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Conserved domains on  [gi|1622849857|ref|XP_028686549|]
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pre-mRNA-processing factor 40 homolog A isoform X12 [Macaca mulatta]

Protein Classification

PRP40 family protein( domain architecture ID 1003925)

PRP40 family protein similar to Homo sapiens pre-mRNA-processing factor 40 homolog A that binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function

Gene Ontology:  GO:0000398|GO:0003723
PubMed:  26494226

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRP40 super family cl34905
Splicing factor [RNA processing and modification];
54-695 1.79e-47

Splicing factor [RNA processing and modification];


The actual alignment was detected with superfamily member COG5104:

Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 178.74  E-value: 1.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857  54 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 132
Cdd:COG5104     7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 133 EdleamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaananaststsntvsgtvpvv 212
Cdd:COG5104    87 K------KVEPIAEQKHDERSM---------------------------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 213 pepevtsivATVVDNENTVTisteeqaqltstpAIQDQSVEVSSNTGEETSKQETVADFTPKKeeeesqpakktytwnTK 292
Cdd:COG5104   103 ---------IGGNGNDMAIT-------------DHETSEPKYLLGRLMSQYGITSTKDAVYRL---------------TK 145

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 293 EEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLEN 372
Cdd:COG5104   146 EEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAG 225

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 373 HEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsTTWSE 451
Cdd:COG5104   226 NSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-IIWLL 304

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 452 AQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRESFQIFLDELHEHGQLHSMSS 531
Cdd:COG5104   305 NHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMK 384

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 532 WMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD-ILKDKGFVVEVNTTFEDFVAII----SSTK 606
Cdd:COG5104   385 WKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYEReTRTGQISPTDRRAVDEIFEAIAekkeEGEI 464

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 607 RSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA------PPIELDAVWEDIRERFVKEPAFE 680
Cdd:COG5104   465 KFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtktgkpKPSTWDLASKELGESLEYKALGD 544

                         650
                  ....*....|....*
gi 1622849857 681 DitlESERKRIFKDF 695
Cdd:COG5104   545 E---DNIRRQIFEDF 556
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
54-695 1.79e-47

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 178.74  E-value: 1.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857  54 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 132
Cdd:COG5104     7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 133 EdleamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaananaststsntvsgtvpvv 212
Cdd:COG5104    87 K------KVEPIAEQKHDERSM---------------------------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 213 pepevtsivATVVDNENTVTisteeqaqltstpAIQDQSVEVSSNTGEETSKQETVADFTPKKeeeesqpakktytwnTK 292
Cdd:COG5104   103 ---------IGGNGNDMAIT-------------DHETSEPKYLLGRLMSQYGITSTKDAVYRL---------------TK 145

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 293 EEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLEN 372
Cdd:COG5104   146 EEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAG 225

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 373 HEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsTTWSE 451
Cdd:COG5104   226 NSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-IIWLL 304

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 452 AQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRESFQIFLDELHEHGQLHSMSS 531
Cdd:COG5104   305 NHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMK 384

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 532 WMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD-ILKDKGFVVEVNTTFEDFVAII----SSTK 606
Cdd:COG5104   385 WKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYEReTRTGQISPTDRRAVDEIFEAIAekkeEGEI 464

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 607 RSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA------PPIELDAVWEDIRERFVKEPAFE 680
Cdd:COG5104   465 KFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtktgkpKPSTWDLASKELGESLEYKALGD 544

                         650
                  ....*....|....*
gi 1622849857 681 DitlESERKRIFKDF 695
Cdd:COG5104   545 E---DNIRRQIFEDF 556
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 294-343 1.96e-14

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 67.87  E-value: 1.96e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622849857 294 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 343
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 63-90 2.45e-11

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 58.69  E-value: 2.45e-11
                          10        20
                  ....*....|....*....|....*...
gi 1622849857  63 WTEHKSPDGRTYYYNTETKQSTWEKPDD 90
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 63-90 7.63e-11

