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Conserved domains on  [gi|1985651394|emb|CAE5959227|]
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unnamed protein product [Arabidopsis arenosa]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02511 super family cl27029
hydrolase
73-394 4.79e-82

hydrolase


The actual alignment was detected with superfamily member PLN02511:

Pssm-ID: 215282 [Multi-domain]  Cd Length: 388  Bit Score: 276.28  E-value: 4.79e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394   73 GVVSRCRILHGRYVATPWLASPHIQTCFLNFHGLPPVFSYRRQLFLASDGGTIALDWVTNSDVldggfqnqseiTKEDTT 152
Cdd:PLN02511    32 SFLPKFKSLERPYDAFPLLGNRHVETIFASFFRSLPAVRYRRECLRTPDGGAVALDWVSGDDR-----------ALPADA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  153 PIAVVIPGLTSDSSSAYLKHLAYNTAKTGWNVVISNHRGLGGVSVTSDRFYNAGWTEDIRVVLGYLQQKYPRAPLFAIGT 232
Cdd:PLN02511   101 PVLILLPGLTGGSDDSYVRHMLLRARSKGWRVVVFNSRGCADSPVTTPQFYSASFTGDLRQVVDHVAGRYPSANLYAAGW 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  233 SIGANVLVKYLGEEGERTPLRGAVAICSPWDLLIGDRFIcRTLKQKLYDKALTIGLQGYAQLHEPQFLRLA---NWEGIK 309
Cdd:PLN02511   181 SLGANILVNYLGEEGENCPLSGAVSLCNPFDLVIADEDF-HKGFNNVYDKALAKALRKIFAKHALLFEGLGgeyNIPLVA 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  310 KSRSIRDFDNHATCLVGKFETVDTYYRKSSSTQYVGNVAVPLLCISALDDPLCTKEAIPWDECRANKNIVLATTNHGGHL 389
Cdd:PLN02511   260 NAKTVRDFDDGLTRVSFGFKSVDAYYSNSSSSDSIKHVRVPLLCIQAANDPIAPARGIPREDIKANPNCLLIVTPSGGHL 339

                   ....*
gi 1985651394  390 AFFEG 394
Cdd:PLN02511   340 GWVAG 344
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
667-793 5.52e-59

forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.


:

Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 198.80  E-value: 5.52e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  667 IPVFTVLKNGAILKNIFVVNSRDFSsperigstvsddddEVEEILVVGRHPDCDILLTHPSISRFHLEIRSISSRQKLSV 746
Cdd:cd22691      1 IPVLTVLKNGSVLKNIFLHGKFSKS--------------EEEDILVVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITL 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1985651394  747 TDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGSTRIYRLHWIPLS 793
Cdd:cd22691     67 TDLSSVHGTWVNGQRIEPGVPVELEEGDTVRLGASTRVYRLHWIPVS 113
TMEM18 pfam14770
Transmembrane protein 18; The function of this family is not known, however it is predicted to ...
533-650 1.09e-57

Transmembrane protein 18; The function of this family is not known, however it is predicted to be a three-pass membrane protein.


:

Pssm-ID: 405460  Cd Length: 118  Bit Score: 195.51  E-value: 1.09e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  533 GFFHAIDWKEPWIMGLMAFHALLLLVTLLSRRHLNFHMFLFLLALAGVYFAENLNRELRKNWKSFSTQNYFDSQGVFLSV 612
Cdd:pfam14770    1 GFLHAVDWSEPWLIGLIAFHVLLLVLALLTRRSYNFQMVLFLLLLLLVYFAEYINELAARNWRSFSKQNYFDSRGLFISV 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1985651394  613 LWSGPLLVIAMIILINTLFSLCYLIVKWKRAELRHRAR 650
Cdd:pfam14770   81 VFSGPLLLNCLIILVNWLYQTVSLMVELKRAQLKRRAR 118
InfC COG0290
Translation initiation factor IF-3 [Translation, ribosomal structure and biogenesis]; ...
2191-2308 9.01e-33

Translation initiation factor IF-3 [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-3 is part of the Pathway/BioSystem: Translation factors


:

Pssm-ID: 440059  Cd Length: 175  Bit Score: 126.34  E-value: 9.01e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2191 SDGPRLNEKITGDYVRLVSEEG--HCVVSLREALRRAKELECDLVEVQRDAKPPVCKIV---KYSLEQYKKAKvgkeraK 2265
Cdd:COG0290      6 KKEPRINEEIRAPEVRLIGEDGeqLGIVSTREALRLAEEAGLDLVEISPNAKPPVCKIMdygKFKYEQQKKAK------E 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1985651394 2266 AKRAEAIrPEVKEIRFTPKIEAKDLKFKSDQALKLMESGYRVK 2308
Cdd:COG0290     80 AKKKQKV-IEVKEIKFRPNIDEHDYETKLKNARRFLEEGDKVK 121
PIN_Smg5-6-like cd09880
VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related ...
1895-2061 3.20e-31

VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related proteins; PIN (PilT N terminus) domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and homologs are included in this family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo. Many of the bacterial homologs in this group have an N-terminal PIN domain and a C-terminal PhoH-like ATPase domain.


:

Pssm-ID: 350228  Cd Length: 152  Bit Score: 120.86  E-value: 3.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1895 VVDTSSLLDKESRkpLHLLQGLKGTHLVLPRTVLREVNEVKRSRSFLfrrrTEMASSALDWIEECKVNTKWWIQVQSPSE 1974
Cdd:cd09880      1 VFDTNILLSHLDV--LKLLVESGKWTVVIPLIVITELDGLKKNPDPL----GPKARSALRYIEACLKKHSRWLRVQTSKG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1975 ETKATAPTPPVTpqsngsafpfslhwNNYAPEIDSPTSEDQVLECALLYRNRNRD-----EKLVLLSNDVTLKIKAMAEG 2049
Cdd:cd09880     75 NYLADLTIRSEQ--------------LSDASELRRRNNDDRILECALWQQKHFVDredgdGKVVLVTNDRNLRLKARARG 140
                          170
                   ....*....|..
gi 1985651394 2050 VICETPQEFYES 2061
Cdd:cd09880    141 VEAVTVKELLKS 152
Cytadhesin_P30 super family cl25798
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
2379-2576 9.69e-14

Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 and P30 proteins. P30 has been found to be membrane associated and localized on the tip organelle. It is thought that it is important in cytadherence and virulence. The N-terminus contains two predicted transmembrane helices followed by a long region of a short 6 residue proline rich repeat.


The actual alignment was detected with superfamily member pfam07271:

Pssm-ID: 429374 [Multi-domain]  Cd Length: 275  Bit Score: 74.23  E-value: 9.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2379 KSARVKEEKSDSSEAGES--TVDDHGDIEKCEPGFSVDQAQPVQVQNTYAKREPgsefsggrdasRFEPRSPnqHVNPQr 2456
Cdd:pfam07271   95 KEKRLLEEKERQEQMAEQlqRISEQQETQAIEPTEQQNTAEPTQPAGVNVANQP-----------QMGINQP--QINPQ- 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2457 prFQAPNQQPTGridpqSPNQPPSAPRPQFPNQ--QPTGRFDPQFPNQPPGPPRRQFPDQAPNQQPTGRFNPQfpnksps 2534
Cdd:pfam07271  161 --FGPNPQQRIG-----FPMQPNMGMRPGFNQMpgMPPNQMRPGFNQMPGMPPRPGFPNPMPNMQPRPGFRPQ------- 226
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1985651394 2535 ppqspfpdQAPNQQPSGPSPNrHIDRQGPPPRFQNQAPNQQP 2576
Cdd:pfam07271  227 --------PGPMGNRPGGGFP-HPGTPMGPNRMPNPGMNQRP 259
 
Name Accession Description Interval E-value
PLN02511 PLN02511
hydrolase
73-394 4.79e-82

hydrolase


Pssm-ID: 215282 [Multi-domain]  Cd Length: 388  Bit Score: 276.28  E-value: 4.79e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394   73 GVVSRCRILHGRYVATPWLASPHIQTCFLNFHGLPPVFSYRRQLFLASDGGTIALDWVTNSDVldggfqnqseiTKEDTT 152
Cdd:PLN02511    32 SFLPKFKSLERPYDAFPLLGNRHVETIFASFFRSLPAVRYRRECLRTPDGGAVALDWVSGDDR-----------ALPADA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  153 PIAVVIPGLTSDSSSAYLKHLAYNTAKTGWNVVISNHRGLGGVSVTSDRFYNAGWTEDIRVVLGYLQQKYPRAPLFAIGT 232
Cdd:PLN02511   101 PVLILLPGLTGGSDDSYVRHMLLRARSKGWRVVVFNSRGCADSPVTTPQFYSASFTGDLRQVVDHVAGRYPSANLYAAGW 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  233 SIGANVLVKYLGEEGERTPLRGAVAICSPWDLLIGDRFIcRTLKQKLYDKALTIGLQGYAQLHEPQFLRLA---NWEGIK 309
Cdd:PLN02511   181 SLGANILVNYLGEEGENCPLSGAVSLCNPFDLVIADEDF-HKGFNNVYDKALAKALRKIFAKHALLFEGLGgeyNIPLVA 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  310 KSRSIRDFDNHATCLVGKFETVDTYYRKSSSTQYVGNVAVPLLCISALDDPLCTKEAIPWDECRANKNIVLATTNHGGHL 389
Cdd:PLN02511   260 NAKTVRDFDDGLTRVSFGFKSVDAYYSNSSSSDSIKHVRVPLLCIQAANDPIAPARGIPREDIKANPNCLLIVTPSGGHL 339

                   ....*
gi 1985651394  390 AFFEG 394
Cdd:PLN02511   340 GWVAG 344
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
84-412 1.02e-76

