAKPAAPAIKKPSGGSSSKKPTAsGRK 539
Cdd:PHA03378  756 PPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTG-GVK 834

                          90
                  ....*....|....
gi 2024379311 540 EVKPSAKGKSAMRK 553
Cdd:PHA03378  835 RGRPSLKKPAALER 848
PRK13808 PRK13808
adenylate kinase; Provisional
 463-554 8.94e-04

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 41.80  E-value: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024379311 463 KKRMQKRPPPKSRSRAPPMKRRESKPKPRKTPAAHQGKAKPPPKVKTPVKKAKPAAPAIKKPSGGSSSKKPTASGRKEVK 542
Cdd:PRK13808  204 KTPAAKSGAKKASAKAKSAAKKVSKKKAAKTAVSAKKAAKTAAKAAKKAKKTAKKALKKAAKAVKKAAKKAAKAAAKAAK 283

                          90
                  ....*....|..
gi 2024379311 543 PSAKGKSAMRKS 554
Cdd:PRK13808  284 GAAKATKGKAKA 295
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 21-138 1.38e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 41.50  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024379311  21 GTQLIHTDKLSEKAEDDTMPIRRSVNSSRETPPKSKPAEGGEEVKADAEATSEESASAGEEQENETLPAAAPSEAEQPKE 100
Cdd:PRK13108  329 VAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEA 408

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2024379311 101 PENEEKGET-KSSVETKKDDKDQSKEKEKKVKKTIPAWA 138
Cdd:PRK13108  409 HDETEPEVPeKAAPIPDPAKPDELAVAGPGDDPAEPDGI 447
PHA03378 PHA03378
EBNA-3B; Provisional
 469-557 7.00e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.28  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024379311 469 RPPPKSRSRAPP-------MKRRESKPKPRKTPAAHQGKAKPPPKVKTPVKKAKPAAPAIKKPSGGSSSKKPTAS--GRK 539
Cdd:PHA03378  695 QPPPRAPTPMRPpaappgrAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAapGAP 774

                          90
                  ....*....|....*...
gi 2024379311 540 EVKPSAKGKSAMRKSLRA 557
Cdd:PHA03378  775 TPQPPPQAPPAPQQRPRG 792
 
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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