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 57.23  E-value: 7.63e-11
                           10        20
                   ....*....|....*....|....*...
gi 1622849857   63 WTEHKSPDGRTYYYNTETKQSTWEKPDD 90
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
PHA03255 PHA03255
BDLF3; Provisional
 144-286 1.19e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 44.51  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 144 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSTSNTVSGTvpvVPEPEVTSIVAT 223
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849857 224 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 286
Cdd:PHA03255  131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
 
Name Accession Description Interval E-value
PRP40 COG5104
Splicing factor [RNA processing and modification];
54-695 1.79e-47

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 178.74  E-value: 1.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857  54 GTASG-AKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKEL 132
Cdd:COG5104     7 GMASGeARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIPPER 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 133 EdleamiKAEESSKQEECTTTStapvptteipttmstmaaaeaaaavvaaaaaaaaaaaaananaststsntvsgtvpvv 212
Cdd:COG5104    87 K------KVEPIAEQKHDERSM---------------------------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 213 pepevtsivATVVDNENTVTisteeqaqltstpAIQDQSVEVSSNTGEETSKQETVADFTPKKeeeesqpakktytwnTK 292
Cdd:COG5104   103 ---------IGGNGNDMAIT-------------DHETSEPKYLLGRLMSQYGITSTKDAVYRL---------------TK 145

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 293 EEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLEN 372
Cdd:COG5104   146 EEAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAG 225

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 373 HEKMTSTTRYKKAEQMFGEMEVWNAI-SERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYsTTWSE 451
Cdd:COG5104   226 NSHIKYYTDWFTFKSIFSKHPYYSSVvNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETF-IIWLL 304

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 452 AQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRESFQIFLDELHEHGQLHSMSS 531
Cdd:COG5104   305 NHYVFDSVVRYLKNKEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAAQNARHHRDEFRTLLRKLYSEGKIYYRMK 384

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 532 WMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKD-ILKDKGFVVEVNTTFEDFVAII----SSTK 606
Cdd:COG5104   385 WKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYEReTRTGQISPTDRRAVDEIFEAIAekkeEGEI 464

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 607 RSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAA------PPIELDAVWEDIRERFVKEPAFE 680
Cdd:COG5104   465 KFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYtktgkpKPSTWDLASKELGESLEYKALGD 544

                         650
                  ....*....|....*
gi 1622849857 681 DitlESERKRIFKDF 695
Cdd:COG5104   545 E---DNIRRQIFEDF 556
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 294-343 1.96e-14

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 67.87  E-value: 1.96e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622849857 294 EAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAY 343
Cdd:pfam01846   1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 63-90 2.45e-11

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 58.69  E-value: 2.45e-11
                          10        20
                  ....*....|....*....|....*...
gi 1622849857  63 WTEHKSPDGRTYYYNTETKQSTWEKPDD 90
Cdd:cd00201     4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 63-88 4.08e-11

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 58.29  E-value: 4.08e-11
                          10        20
                  ....*....|....*....|....*.
gi 1622849857  63 WTEHKSPDGRTYYYNTETKQSTWEKP 88
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 63-90 7.63e-11

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 57.23  E-value: 7.63e-11
                           10        20
                   ....*....|....*....|....*...
gi 1622849857   63 WTEHKSPDGRTYYYNTETKQSTWEKPDD 90
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 293-346 3.40e-09

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 53.35  E-value: 3.40e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849857  293 EEAKQAFKELLKEKRVP-SNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQ 346
Cdd:smart00441   1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 101-131 1.96e-08

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 50.60  E-value: 1.96e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622849857 101 KCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 131
Cdd:cd00201     1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 100-131 1.99e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 50.68  E-value: 1.99e-08
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622849857  100 SKCPWKEYKSDSGKPYYYNSQTKESRWAKPKE 131
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 643-697 5.70e-08

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 49.88  E-value: 5.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849857  643 KRKESAFKSMLKQAaPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMH 697
Cdd:smart00441   1 EEAKEAFKELLKEH-EVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 103-129 6.68e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 49.04  E-value: 6.68e-08
                          10        20
                  ....*....|....*....|....*..
gi 1622849857 103 PWKEYKSDSGKPYYYNSQTKESRWAKP 129
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 427-486 5.96e-06