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 258.15  E-value: 1.02e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394   84 RYVATPWLASPHIQTCFLNFHGLPPVFSYRRQLFLASDGGTIALDWVTNSDvldggfqnqseitkeDTTPIAVVIPGLTS 163
Cdd:COG0429      8 PFRPPWWLRNGHLQTIYPSLFRRRPALPYRRERLELPDGDFVDLDWSDPPA---------------PSKPLVVLLHGLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  164 DSSSAYLKHLAYNTAKTGWNVVISNHRGLGGVSVTSDRFYNAGWTEDIRVVLGYLQQKYPRAPLFAIGTSIGANVLVKYL 243
Cdd:COG0429     73 SSDSHYARGLARALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  244 GEEGERTP-LRGAVAICSPWDLLIGdrfiCRTLKQ---KLYDKALTIGLQGYAQLHEPQFLRLANWEGIKKSRSIRDFDN 319
Cdd:COG0429    153 GEQGDDAPpLKAAVAVSPPLDLAAS----ADRLERgfnRLYQRYFLRSLKRKLRRKLALFPGLIDLEALKRIRTLREFDD 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  320 HAT-CLVGkFETVDTYYRKSSSTQYVGNVAVPLLCISALDDPLCTKEAIPwDECRANKNIVLATTNHGGHLAFFEGLTGS 398
Cdd:COG0429    229 AYTaPLHG-FKDAEDYYQRASALPFLPQIRVPTLILNAADDPFLPPECLP-EAAELNPNVTLELTKHGGHVGFISGKSPG 306
                          330
                   ....*....|....*
gi 1985651394  399 SLWWV-RATNEFLGA 412
Cdd:COG0429    307 RRYWLeRRILEFLDA 321
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
667-793 5.52e-59

forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 198.80  E-value: 5.52e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  667 IPVFTVLKNGAILKNIFVVNSRDFSsperigstvsddddEVEEILVVGRHPDCDILLTHPSISRFHLEIRSISSRQKLSV 746
Cdd:cd22691      1 IPVLTVLKNGSVLKNIFLHGKFSKS--------------EEEDILVVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITL 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1985651394  747 TDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGSTRIYRLHWIPLS 793
Cdd:cd22691     67 TDLSSVHGTWVNGQRIEPGVPVELEEGDTVRLGASTRVYRLHWIPVS 113
TMEM18 pfam14770
Transmembrane protein 18; The function of this family is not known, however it is predicted to ...
533-650 1.09e-57

Transmembrane protein 18; The function of this family is not known, however it is predicted to be a three-pass membrane protein.


Pssm-ID: 405460  Cd Length: 118  Bit Score: 195.51  E-value: 1.09e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  533 GFFHAIDWKEPWIMGLMAFHALLLLVTLLSRRHLNFHMFLFLLALAGVYFAENLNRELRKNWKSFSTQNYFDSQGVFLSV 612
Cdd:pfam14770    1 GFLHAVDWSEPWLIGLIAFHVLLLVLALLTRRSYNFQMVLFLLLLLLVYFAEYINELAARNWRSFSKQNYFDSRGLFISV 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1985651394  613 LWSGPLLVIAMIILINTLFSLCYLIVKWKRAELRHRAR 650
Cdd:pfam14770   81 VFSGPLLLNCLIILVNWLYQTVSLMVELKRAQLKRRAR 118
InfC COG0290
Translation initiation factor IF-3 [Translation, ribosomal structure and biogenesis]; ...
2191-2308 9.01e-33

Translation initiation factor IF-3 [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-3 is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440059  Cd Length: 175  Bit Score: 126.34  E-value: 9.01e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2191 SDGPRLNEKITGDYVRLVSEEG--HCVVSLREALRRAKELECDLVEVQRDAKPPVCKIV---KYSLEQYKKAKvgkeraK 2265
Cdd:COG0290      6 KKEPRINEEIRAPEVRLIGEDGeqLGIVSTREALRLAEEAGLDLVEISPNAKPPVCKIMdygKFKYEQQKKAK------E 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1985651394 2266 AKRAEAIrPEVKEIRFTPKIEAKDLKFKSDQALKLMESGYRVK 2308
Cdd:COG0290     80 AKKKQKV-IEVKEIKFRPNIDEHDYETKLKNARRFLEEGDKVK 121
PIN_Smg5-6-like cd09880
VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related ...
1895-2061 3.20e-31

VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related proteins; PIN (PilT N terminus) domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and homologs are included in this family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo. Many of the bacterial homologs in this group have an N-terminal PIN domain and a C-terminal PhoH-like ATPase domain.


Pssm-ID: 350228  Cd Length: 152  Bit Score: 120.86  E-value: 3.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1895 VVDTSSLLDKESRkpLHLLQGLKGTHLVLPRTVLREVNEVKRSRSFLfrrrTEMASSALDWIEECKVNTKWWIQVQSPSE 1974
Cdd:cd09880      1 VFDTNILLSHLDV--LKLLVESGKWTVVIPLIVITELDGLKKNPDPL----GPKARSALRYIEACLKKHSRWLRVQTSKG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1975 ETKATAPTPPVTpqsngsafpfslhwNNYAPEIDSPTSEDQVLECALLYRNRNRD-----EKLVLLSNDVTLKIKAMAEG 2049
Cdd:cd09880     75 NYLADLTIRSEQ--------------LSDASELRRRNNDDRILECALWQQKHFVDredgdGKVVLVTNDRNLRLKARARG 140
                          170
                   ....*....|..
gi 1985651394 2050 VICETPQEFYES 2061
Cdd:cd09880    141 VEAVTVKELLKS 152
PIN_4 pfam13638
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ...
1894-2054 3.57e-24

PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).


Pssm-ID: 433369  Cd Length: 131  Bit Score: 100.00  E-value: 3.57e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1894 IVVDTSSLLDKesrkPLHLLQGLKGTHLVLPRTVLREVNEVKRSRSFLFRRRTEMASSALDWIEECKVNTKWWIQVQSPS 1973
Cdd:pfam13638    1 YVLDTNVLLHD----PDALFNFGEENDVVIPITVLEELDGLKKGSDESGRELARLARQANRWLDELLENNGGRLRGQTLD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1974 EEtkataptppvtpqsngsafpfslhwnnyAPEIDSPTSEDQVLECALLYRNRNRDEKLVLLSNDVTLKIKAMAEGVICE 2053
Cdd:pfam13638   77 ER----------------------------LPPDPFDKNDNRILAVALYLKEELPDRPVILVSKDINLRIKADALGIPAE 128

                   .
gi 1985651394 2054 T 2054
Cdd:pfam13638  129 D 129
infC TIGR00168
translation initiation factor IF-3; infC uses abnormal initiation codons such as AUA, AUC, and ...
2196-2308 3.61e-23

translation initiation factor IF-3; infC uses abnormal initiation codons such as AUA, AUC, and CUG which render its expression particularly sensitive to excess of its gene product IF-3 thereby regulating its own expression [Protein synthesis, Translation factors]


Pssm-ID: 129272  Cd Length: 165  Bit Score: 98.62  E-value: 3.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2196 LNEKITGDYVRLVSEEGHC--VVSLREALRRAKELECDLVEVQRDAKPPVCKIV---KYSLEQYKKAKVGKERAKAKrae 2270
Cdd:TIGR00168    1 INERIRFNEVRLIDENGEQlgIVSREEALEIAEEAGLDLVLISPNAKPPVCKIMdygKYKYEQEKKKKEAKKNQKII--- 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1985651394 2271 airpEVKEIRFTPKIEAKDLKFKSDQALKLMESGYRVK 2308
Cdd:TIGR00168   78 ----QVKEVKMRPTIDEHDLQFKLKQAIRFLEKGDKVK 111
IF3_N pfam05198
Translation initiation factor IF-3, N-terminal domain;
2196-2262 1.63e-22

Translation initiation factor IF-3, N-terminal domain;


Pssm-ID: 461584  Cd Length: 70  Bit Score: 93.25  E-value: 1.63e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985651394 2196 LNEKITGDYVRLVSEEG--HCVVSLREALRRAKELECDLVEVQRDAKPPVCKIVKYSLEQYKKAKVGKE 2262
Cdd:pfam05198    1 INEEIRAREVRLIDEDGeqLGVMSTREALRLAEEAGLDLVEVSPNAKPPVCKIMDYGKFKYEQQKKEKE 69
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
708-787 7.12e-18

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 80.77  E-value: 7.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  708 EEILVVGRHPDCDILLTHPSISRFHLEIRSISSRqkLSVTDLSSVHGTWVRDLRVEphTCMEVEEGDTIRIGGSTRIYRL 787
Cdd:COG1716     20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGG--WVLEDLGSTNGTFVNGQRVT--EPAPLRDGDVIRLGKTELRFRL 95
infC CHL00199
translation initiation factor 3; Provisional
2184-2310 2.28e-16

translation initiation factor 3; Provisional


Pssm-ID: 164575  Cd Length: 182  Bit Score: 79.52  E-value: 2.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2184 KKEAEVDSDGPRLNEKITGDYVRLVSEEGH--CVVSLREALRRAKELECDLVEVQRDAKPPVCKIVKYSLEQYKKAKvgk 2261
Cdd:CHL00199     6 KNSKKLSRDLPLINERIRFPKVRVIDDSGEqlGIFTSEQAIQLAANQGLDLVLVSEKSDPPVCRIIDYGKYKFTQEK--- 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1985651394 2262 eRAKAKRAEAIRPEVKEIRFTPKIEAKDLKFKSDQALKLMESGYRVKCN 2310
Cdd:CHL00199    83 -RAKEAKKKQHNSSIKEVKMRYKIEEHDYKVRINQAFKFLQAGDKVKAT 130
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
712-778 1.46e-14

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 70.30  E-value: 1.46e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985651394  712 VVGRHPDCDILLTHPSISRFHLEIRSISSRQkLSVTDLSSVHGTWVRDLRVEPHTCmEVEEGDTIRI 778
Cdd:pfam00498    2 TIGRSPDCDIVLDDPSVSRRHAEIRYDGGGR-FYLEDLGSTNGTFVNGQRLGPEPV-RLKDGDVIRL 66
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
2379-2576 9.69e-14

Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 and P30 proteins. P30 has been found to be membrane associated and localized on the tip organelle. It is thought that it is important in cytadherence and virulence. The N-terminus contains two predicted transmembrane helices followed by a long region of a short 6 residue proline rich repeat.


Pssm-ID: 429374 [Multi-domain]  Cd Length: 275  Bit Score: 74.23  E-value: 9.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2379 KSARVKEEKSDSSEAGES--TVDDHGDIEKCEPGFSVDQAQPVQVQNTYAKREPgsefsggrdasRFEPRSPnqHVNPQr 2456
Cdd:pfam07271   95 KEKRLLEEKERQEQMAEQlqRISEQQETQAIEPTEQQNTAEPTQPAGVNVANQP-----------QMGINQP--QINPQ- 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2457 prFQAPNQQPTGridpqSPNQPPSAPRPQFPNQ--QPTGRFDPQFPNQPPGPPRRQFPDQAPNQQPTGRFNPQfpnksps 2534
Cdd:pfam07271  161 --FGPNPQQRIG-----FPMQPNMGMRPGFNQMpgMPPNQMRPGFNQMPGMPPRPGFPNPMPNMQPRPGFRPQ------- 226
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1985651394 2535 ppqspfpdQAPNQQPSGPSPNrHIDRQGPPPRFQNQAPNQQP 2576
Cdd:pfam07271  227 --------PGPMGNRPGGGFP-HPGTPMGPNRMPNPGMNQRP 259
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
712-762 1.52e-08

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 52.95  E-value: 1.52e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1985651394   712 VVGRHP-DCDILLTHPSISRFHLEIRSISSRqKLSVTDLSSVHGTWVRDLRV 762
Cdd:smart00240    2 TIGRSSeDCDIQLDGPSISRRHAVIVYDGGG-RFYLIDLGSTNGTFVNGKRI 52
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
156-394 3.66e-08

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 56.74  E-value: 3.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  156 VVIPGLTSDSSSAYlkHLAYNTAKTGWNVVISNHRGLGG--VSVTSDRFYnagwTEDIRVVLGYLQQKYPRAPLFAIGTS 233
Cdd:pfam00561    4 LLLHGLPGSSDLWR--KLAPALARDGFRVIALDLRGFGKssRPKAQDDYR----TDDLAEDLEYILEALGLEKVNLVGHS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  234 IGANVLVKYLGEEGERtpLRGAVAICSP-----WDLLigDRFIcRTLKQKLYDK----------ALTIG--LQGYAQLHE 296
Cdd:pfam00561   78 MGGLIALAYAAKYPDR--VKALVLLGALdppheLDEA--DRFI-LALFPGFFDGfvadfapnplGRLVAklLALLLLRLR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  297 PQFlRLANWEGIKKSRSIRDFDNHATCLVGKFETVDTYYRKSSSTQYvgnvAVPLLCISALDDPLcTKEAIPWDECRANK 376
Cdd:pfam00561  153 LLK-ALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRL----DEPTLIIWGDQDPL-VPPQALEKLAQLFP 226
                          250
                   ....*....|....*...
gi 1985651394  377 NIVLATTNHGGHLAFFEG 394
Cdd:pfam00561  227 NARLVVIPDAGHFAFLEG 244
PHA03247 PHA03247
large tegument protein UL36; Provisional
2430-2618 3.04e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 3.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2430 PGSEFSGgRDASRFEPRSPNQHVNPQRPRFQAPNQQPTGRIDPQSPNQPPSAPRPQFPNQ---QPTGRFDPQFPNQPPGP 2506
Cdd:PHA03247  2858 PGGDVRR-RPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPpqpQPQPPPPPQPQPPPPPP 2936
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2507 PRRQFP-----DQAPNQQPTGRFNPQFPNKSPSPPQSPFPDQAPNQQPS--GPSPNRHIDRQGPPPRFQNQA-------- 2571
Cdd:PHA03247  2937 PRPQPPlapttDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSreAPASSTPPLTGHSLSRVSSWAsslalhee 3016
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985651394 2572 PNQQP-------------------------TGRFEPQPPNPPRAPPRPQTRLPNDTPPTAPGRSGGPASSYG 2618
Cdd:PHA03247  3017 TDPPPvslkqtlwppddtedsdadslfdsdSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFG 3088
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
2445-2516 4.58e-06

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 49.02  E-value: 4.58e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985651394  2445 PRSPNQHVNPQRPRFQAPNQQPtgridpqspnQPPSAPRPQFP-NQQPTGRFDPQFPNQPPGPPrrQFPDQAP 2516
Cdd:smart00818   81 SMTPTQHHQPNLPQPAQQPFQP----------QPLQPPQPQQPmQPQPPVHPIPPLPPQPPLPP--MFPMQPL 141
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
2339-2580 9.10e-05

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 47.75  E-value: 9.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2339 DALVEFGPEADRKsAVVIVRHAKFGPPKKGGVKKLKDIDIKSARVKEEKSDSSEAGESTVDDHGdiEKCEPGFSVDQAQP 2418
Cdd:COG5180    190 DALKDSPEKLDRP-KVEVKDEAQEEPPDLTGGADHPRPEAASSPKVDPPSTSEARSRPATVDAQ--PEMRPPADAKERRR 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2419 VQVQNTYAKREPGSEFSGGR-----DASRFEPRSPNQH-------------------VNPQRPRFQAPNQQPTGRIDPQS 2474
Cdd:COG5180    267 AAIGDTPAAEPPGLPVLEAGsepqsDAPEAETARPIDVkgvasappatrpvrppggaRDPGTPRPGQPTERPAGVPEAAS 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2475 P-NQPPSAPRPQFPnqqptgrfdpqfpnQPPGPPRRQF-PDQAPNQQPTGRFNPQFpnkspsppqspfpdQAPNQQPSGP 2552
Cdd:COG5180    347 DaGQPPSAYPPAEE--------------AVPGKPLEQGaPRPGSSGGDGAPFQPPN--------------GAPQPGLGRR 398
                          250       260
                   ....*....|....*....|....*...
gi 1985651394 2553 SPNRHIDRQGPPPRFQNQAPNQQPTGRF 2580
Cdd:COG5180    399 GAPGPPMGAGDLVQAALDGGGRETASLG 426
 
Name Accession Description Interval E-value
PLN02511 PLN02511
hydrolase
73-394 4.79e-82

hydrolase


Pssm-ID: 215282 [Multi-domain]  Cd Length: 388  Bit Score: 276.28  E-value: 4.79e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394   73 GVVSRCRILHGRYVATPWLASPHIQTCFLNFHGLPPVFSYRRQLFLASDGGTIALDWVTNSDVldggfqnqseiTKEDTT 152
Cdd:PLN02511    32 SFLPKFKSLERPYDAFPLLGNRHVETIFASFFRSLPAVRYRRECLRTPDGGAVALDWVSGDDR-----------ALPADA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  153 PIAVVIPGLTSDSSSAYLKHLAYNTAKTGWNVVISNHRGLGGVSVTSDRFYNAGWTEDIRVVLGYLQQKYPRAPLFAIGT 232
Cdd:PLN02511   101 PVLILLPGLTGGSDDSYVRHMLLRARSKGWRVVVFNSRGCADSPVTTPQFYSASFTGDLRQVVDHVAGRYPSANLYAAGW 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  233 SIGANVLVKYLGEEGERTPLRGAVAICSPWDLLIGDRFIcRTLKQKLYDKALTIGLQGYAQLHEPQFLRLA---NWEGIK 309
Cdd:PLN02511   181 SLGANILVNYLGEEGENCPLSGAVSLCNPFDLVIADEDF-HKGFNNVYDKALAKALRKIFAKHALLFEGLGgeyNIPLVA 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  310 KSRSIRDFDNHATCLVGKFETVDTYYRKSSSTQYVGNVAVPLLCISALDDPLCTKEAIPWDECRANKNIVLATTNHGGHL 389
Cdd:PLN02511   260 NAKTVRDFDDGLTRVSFGFKSVDAYYSNSSSSDSIKHVRVPLLCIQAANDPIAPARGIPREDIKANPNCLLIVTPSGGHL 339

                   ....*
gi 1985651394  390 AFFEG 394
Cdd:PLN02511   340 GWVAG 344
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
84-412 1.02e-76

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 258.15  E-value: 1.02e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394   84 RYVATPWLASPHIQTCFLNFHGLPPVFSYRRQLFLASDGGTIALDWVTNSDvldggfqnqseitkeDTTPIAVVIPGLTS 163
Cdd:COG0429      8 PFRPPWWLRNGHLQTIYPSLFRRRPALPYRRERLELPDGDFVDLDWSDPPA---------------PSKPLVVLLHGLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  164 DSSSAYLKHLAYNTAKTGWNVVISNHRGLGGVSVTSDRFYNAGWTEDIRVVLGYLQQKYPRAPLFAIGTSIGANVLVKYL 243
Cdd:COG0429     73 SSDSHYARGLARALYARGWDVVRLNFRGCGGEPNLLPRLYHSGDTEDLVWVLAHLRARYPYAPLYAVGFSLGGNLLLKYL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  244 GEEGERTP-LRGAVAICSPWDLLIGdrfiCRTLKQ---KLYDKALTIGLQGYAQLHEPQFLRLANWEGIKKSRSIRDFDN 319
Cdd:COG0429    153 GEQGDDAPpLKAAVAVSPPLDLAAS----ADRLERgfnRLYQRYFLRSLKRKLRRKLALFPGLIDLEALKRIRTLREFDD 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  320 HAT-CLVGkFETVDTYYRKSSSTQYVGNVAVPLLCISALDDPLCTKEAIPwDECRANKNIVLATTNHGGHLAFFEGLTGS 398
Cdd:COG0429    229 AYTaPLHG-FKDAEDYYQRASALPFLPQIRVPTLILNAADDPFLPPECLP-EAAELNPNVTLELTKHGGHVGFISGKSPG 306
                          330
                   ....*....|....*
gi 1985651394  399 SLWWV-RATNEFLGA 412
Cdd:COG0429    307 RRYWLeRRILEFLDA 321
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
667-793 5.52e-59

forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 198.80  E-value: 5.52e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  667 IPVFTVLKNGAILKNIFVVNSRDFSsperigstvsddddEVEEILVVGRHPDCDILLTHPSISRFHLEIRSISSRQKLSV 746
Cdd:cd22691      1 IPVLTVLKNGSVLKNIFLHGKFSKS--------------EEEDILVVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITL 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1985651394  747 TDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGSTRIYRLHWIPLS 793
Cdd:cd22691     67 TDLSSVHGTWVNGQRIEPGVPVELEEGDTVRLGASTRVYRLHWIPVS 113
TMEM18 pfam14770
Transmembrane protein 18; The function of this family is not known, however it is predicted to ...
533-650 1.09e-57

Transmembrane protein 18; The function of this family is not known, however it is predicted to be a three-pass membrane protein.