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 44.10  E-value: 5.96e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857  427 KRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAedeelQNMDKEDALICFEEHIRA 486
Cdd:smart00441   1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYK-----ALLSESEREQLFEDHIEE 55
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 644-695 3.03e-05

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 42.06  E-value: 3.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622849857 644 RKESAFKSMLKQaaPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDF 695
Cdd:pfam01846   1 KAREAFKELLKE--HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
PHA03255 PHA03255
BDLF3; Provisional
 144-286 1.19e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 44.51  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 144 SSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSTSNTVSGTvpvVPEPEVTSIVAT 223
Cdd:PHA03255   54 STNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGT---GTSTGVTSNVTT 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622849857 224 vvDNENTVTISTEEQAQLTSTPAIQDQSvevSSNTGEETSKQETVADftpkkeeeESQPAKKT 286
Cdd:PHA03255  131 --RSSSTTSATTRITNATTLAPTLSSKG---TSNATKTTAELPTVPD--------ERQPSLSY 180
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 511-563 1.11e-03

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 37.44  E-value: 1.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622849857 511 ESFQIFLDELHehgqLHSMSSWMELYPTISSDIRFTNMlgQPGSTALDLFKFY 563
Cdd:pfam01846   4 EAFKELLKEHK----ITPYSTWSEIKKKIENDPRYKAL--LDGSEREELFEDY 50
alt PHA02566
ADP-ribosyltransferase; Provisional
 252-457 5.49e-03

ADP-ribosyltransferase; Provisional


Pssm-ID: 222881 [Multi-domain]  Cd Length: 684  Bit Score: 40.50  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 252 VEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFkELLKEKRVPSNASWEQAMKMIINDPRYSALA 331
Cdd:PHA02566  192 VYISKKTGEKVTKVEAIAASIAKEEEKRTDQAVITKTKISRRAIAKAQ-SLESDREAELFQKFENSANDYNKPAEAPLIP 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 332 KLSEKKQAFNAyKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMT-STTRYKKAEQMFGE-------MEVWNAISERdR 403
Cdd:PHA02566  271 PAEEIKTNEGS-GAIKTMVAASRFESSDYELDYFRKFIFLRHIGEVdEKIKLKISEAIKQEdqtsiknLEKFAASVDE-L 348

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849857 404 LEIYEDVLFFLSKKEKEQAKQLRKRNwealKNILDNMANVTYSTTWSEAQ-QYLM 457
Cdd:PHA02566  349 LEDYKDIVFENSLDALEWINDLNKGR----KGMPDEVKAELTRSKWKQAKtKFLM 399
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 44-288 8.65e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 39.90  E-value: 8.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857  44 PGVNSMDVA----AGTASGAKSMwTEHKSPdgrtyyynteTKQSTWEKPDDLKTPAEQLLSKCPwkeyksdsgkpyyyNS 119
Cdd:pfam05109 466 PTVSTADVTsptpAGTTSGASPV-TPSPSP----------RDNGTESKAPDMTSPTSAVTTPTP--------------NA 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 120 QTKESRWAKPKELEDLEAMIKAEESSKQEECTTTSTAPVPTTEIPT---TMSTMAAAEAAAAVVAAAAAAAAAAAAANAN 196
Cdd:pfam05109 521 TSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTpnaTIPTLGKTSPTSAVTTPTPNATSPTVGETSP 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849857 197 ASTSTSNTVSGT--VPVVPEPEVTSIVATVVDNENTVTISTEEQA------QLTSTPAIQDQS------VEVSSNTGEET 262
Cdd:pfam05109 601 QANTTNHTLGGTssTPVVTSPPKNATSAVTTGQHNITSSSTSSMSlrpssiSETLSPSTSDNStshmplLTSAHPTGGEN 680

                         250       260
                  ....*....|....*....|....*.
gi 1622849857 263 SKQETVADfTPKKEEEESQPAKKTYT 288
Cdd:pfam05109 681 ITQVTPAS-TSTHHVSTSSPAPRPGT 705
 
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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