Pssm-ID: 405460  Cd Length: 118  Bit Score: 195.51  E-value: 1.09e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  533 GFFHAIDWKEPWIMGLMAFHALLLLVTLLSRRHLNFHMFLFLLALAGVYFAENLNRELRKNWKSFSTQNYFDSQGVFLSV 612
Cdd:pfam14770    1 GFLHAVDWSEPWLIGLIAFHVLLLVLALLTRRSYNFQMVLFLLLLLLVYFAEYINELAARNWRSFSKQNYFDSRGLFISV 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1985651394  613 LWSGPLLVIAMIILINTLFSLCYLIVKWKRAELRHRAR 650
Cdd:pfam14770   81 VFSGPLLLNCLIILVNWLYQTVSLMVELKRAQLKRRAR 118
PRK10985 PRK10985
putative hydrolase; Provisional
85-394 2.21e-33

putative hydrolase; Provisional


Pssm-ID: 182883  Cd Length: 324  Bit Score: 133.16  E-value: 2.21e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394   85 YVATPWLASPHIQTcflnfhgLPPVFSYRRQLFLA-------SDGGTIALDWVTNSDvldggfQNQSEitkedttPIAVV 157
Cdd:PRK10985     4 FTPMRGASNPHLQT-------LLPRLIRRKVLFTPywqrlelPDGDFVDLAWSEDPA------QARHK-------PRLVL 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  158 IPGLTSDSSSAYLKHLAYNTAKTGWNVVISNHRGLGGVSVTSDRFYNAGWTEDIRVVLGYLQQKYPRAPLFAIGTSIGAN 237
Cdd:PRK10985    64 FHGLEGSFNSPYAHGLLEAAQKRGWLGVVMHFRGCSGEPNRLHRIYHSGETEDARFFLRWLQREFGHVPTAAVGYSLGGN 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  238 VLVKYLGEEGERTPLRGAVAICSPWDL------------LIGDRFICRTLKQ------KLYDKALTIGLQgyaqlhepqf 299
Cdd:PRK10985   144 MLACLLAKEGDDLPLDAAVIVSAPLMLeacsyrmeqgfsRVYQRYLLNLLKAnaarklAAYPGTLPINLA---------- 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  300 lrlanweGIKKSRSIRDFDNHATCLVGKFETVDTYYRKSSSTQYVGNVAVPLLCISALDDPLCTKEAIPwDECRANKNIV 379
Cdd:PRK10985   214 -------QLKSVRRLREFDDLITARIHGFADAIDYYRQCSALPLLNQIRKPTLIIHAKDDPFMTHEVIP-KPESLPPNVE 285
                          330
                   ....*....|....*
gi 1985651394  380 LATTNHGGHLAFFEG 394
Cdd:PRK10985   286 YQLTEHGGHVGFVGG 300
InfC COG0290
Translation initiation factor IF-3 [Translation, ribosomal structure and biogenesis]; ...
2191-2308 9.01e-33

Translation initiation factor IF-3 [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-3 is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440059  Cd Length: 175  Bit Score: 126.34  E-value: 9.01e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2191 SDGPRLNEKITGDYVRLVSEEG--HCVVSLREALRRAKELECDLVEVQRDAKPPVCKIV---KYSLEQYKKAKvgkeraK 2265
Cdd:COG0290      6 KKEPRINEEIRAPEVRLIGEDGeqLGIVSTREALRLAEEAGLDLVEISPNAKPPVCKIMdygKFKYEQQKKAK------E 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1985651394 2266 AKRAEAIrPEVKEIRFTPKIEAKDLKFKSDQALKLMESGYRVK 2308
Cdd:COG0290     80 AKKKQKV-IEVKEIKFRPNIDEHDYETKLKNARRFLEEGDKVK 121
PIN_Smg5-6-like cd09880
VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related ...
1895-2061 3.20e-31

VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related proteins; PIN (PilT N terminus) domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and homologs are included in this family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo. Many of the bacterial homologs in this group have an N-terminal PIN domain and a C-terminal PhoH-like ATPase domain.


Pssm-ID: 350228  Cd Length: 152  Bit Score: 120.86  E-value: 3.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1895 VVDTSSLLDKESRkpLHLLQGLKGTHLVLPRTVLREVNEVKRSRSFLfrrrTEMASSALDWIEECKVNTKWWIQVQSPSE 1974
Cdd:cd09880      1 VFDTNILLSHLDV--LKLLVESGKWTVVIPLIVITELDGLKKNPDPL----GPKARSALRYIEACLKKHSRWLRVQTSKG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1975 ETKATAPTPPVTpqsngsafpfslhwNNYAPEIDSPTSEDQVLECALLYRNRNRD-----EKLVLLSNDVTLKIKAMAEG 2049
Cdd:cd09880     75 NYLADLTIRSEQ--------------LSDASELRRRNNDDRILECALWQQKHFVDredgdGKVVLVTNDRNLRLKARARG 140
                          170
                   ....*....|..
gi 1985651394 2050 VICETPQEFYES 2061
Cdd:cd09880    141 VEAVTVKELLKS 152
PIN_4 pfam13638
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ...
1894-2054 3.57e-24

PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).


Pssm-ID: 433369  Cd Length: 131  Bit Score: 100.00  E-value: 3.57e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1894 IVVDTSSLLDKesrkPLHLLQGLKGTHLVLPRTVLREVNEVKRSRSFLFRRRTEMASSALDWIEECKVNTKWWIQVQSPS 1973
Cdd:pfam13638    1 YVLDTNVLLHD----PDALFNFGEENDVVIPITVLEELDGLKKGSDESGRELARLARQANRWLDELLENNGGRLRGQTLD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1974 EEtkataptppvtpqsngsafpfslhwnnyAPEIDSPTSEDQVLECALLYRNRNRDEKLVLLSNDVTLKIKAMAEGVICE 2053
Cdd:pfam13638   77 ER----------------------------LPPDPFDKNDNRILAVALYLKEELPDRPVILVSKDINLRIKADALGIPAE 128

                   .
gi 1985651394 2054 T 2054
Cdd:pfam13638  129 D 129
infC TIGR00168
translation initiation factor IF-3; infC uses abnormal initiation codons such as AUA, AUC, and ...
2196-2308 3.61e-23

translation initiation factor IF-3; infC uses abnormal initiation codons such as AUA, AUC, and CUG which render its expression particularly sensitive to excess of its gene product IF-3 thereby regulating its own expression [Protein synthesis, Translation factors]


Pssm-ID: 129272  Cd Length: 165  Bit Score: 98.62  E-value: 3.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2196 LNEKITGDYVRLVSEEGHC--VVSLREALRRAKELECDLVEVQRDAKPPVCKIV---KYSLEQYKKAKVGKERAKAKrae 2270
Cdd:TIGR00168    1 INERIRFNEVRLIDENGEQlgIVSREEALEIAEEAGLDLVLISPNAKPPVCKIMdygKYKYEQEKKKKEAKKNQKII--- 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1985651394 2271 airpEVKEIRFTPKIEAKDLKFKSDQALKLMESGYRVK 2308
Cdd:TIGR00168   78 ----QVKEVKMRPTIDEHDLQFKLKQAIRFLEKGDKVK 111
IF3_N pfam05198
Translation initiation factor IF-3, N-terminal domain;
2196-2262 1.63e-22

Translation initiation factor IF-3, N-terminal domain;


Pssm-ID: 461584  Cd Length: 70  Bit Score: 93.25  E-value: 1.63e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985651394 2196 LNEKITGDYVRLVSEEG--HCVVSLREALRRAKELECDLVEVQRDAKPPVCKIVKYSLEQYKKAKVGKE 2262
Cdd:pfam05198    1 INEEIRAREVRLIDEDGeqLGVMSTREALRLAEEAGLDLVEVSPNAKPPVCKIMDYGKFKYEQQKKEKE 69
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
670-787 7.42e-22

forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438729 [Multi-domain]  Cd Length: 106  Bit Score: 92.62  E-value: 7.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  670 FTVLKNGAILKNIfVVNSRDFssperigstvsddddeveeiLVVGRHPDCDILLTHPSISRFH--LEIRSISSRQKLS-- 745
Cdd:cd22677      4 LEVLKNGVIVETL-DLNGKSF--------------------YVFGRLPGCDVVLEHPSISRYHavLQYRGDADDHDGGfy 62
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1985651394  746 VTDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGSTRIYRL 787
Cdd:cd22677     63 LYDLGSTHGTFLNKQRIPPKQYYRLRVGHVLKFGGSTRLYIL 104
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
699-788 2.62e-18

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 81.94  E-value: 2.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  699 TVSDDDDEVEEI------LVVGRHPDCDILLTHPSISRFHLEIRSISSRqkLSVTDLSSVHGTWVRDLRVEPHTcmEVEE 772
Cdd:cd00060      3 IVLDGDGGGREFpltkgvVTIGRSPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRITPPV--PLQD 78
                           90
                   ....*....|....*.
gi 1985651394  773 GDTIRIGGSTriYRLH 788
Cdd:cd00060     79 GDVIRLGDTT--FRFE 92
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
708-787 7.12e-18

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 80.77  E-value: 7.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  708 EEILVVGRHPDCDILLTHPSISRFHLEIRSISSRqkLSVTDLSSVHGTWVRDLRVEphTCMEVEEGDTIRIGGSTRIYRL 787
Cdd:COG1716     20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGG--WVLEDLGSTNGTFVNGQRVT--EPAPLRDGDVIRLGKTELRFRL 95
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
714-787 1.02e-17

forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438726 [Multi-domain]  Cd Length: 108  Bit Score: 80.77  E-value: 1.02e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985651394  714 GRHPD-CDILLTHPSISRFHLEIRSISSRQKLSVTDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGSTRIYRL 787
Cdd:cd22674     32 GRNSDvCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEPHKPQQLPIDSTLRFGASTRRYIL 106
infC CHL00199
translation initiation factor 3; Provisional
2184-2310 2.28e-16

translation initiation factor 3; Provisional


Pssm-ID: 164575  Cd Length: 182  Bit Score: 79.52  E-value: 2.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2184 KKEAEVDSDGPRLNEKITGDYVRLVSEEGH--CVVSLREALRRAKELECDLVEVQRDAKPPVCKIVKYSLEQYKKAKvgk 2261
Cdd:CHL00199     6 KNSKKLSRDLPLINERIRFPKVRVIDDSGEqlGIFTSEQAIQLAANQGLDLVLVSEKSDPPVCRIIDYGKYKFTQEK--- 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1985651394 2262 eRAKAKRAEAIRPEVKEIRFTPKIEAKDLKFKSDQALKLMESGYRVKCN 2310
Cdd:CHL00199    83 -RAKEAKKKQHNSSIKEVKMRYKIEEHDYKVRINQAFKFLQAGDKVKAT 130
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
712-778 1.46e-14

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 70.30  E-value: 1.46e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985651394  712 VVGRHPDCDILLTHPSISRFHLEIRSISSRQkLSVTDLSSVHGTWVRDLRVEPHTCmEVEEGDTIRI 778
Cdd:pfam00498    2 TIGRSPDCDIVLDDPSVSRRHAEIRYDGGGR-FYLEDLGSTNGTFVNGQRLGPEPV-RLKDGDVIRL 66
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
2379-2576 9.69e-14

Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 and P30 proteins. P30 has been found to be membrane associated and localized on the tip organelle. It is thought that it is important in cytadherence and virulence. The N-terminus contains two predicted transmembrane helices followed by a long region of a short 6 residue proline rich repeat.


Pssm-ID: 429374 [Multi-domain]  Cd Length: 275  Bit Score: 74.23  E-value: 9.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2379 KSARVKEEKSDSSEAGES--TVDDHGDIEKCEPGFSVDQAQPVQVQNTYAKREPgsefsggrdasRFEPRSPnqHVNPQr 2456
Cdd:pfam07271   95 KEKRLLEEKERQEQMAEQlqRISEQQETQAIEPTEQQNTAEPTQPAGVNVANQP-----------QMGINQP--QINPQ- 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2457 prFQAPNQQPTGridpqSPNQPPSAPRPQFPNQ--QPTGRFDPQFPNQPPGPPRRQFPDQAPNQQPTGRFNPQfpnksps 2534
Cdd:pfam07271  161 --FGPNPQQRIG-----FPMQPNMGMRPGFNQMpgMPPNQMRPGFNQMPGMPPRPGFPNPMPNMQPRPGFRPQ------- 226
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1985651394 2535 ppqspfpdQAPNQQPSGPSPNrHIDRQGPPPRFQNQAPNQQP 2576
Cdd:pfam07271  227 --------PGPMGNRPGGGFP-HPGTPMGPNRMPNPGMNQRP 259
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
708-788 6.52e-12

forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438722 [Multi-domain]  Cd Length: 105  Bit Score: 64.17  E-value: 6.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  708 EEILVVGRHPDCDILLTHPSISRFHLEIRSI----SSRQKLSVTDLSSvHGTWVRDLRVEPHTCMEVEEGDTIRIGGSTR 783
Cdd:cd22670     21 NQVITIGRSPSCDIVINDPFVSRTHCRIYSVqfdeSSAPLVYVEDLSS-NGTYLNGKLIGRNNTVLLSDGDVIEIAHSAT 99

                   ....*
gi 1985651394  784 IYRLH 788
Cdd:cd22670    100 FVYVH 104
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
703-787 5.42e-11

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438728 [Multi-domain]  Cd Length: 111  Bit Score: 61.55  E-value: 5.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  703 DDDEVEEILVV--------GRHPD-CDILLTHPSISRFH--LEIRSISSRQKLSVT--------DLSSVHGTWVRDLRVE 763
Cdd:cd22676      7 KGGEQLETIDIhrqsayliGRDRRvADIPLDHPSCSKQHavIQFREVEKRNEGDVIenirpyiiDLGSTNGTFLNGEKIE 86
                           90       100
                   ....*....|....*....|....
gi 1985651394  764 PHTCMEVEEGDTIRIGGSTRIYRL 787
Cdd:cd22676     87 PRRYYELREKDVLKFGLSTREYVL 110
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
697-779 3.34e-10

first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438746 [Multi-domain]  Cd Length: 93  Bit Score: 58.88  E-value: 3.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  697 GSTVSDDDDEVeeilVVGRHPDCDILLTHPSISRFHLEIRSISSRQKlsVTDLSSVHGTWVRDLRVEPhtcMEVEEGDTI 776
Cdd:cd22694      8 GELRFDPGSSV----RIGRDPDADVRLDDPRVSRRHALLEFDGDGWV--YTDLGSRNGTYLNGRRVQQ---VKLSDGTRV 78

                   ...
gi 1985651394  777 RIG 779
Cdd:cd22694     79 RLG 81
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
691-784 4.45e-10

forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438732 [Multi-domain]  Cd Length: 96  Bit Score: 58.51  E-value: 4.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  691 SSPERIGSTVSDDDDEVeeilVVGRHPDCDILLTHPSISRFHLEIRSISsrQKLSVTDLSSVHGTWVRDL-RVEPHtcME 769
Cdd:cd22680      7 SSPNLTGKKFPFDFSSV----SIGRDPENVIVIPDPFVSRNHARITVDS--NEIYIEDLGSTNGTFVNDFkRIKGP--AK 78
                           90
                   ....*....|....*
gi 1985651394  770 VEEGDTIRIGGSTRI 784
Cdd:cd22680     79 LHPNDIIKLGRTTVL 93
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
708-780 8.09e-10

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 57.99  E-value: 8.09e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985651394  708 EEILVVGRHPDCDILLTHPSISRFHLEIRsISSRQKLSVTDLSSVHGTWVRDLRVEphTCMEVEEGDTIRIGG 780
Cdd:cd22673     20 KKSCTFGRDLSCDIRIQLPGVSREHCRIE-VDENGKAYLENLSTTNPTLVNGKAIE--KSAELKDGDVITIGG 89
FHA_Cep170 cd22704
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ...
708-787 1.22e-09

forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438756 [Multi-domain]  Cd Length: 102  Bit Score: 57.71  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  708 EEILVVGRHpDCDILLTHPSISRFHLEIRSISSRQKLSVTDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGSTRIYRL 787
Cdd:cd22704     16 RSMLFVGRE-DCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIPEQTYITLKLGDSIRFGYDTNVYRF 94
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
712-789 1.40e-09

forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438719 [Multi-domain]  Cd Length: 108  Bit Score: 57.72  E-value: 1.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  712 VVGRhPDCDILLTH-PSISRFHLEIR---------SISSRQKLSVTDLSSvHGTWVRDLRVEPHTCMEVEEGDTIRIGGS 781
Cdd:cd22667     23 TVGR-KDCDIIIVDdSSISRKHATLTvlhpeanlsDPDTRPELTLKDLSK-YGTFVNGEKLKGGSEVTLKDGDVITFGVL 100

                   ....*...
gi 1985651394  782 TRIYRLHW 789
Cdd:cd22667    101 GSKFRVEY 108
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
703-779 2.12e-09

forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438715 [Multi-domain]  Cd Length: 110  Bit Score: 56.98  E-value: 2.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  703 DDDEVeeilVVGRHPD--CDILLTHP-SISRFHLEIRSISSRQkLSVTDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIG 779
Cdd:cd22663     19 DGKEV----TVGRGLGvtYQLVSTCPlMISRNHCVLKKNDEGQ-WTIKDNKSLNGVWVNGERIEPLKPYPLNEGDLIQLG 93
FHA_RAD53-like_rpt1 cd22689
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
698-779 6.22e-09

first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the first one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438741 [Multi-domain]  Cd Length: 132  Bit Score: 56.51  E-value: 6.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  698 STVSDDDDEVEEILVVGRHPDCDILLTHPSISRFHLEI---RSISSRQKLSVTDLSSvHGTWVRDLRVEPHTCMEVEEGD 774
Cdd:cd22689     34 SQVLKEKRSIKKVWTFGRHPACDYHLGNSRLSNKHFQIllgESDPSDGNVLLNDISS-NGTWLNGQRLEKNSNQLLSQGD 112

                   ....*
gi 1985651394  775 TIRIG 779
Cdd:cd22689    113 EITIG 117
PIN_Swt1-like cd18727
VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; ...
1895-2058 6.59e-09

VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; Saccharomyces cerevisiae mRNA-processing endoribonuclease Swt1p plays an important role in quality control of nuclear mRNPs in eukaryotes. Human transcriptional protein SWT1 (RNA endoribonuclease homolog, also known as HsSwt1, C1orf26, and chromosome 1 open reading frame 26) is an RNA endonuclease that participates in quality control of nuclear mRNPs and can associate with the nuclear pore complex (NPC). This subfamily belongs to the Smg5 and Smg6-like PIN domain family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo.


Pssm-ID: 350294  Cd Length: 141  Bit Score: 56.80  E-value: 6.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1895 VVDTSSLLDKesrkpLHLLQGLKGTH--------LVLPRTVLREVNEVKRSRSFLFRRRteMASSALDWIEECKVNTKWW 1966
Cdd:cd18727      1 VLDTNVLISH-----LDLLKQLVEDVeklslpvvIVIPWVVLQELDGLKKSKRKSSLGW--LARRASTWLLEKLRSKHPR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 1967 IQVQSPSEetkatAPTPPVTPQSNGsafpfslhwnnyapeiDsptseDQVLECALLYRNRnRDEKLVLLSNDVTLKIKAM 2046
Cdd:cd18727     74 VRGQALSE-----TLRASGDPGESN----------------D-----DAILDCCLYFQEK-YGAPVVLLSNDKNLCNKAL 126
                          170
                   ....*....|..
gi 1985651394 2047 AEGVICETPQEF 2058
Cdd:cd18727    127 INGIPTISPEEG 138
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
113-262 9.19e-09

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 58.09  E-value: 9.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  113 RRQLFLASDGGTIALdwvtnsdvldggfqnQSEITKEDTTPIAVVIPGLTSdsSSAYLKHLAYNTAKTGWNVVISNHRGL 192
Cdd:COG2267      4 RLVTLPTRDGLRLRG---------------RRWRPAGSPRGTVVLVHGLGE--HSGRYAELAEALAAAGYAVLAFDLRGH 66
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985651394  193 GGVSVTSDRFYN-AGWTEDIRVVLGYLQQKyPRAPLFAIGTSIGANVLVKYLGEEGERtpLRGAVAiCSPW 262
Cdd:COG2267     67 GRSDGPRGHVDSfDDYVDDLRAALDALRAR-PGLPVVLLGHSMGGLIALLYAARYPDR--VAGLVL-LAPA 133
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
708-779 1.18e-08

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 54.57  E-value: 1.18e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985651394  708 EEILVVGRHPDCDILLTHPSISRFHLEIRSISSRqkLSVTDLSSVHGTWVRDLRVEPHTcMEVEEGDTIRIG 779
Cdd:pfam16697   16 GGRYRIGSDPDCDIVLSDKEVSRVHLKLEVDDEG--WRLDDLGSGNGTLVNGQRVTELG-IALRPGDRIELG 84
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
2447-2576 1.44e-08

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 56.58  E-value: 1.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2447 SPNQHVNPQRPRfQAPNQQPTGRIDPQSPNQPPSAPRPQFPNQQ--PTGRfDPQFPNQPPGPPRRQFPDQAPNQQPTGrf 2524
Cdd:pfam15240   28 SPSLISEEEGQS-QQGGQGPQGPPPGGFPPQPPASDDPPGPPPPggPQQP-PPQGGKQKPQGPPPQGGPRPPPGKPQG-- 103
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1985651394 2525 NPQFPNKSPSPPQSPFPDQAPNQQPSGPSPN-RHIDRQGPPPRFQNQAPNQQP 2576
Cdd:pfam15240  104 PPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQgGNQQGPPPPPPGNPQGPPQRP 156
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
712-762 1.52e-08

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 52.95  E-value: 1.52e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1985651394   712 VVGRHP-DCDILLTHPSISRFHLEIRSISSRqKLSVTDLSSVHGTWVRDLRV 762
Cdd:smart00240    2 TIGRSSeDCDIQLDGPSISRRHAVIVYDGGG-RFYLIDLGSTNGTFVNGKRI 52
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
156-394 3.66e-08

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 56.74  E-value: 3.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  156 VVIPGLTSDSSSAYlkHLAYNTAKTGWNVVISNHRGLGG--VSVTSDRFYnagwTEDIRVVLGYLQQKYPRAPLFAIGTS 233
Cdd:pfam00561    4 LLLHGLPGSSDLWR--KLAPALARDGFRVIALDLRGFGKssRPKAQDDYR----TDDLAEDLEYILEALGLEKVNLVGHS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  234 IGANVLVKYLGEEGERtpLRGAVAICSP-----WDLLigDRFIcRTLKQKLYDK----------ALTIG--LQGYAQLHE 296
Cdd:pfam00561   78 MGGLIALAYAAKYPDR--VKALVLLGALdppheLDEA--DRFI-LALFPGFFDGfvadfapnplGRLVAklLALLLLRLR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  297 PQFlRLANWEGIKKSRSIRDFDNHATCLVGKFETVDTYYRKSSSTQYvgnvAVPLLCISALDDPLcTKEAIPWDECRANK 376
Cdd:pfam00561  153 LLK-ALPLLNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRL----DEPTLIIWGDQDPL-VPPQALEKLAQLFP 226
                          250
                   ....*....|....*...
gi 1985651394  377 NIVLATTNHGGHLAFFEG 394
Cdd:pfam00561  227 NARLVVIPDAGHFAFLEG 244
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
696-779 7.16e-08

forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438735 [Multi-domain]  Cd Length: 96  Bit Score: 52.49  E-value: 7.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  696 IGSTVSDDDDEVE----EILVVGRHPDCDILLTHPSISRFHLEIRSISSRqkLSVTDLSSVHGTWVRDLRVEPHTcMEVE 771
Cdd:cd22683      4 VNLIVG*KEQKISitnrNVTTIGRSRSCDLVLSDPSISRFHAELRLEQNG--INVIDNNSANGTFINGKRIKGKT-YILK 80

                   ....*...
gi 1985651394  772 EGDTIRIG 779
Cdd:cd22683     81 NGDIIVFG 88
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
697-779 7.19e-08

forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438736 [Multi-domain]  Cd Length: 94  Bit Score: 52.38  E-value: 7.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  697 GSTVSDDDDEVeeilVVGRHPDCDILLTHPSISRFHLEIRSISSRqkLSVTDLSSVHGTWVRDLRVEPhtcMEVEEGDTI 776
Cdd:cd22684     13 GARFLLDQDVT----TAGRHPESDIFLDDVTVSRRHAEFRRAEGG--FVVRDVGSLNGTYVNRERIDS---AVLRNGDEV 83

                   ...
gi 1985651394  777 RIG 779
Cdd:cd22684     84 QIG 86
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
710-784 7.94e-08

forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.


Pssm-ID: 438737 [Multi-domain]  Cd Length: 130  Bit Score: 53.19  E-value: 7.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  710 ILVVGRHP-DCDILL---THPS-ISRFHLEI---RSISSRQKLSVTDlSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGS 781
Cdd:cd22685     29 EYRIGRNPeVCDVFLcssQHPNlISREHAEIhaeRDGNGNWKVLIED-RSTNGTYVNDVRLQDGQRRELSDGDTITFGHK 107

                   ...
gi 1985651394  782 TRI 784
Cdd:cd22685    108 NGR 110
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
2412-2574 1.10e-07

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 53.89  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2412 SVDQAQPVQVQNTYAKREPGSEFSggRDASRFEPRSPNQHVNPQRPRFQAPNQQPTGRIDPQSPNQPPSapRPQFPNQQp 2491
Cdd:pfam15240   33 SEEEGQSQQGGQGPQGPPPGGFPP--QPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPG--KPQGPPPQ- 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2492 tGRFDPQFPNQPPGPprRQFPDQAPNQQPTGRfNPQfpnkspsppqspFPDQAPNQQPSGPsPNRhidrqgPPPRFQNQA 2571
Cdd:pfam15240  108 -GGNQQQGPPPPGKP--QGPPPQGGGPPPQGG-NQQ------------GPPPPPPGNPQGP-PQR------PPQPGNPQG 164

                   ...
gi 1985651394 2572 PNQ 2574
Cdd:pfam15240  165 PPQ 167
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
2460-2614 1.82e-07

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 53.12  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2460 QAPNQQPTGRIDPQSPNQPPSAPRPQFPNQQPTGRfDPQFPNQPPGPprRQFPDQAPNQQPTGRFNPQfpnkspsppqsp 2539
Cdd:pfam15240   28 SPSLISEEEGQSQQGGQGPQGPPPGGFPPQPPASD-DPPGPPPPGGP--QQPPPQGGKQKPQGPPPQG------------ 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985651394 2540 fPDQAPNQQPSGPSPNRHIDRQGPPPRFQNQAPnQQPTGRFEPQPPNPPRAPPRPQTRlPNDTP--PTAPGRSGGPA 2614
Cdd:pfam15240   93 -GPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGP-PPQGGGPPPQGGNQQGPPPPPPGN-PQGPPqrPPQPGNPQGPP 166
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
707-776 2.97e-07

second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438742 [Multi-domain]  Cd Length: 105  Bit Score: 50.75  E-value: 2.97e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985651394  707 VEEILVVGRHPDCDILLTHPSISRFHLEIRSISSRQKLS---VTDlSSVHGTWVRDLRVEPHTCMEVEEGDTI 776
Cdd:cd22690     17 TQNTTFIGRSKDCDEEITDPRISKHHCIITRKRSGKGLDdvyVTD-TSTNGTFINNNRLGKGSQSLLQDGDEI 88
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
712-779 3.04e-07

forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438717 [Multi-domain]  Cd Length: 97  Bit Score: 50.69  E-value: 3.04e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985651394  712 VVGRHPDCDILLTHPSISRFHLEIrSISSRQkLSVTDLSSVHGTWV-RDLRVEPHTCMEVEEGDTIRIG 779
Cdd:cd22665     24 VIGRDPSCSVVLPDKSVSKQHACI-EVDGGT-HLIEDLGSTNGTRIgNKVRLKPNVRYELIDGDLLLFG 90
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
709-791 3.35e-07

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438777 [Multi-domain]  Cd Length: 106  Bit Score: 50.70  E-value: 3.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  709 EILVVGRHpDCDILLTHPSISRFHLEIRSISSRQKLSVTDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGSTRIYRL- 787
Cdd:cd22725     21 EMIFVGRE-DCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYITLKLNDVIRFGYDSNMYVLe 99

                   ....*..
gi 1985651394  788 ---HWIP 791
Cdd:cd22725    100 rsqHKVP 106
FHA_Par42-like cd22675
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ...
714-787 3.89e-07

forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar proteins; TbPar42 is a nuclear protein that plays a key role in parasite cell proliferation. It exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Its PPIase domain adopts a parvulin fold and reflects structural elements of Pin1-type proteins but is catalytically inactive. Its FHA domain may be involved in the binding of phosphorylated target proteins. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438727 [Multi-domain]  Cd Length: 113  Bit Score: 51.02  E-value: 3.89e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985651394  714 GRHPDCDILLTHPSISRFHLEIRSISSRQKLSVTDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGSTRIYRL 787
Cdd:cd22675     34 GRSPVCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIEKGRPLPLPVGSVIQFGFSARKYKV 107
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
713-786 7.19e-07

forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438750 [Multi-domain]  Cd Length: 93  Bit Score: 49.33  E-value: 7.19e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985651394  713 VGRHPDCDILLTHPSISRFHLEIrsisSRQ--KLSVTDLSSVHGTWVRDLRVEPHtcmEVEEGDTIRIGgsTRIYR 786
Cdd:cd22698     25 IGRSSNNDIRLNDHSVSRHHARI----VRQgdKCNLTDLGSTNGTFLNGIRVGTH---ELKHGDRIQLG--ETIFR 91
FHA_OdhI-like cd22721
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate ...
708-779 7.67e-07

forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI) and similar proteins; OdhI is an essential component of the PknG signaling pathway. It regulates glutamate production under biotin non-limiting conditions. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438773 [Multi-domain]  Cd Length: 102  Bit Score: 49.70  E-value: 7.67e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985651394  708 EEILVVGRHPDCDILLTHPSISRFHLEIRSISSrqKLSVTDLSSVHGTWVRDlrvEPHTCMEVEEGDTIRIG 779
Cdd:cd22721     28 QPTTTAGRHPESDIFLDDVTVSRRHAEFRINEG--EFEVVDVGSLNGTYVNR---EPRNAQVMQTGDEIQIG 94
FHA_SNIP1 cd22718
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1) and ...
713-787 7.99e-07

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1) and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex, which associates with both the 3'end of the CCND1 gene and its mRNA. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438770  Cd Length: 149  Bit Score: 50.86  E-value: 7.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  713 VGRHPD-CDILLTHPSISRFH--LEIR---------SISSRQKLSVTDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGG 780
Cdd:cd22718     60 LGRDRKiADIPIDHPSCSKQHavLQYRlveytrpdgTKGRRVRPYIIDLESANGTFLNNKKIEPQRYYELKEKDVLKFGF 139

                   ....*..
gi 1985651394  781 STRIYRL 787
Cdd:cd22718    140 SSREYVL 146
IF3_C pfam00707
Translation initiation factor IF-3, C-terminal domain;
2275-2308 1.17e-06

Translation initiation factor IF-3, C-terminal domain;


Pssm-ID: 459911  Cd Length: 86  Bit Score: 48.50  E-value: 1.17e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1985651394 2275 EVKEIRFTPKIEAKDLKFKSDQALKLMESGYRVK 2308
Cdd:pfam00707    2 EVKEIKLRPKIDEHDYETKLKHARKFLEEGDKVK 35
FHA_Cep170A cd22724
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ...
709-785 1.34e-06

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438776 [Multi-domain]  Cd Length: 106  Bit Score: 49.20  E-value: 1.34e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985651394  709 EILVVGRHpDCDILLTHPSISRFHLEIRSISSRQKLSVTDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGSTRIY 785
Cdd:cd22724     21 EMIFVGRD-DCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIPEQTYITLKLDDKLRFGYDTNLF 96
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
2415-2625 2.22e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.23  E-value: 2.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2415 QAQPVQVQNTYAKREPGSEFSGGRDASRFEPRSPNQhvnPQRPRFQAPNQQPTgridPQSP------NQPPSAPRPQFPN 2488
Cdd:pfam03154  296 QPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQ---SQLQSQQPPREQPL----PPAPlsmphiKPPPTTPIPQLPN 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2489 QQ----PTGRFDP---QFPNQPPGPPRRQFPDQAPNQQPTGRFNPQFPNKSPSPPQSPFPDQAP--NQQPSGPSPNRhid 2559
Cdd:pfam03154  369 PQshkhPPHLSGPspfQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPvlTQSQSLPPPAA--- 445
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985651394 2560 rQGPPPRFQNQAPNQQP--TGRFEPQPPNPPRAPPRPQTRLPNDTPPTAPGRSGGPASSYGIFSTPKT 2625
Cdd:pfam03154  446 -SHPPTSGLHQVPSQSPfpQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSC 512
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
713-788 2.43e-06

forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438738 [Multi-domain]  Cd Length: 123  Bit Score: 48.82  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  713 VGRHPDC--DILLTHPSISRFHLEIRSISSRQKLSVTDLSSVHGTWVRDLRVEPHTC----MEVEEGDTIRIGGSTriYR 786
Cdd:cd22686     30 IGREKDHghTIRIPELGVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEksdpYPLTHGDELKIGETT--LL 107

                   ..
gi 1985651394  787 LH 788
Cdd:cd22686    108 FH 109
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
156-362 2.50e-06

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 51.06  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  156 VVIPGLTsDSSSAYLkHLAYNTAKTGWNVVISNHRGLG---GVSVTSDRFynAGWTEDIRVVLGYLQQKYPRAPLFAIGT 232
Cdd:pfam12146    8 VLVHGLG-EHSGRYA-HLADALAAQGFAVYAYDHRGHGrsdGKRGHVPSF--DDYVDDLDTFVDKIREEHPGLPLFLLGH 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  233 SIGANVLVKYLGEEGERtpLRGAVaICSPWdLLIGDRFICRTLKQKLY-------DKALTIGLQGYAQLHEPQFLRLanw 305
Cdd:pfam12146   84 SMGGLIAALYALRYPDK--VDGLI-LSAPA-LKIKPYLAPPILKLLAKllgklfpRLRVPNNLLPDSLSRDPEVVAA--- 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985651394  306 egikksrsirdFDNHAtcLVGKFETVDTYYRKSSSTQYV----GNVAVPLLCISALDDPLC 362
Cdd:pfam12146  157 -----------YAADP--LVHGGISARTLYELLDAGERLlrraAAITVPLLLLHGGADRVV 204
PHA03247 PHA03247
large tegument protein UL36; Provisional
2430-2618 3.04e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 3.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2430 PGSEFSGgRDASRFEPRSPNQHVNPQRPRFQAPNQQPTGRIDPQSPNQPPSAPRPQFPNQ---QPTGRFDPQFPNQPPGP 2506
Cdd:PHA03247  2858 PGGDVRR-RPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPpqpQPQPPPPPQPQPPPPPP 2936
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2507 PRRQFP-----DQAPNQQPTGRFNPQFPNKSPSPPQSPFPDQAPNQQPS--GPSPNRHIDRQGPPPRFQNQA-------- 2571
Cdd:PHA03247  2937 PRPQPPlapttDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSreAPASSTPPLTGHSLSRVSSWAsslalhee 3016
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985651394 2572 PNQQP-------------------------TGRFEPQPPNPPRAPPRPQTRLPNDTPPTAPGRSGGPASSYG 2618
Cdd:PHA03247  3017 TDPPPvslkqtlwppddtedsdadslfdsdSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFG 3088
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
2445-2516 4.58e-06

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 49.02  E-value: 4.58e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985651394  2445 PRSPNQHVNPQRPRFQAPNQQPtgridpqspnQPPSAPRPQFP-NQQPTGRFDPQFPNQPPGPPrrQFPDQAP 2516
Cdd:smart00818   81 SMTPTQHHQPNLPQPAQQPFQP----------QPLQPPQPQQPmQPQPPVHPIPPLPPQPPLPP--MFPMQPL 141
FHA_ZEP-like cd22702
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ...
705-779 7.66e-06

forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438754 [Multi-domain]  Cd Length: 123  Bit Score: 47.42  E-value: 7.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  705 DEVEEIlVVGRHPDCDIL-----LTHPSISRFHLEIrsISSRQKLSVTDLSSVHGTWVRD-----LRVEPHTCMEVEEGD 774
Cdd:cd22702     29 DEKQPC-IIGSDPHQAISgisvvIPSPQVSELHARI--TCKNGAFFLTDLGSEHGTWINDnegrrYRAPPNFPVRLHPSD 105

                   ....*
gi 1985651394  775 TIRIG 779
Cdd:cd22702    106 VIEFG 110
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
2445-2528 1.43e-05

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 47.86  E-value: 1.43e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  2445 PRSPNQH-VNPQRPRFQAPNQQPTGRIDPQSPNQPPsaprpqfPNQQPtgrFDPQFPNQPPG-PPRRQFPDQAPNQ-QPT 2521
Cdd:smart00818   59 PVLPAQQpVVPQQPLMPVPGQHSMTPTQHHQPNLPQ-------PAQQP---FQPQPLQPPQPqQPMQPQPPVHPIPpLPP 128

                    ....*..
gi 1985651394  2522 GRFNPQF 2528
Cdd:smart00818  129 QPPLPPM 135
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
2461-2576 1.64e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.39  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2461 APNQQPTGRIDPQSPNQPPSAPRPQFPNQQPTGRFDPQFPNQPPGPPRRQFPDQAPNQQPTGRFNPQfpnkspsppqspf 2540
Cdd:pfam09606  150 QPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAG------------- 216
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1985651394 2541 pDQAPNQQPsgpsPNrhidrQGPPPRFQNQAPNQQP 2576
Cdd:pfam09606  217 -AQMGQQAQ----AN-----GGMNPQQMGGAPNQVA 242
PHA03378 PHA03378
EBNA-3B; Provisional
2443-2572 1.82e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.45  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2443 FEPRSPNQhvNPQRPRFQAPnqqptGRIDPqspnqPPSAPRPQFPNQQPTGRFDP----QFPNQPP-GPPRRQFPDQA-- 2515
Cdd:PHA03378   674 YQPSPTGA--NTMLPIQWAP-----GTMQP-----PPRAPTPMRPPAAPPGRAQRpaaaTGRARPPaAAPGRARPPAAap 741
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985651394 2516 -----PNQQPTGRFNPQFPNKSPSPPQSPFPDQAPNQQPSGPSPNRHIDRQGPPPRFQNQAP 2572
Cdd:PHA03378   742 grarpPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAG 803
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
2379-2578 2.19e-05

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 49.04  E-value: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2379 KSARVKEEKSDSSEAGESTVDDHGDIEKCEPGFSVDQAQPVQVQNTYAKREPGSEFSGGRDASRFEP---RSPNQHVNPQ 2455
Cdd:pfam15279   89 RSESVSPGPSSSASPSSSPTSSNSSKPLISVASSSKLLAPKPHEPPSLPPPPLPPKKGRRHRPGLHPplgRPPGSPPMSM 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2456 RPRFQAPNQQPTGRIDPQSPNQPPSAPRPQfPNQQPTGRFDPQF--PNQ-------PPGPPRRQFPDQAPNQQPTgrFNP 2526
Cdd:pfam15279  169 TPRGLLGKPQQHPPPSPLPAFMEPSSMPPP-FLRPPPSIPQPNSplSNPmlpgigpPPKPPRNLGPPSNPMHRPP--FSP 245
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1985651394 2527 QFPNKSPSPPQspfpdqaPNQQPSGPSPNRHIDRQGPPPRFQNQAPNQQPTG 2578
Cdd:pfam15279  246 HHPPPPPTPPG-------PPPGLPPPPPRGFTPPFGPPFPPVNMMPNPPEMN 290
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
713-774 2.35e-05

second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.


Pssm-ID: 439356 [Multi-domain]  Cd Length: 93  Bit Score: 45.18  E-value: 2.35e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985651394  713 VGRHPDCDILLTHPSISRFHLEIRSISSrqKLSVTDLSSVHGTWVRDLRVEP---HTCMEVEEGD 774
Cdd:cd22737     25 IGRASDNDIVIPEGSVSRHHATLVPTPG--GTQIRDLRSTNGTFVNGLRVDAallHDGDVVTIGD 87
FHA_GarA-like cd22720
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ...
714-779 2.65e-05

forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation regulator GarA and similar proteins; GarA is an FHA domain-containing protein involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent ON/OFF molecular switch that modulates the activities of KGD, GDH and GltB. Its FHA domain has dual specificity. It binds to both phosphorylated upstream partners, such as the kinases PknB and PknG, and nonphosphorylated downstream partners, such as the 2-oxoglutarate decarboxylase KGD. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438772 [Multi-domain]  Cd Length: 100  Bit Score: 45.38  E-value: 2.65e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985651394  714 GRHPDCDILLTHPSISRFHLEIRsiSSRQKLSVTDLSSVHGTWVRDlrvEPHTCMEVEEGDTIRIG 779
Cdd:cd22720     29 GRHPDSDIFLDDVTVSRRHAEFR--LENNEFNVVDVGSLNGTYVNR---EPVDSAVLANGDEVQIG 89
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
2458-2577 2.97e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 49.65  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2458 RFQAPN----QQPTGRIDPQSPNQPPSAPRPQFPNQQPTGRFDPQFPNQPPGPPRRQFPD---QAPNQQPTGRFNPQfpn 2530
Cdd:pfam09770  204 RAQAKKpaqqPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilQRPQSPQPDPAQPS--- 280
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1985651394 2531 kspSPPQSPFPDQAPNQQPSGPS-----PNRHIDRQGPPPRFQNQAPNQQPT 2577
Cdd:pfam09770  281 ---IQPQAQQFHQQPPPVPVQPTqilqnPNRLSAARVGYPQNPQPGVQPAPA 329
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
696-781 4.81e-05

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438745 [Multi-domain]  Cd Length: 91  Bit Score: 44.22  E-value: 4.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  696 IGSTVSDDddevEEILVVGRHPDCDILLTHPSISRFHLEIRSISSrqKLSVTDLSSVHGTWVRDLRV-EPHTcmeVEEGD 774
Cdd:cd22693      9 QGQTFPID----KSGITIGRADDNDLVLSDDFVSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRVtQPVV---VQPGD 79

                   ....*..
gi 1985651394  775 TIRIGGS 781
Cdd:cd22693     80 TIRIGAT 86
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
2444-2584 5.70e-05

Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 and P30 proteins. P30 has been found to be membrane associated and localized on the tip organelle. It is thought that it is important in cytadherence and virulence. The N-terminus contains two predicted transmembrane helices followed by a long region of a short 6 residue proline rich repeat.


Pssm-ID: 429374 [Multi-domain]  Cd Length: 275  Bit Score: 47.65  E-value: 5.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2444 EPRSPNQHVNPQRPRFQAPNQQPTGRIDPQSPNQPPSAP-------RPQFPNQQPtgRFDPQFpnQPPGPPRRQFPDQaP 2516
Cdd:pfam07271  101 EEKERQEQMAEQLQRISEQQETQAIEPTEQQNTAEPTQPagvnvanQPQMGINQP--QINPQF--GPNPQQRIGFPMQ-P 175
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985651394 2517 NQQPTGRFNPQfpnkspsppqspfPDQAPNQQPSGPSPNRHIDrqgPPPRFQNQAPNQQPtgrfepQP 2584
Cdd:pfam07271  176 NMGMRPGFNQM-------------PGMPPNQMRPGFNQMPGMP---PRPGFPNPMPNMQP------RP 221
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
708-786 7.72e-05

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438720 [Multi-domain]  Cd Length: 91  Bit Score: 43.61  E-value: 7.72e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985651394  708 EEILVVGRHPDCDILLTHPSISRFHLEIRSISsrQKLSVTDLSSVHGTWVRDLRVEPHtcMEVEEGDTIRIGGSTRIYR 786
Cdd:cd22668     17 EGSNIIGRGSDADFRLPDTGVSRRHAEIRWDG--QVAHLTDLGSTNGTTVNNAPVTPE--WRLADGDVITLGHSEIIVR 91
PRK05733 PRK05733
single-stranded DNA-binding protein; Provisional
2436-2497 7.86e-05

single-stranded DNA-binding protein; Provisional


Pssm-ID: 235585 [Multi-domain]  Cd Length: 172  Bit Score: 45.69  E-value: 7.86e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985651394 2436 GGRdasrfePRSPNQHVNPQRPRFQAPNQQPTGRidPQSPNQPPSAPRPQFPNQQPTGRFDP 2497
Cdd:PRK05733   112 GGR------PQGDDQGGQGGGNYNQSAPRQQAQR--PQQAAQQQSRPAPQQPAPQPAADFDS 165
dnaA PRK14086
chromosomal replication initiator protein DnaA;
2430-2572 8.36e-05

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 47.90  E-value: 8.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2430 PGSEFSGGRDASRFEPRSPNQHVNPQRP--RFQAPNQQPTGRidpqsPNQPPSAPRPQFPNQQPTGrfdpQFPNQPPGPP 2507
Cdd:PRK14086   113 PGRRPYEGYGGPRADDRPPGLPRQDQLPtaRPAYPAYQQRPE-----PGAWPRAADDYGWQQQRLG----FPPRAPYASP 183
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985651394 2508 RRQFPDQAPNQQPTGRFNPQFPNKSPSPPQSPFPDQAPNQQPS---GPSPNR-HIDRQGPPPRFQNQAP 2572
Cdd:PRK14086   184 ASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTdrpEPPPGAgHVHRGGPGPPERDDAP 252
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
2339-2580 9.10e-05

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 47.75  E-value: 9.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2339 DALVEFGPEADRKsAVVIVRHAKFGPPKKGGVKKLKDIDIKSARVKEEKSDSSEAGESTVDDHGdiEKCEPGFSVDQAQP 2418
Cdd:COG5180    190 DALKDSPEKLDRP-KVEVKDEAQEEPPDLTGGADHPRPEAASSPKVDPPSTSEARSRPATVDAQ--PEMRPPADAKERRR 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2419 VQVQNTYAKREPGSEFSGGR-----DASRFEPRSPNQH-------------------VNPQRPRFQAPNQQPTGRIDPQS 2474
Cdd:COG5180    267 AAIGDTPAAEPPGLPVLEAGsepqsDAPEAETARPIDVkgvasappatrpvrppggaRDPGTPRPGQPTERPAGVPEAAS 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2475 P-NQPPSAPRPQFPnqqptgrfdpqfpnQPPGPPRRQF-PDQAPNQQPTGRFNPQFpnkspsppqspfpdQAPNQQPSGP 2552
Cdd:COG5180    347 DaGQPPSAYPPAEE--------------AVPGKPLEQGaPRPGSSGGDGAPFQPPN--------------GAPQPGLGRR 398
                          250       260
                   ....*....|....*....|....*...
gi 1985651394 2553 SPNRHIDRQGPPPRFQNQAPNQQPTGRF 2580
Cdd:COG5180    399 GAPGPPMGAGDLVQAALDGGGRETASLG 426
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
711-788 1.00e-04

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 47.45  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  711 LVVGRHPDCDILLTHPS--ISRFHLEIRSISSRqkLSVTDLSSvHGTWV--RDLRVEPHTCMEVEEGDTIRIGGstriYR 786
Cdd:COG3456     28 GTIGRSADCDWVLPDPDrsVSRRHAEIRFRDGA--FCLTDLST-NGTFLngSDHPLGPGRPVRLRDGDRLRIGD----YE 100

                   ..
gi 1985651394  787 LH 788
Cdd:COG3456    101 IR 102
PHA03378 PHA03378
EBNA-3B; Provisional
2415-2572 1.25e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 47.75  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2415 QAQPVQVQNTYAKREPGSEFSGGRDASRFEPRSPNQHVNPQRP--RFQAPNQQPTGRIDPQ------SPNQPPSAPrpQF 2486
Cdd:PHA03378   708 AAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAApgRARPPAAAPGRARPPAaapgapTPQPPPQAP--PA 785
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2487 PNQQPTGRFDPQFPNQPPGPPRRQFPDQAPNQQ-PTGRFNPQFPNKSPSPPQSPFPDQA--PNQQPSGPSPnrhiDRQGP 2563
Cdd:PHA03378   786 PQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQgPTKQILRQLLTGGVKRGRPSLKKPAalERQAAAGPTP----SPGSG 861

                   ....*....
gi 1985651394 2564 PPRFQNQAP 2572
Cdd:PHA03378   862 TSDKIVQAP 870
PHA03378 PHA03378
EBNA-3B; Provisional
2445-2578 1.53e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 47.37  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2445 PRSPNQHVNP-------QRPRfQAPNQQPTGRIDPQSPNQPPSAPRPQFPNQQPTGRFDP--------QFPNQPPGPPRR 2509
Cdd:PHA03378   698 PRAPTPMRPPaappgraQRPA-AATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPpaaapgraRPPAAAPGAPTP 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2510 QFPDQA---PNQQPTGRFNPQFPNKSPSPPQSPFPDQAPNQQpsgpSPNRHIDRQG---------PPPRFQNQAPNQQPT 2577
Cdd:PHA03378   777 QPPPQAppaPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQ----GPTKQILRQLltggvkrgrPSLKKPAALERQAAA 852

                   .
gi 1985651394 2578 G 2578
Cdd:PHA03378   853 G 853
PHA03247 PHA03247
large tegument protein UL36; Provisional
2441-2579 1.90e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2441 SRFEPRSPNQHVNPQRPRFQAPNQQPTGRIdPQSPNQPPSAPRPqfPNQQPTgrfDPQFPNqPPGPPRRQFPDQAPNQQP 2520
Cdd:PHA03247  2571 PRPAPRPSEPAVTSRARRPDAPPQSARPRA-PVDDRGDPRGPAP--PSPLPP---DTHAPD-PPPPSPSPAANEPDPHPP 2643
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985651394 2521 TGRFNPqfpnkspsppqspfpdQAPNQQPSGP--SPNRHIDRQGPPPrfQNQAPNQQPTGR 2579
Cdd:PHA03247  2644 PTVPPP----------------ERPRDDPAPGrvSRPRRARRLGRAA--QASSPPQRPRRR 2686
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
711-785 2.17e-04

forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438730 [Multi-domain]  Cd Length: 102  Bit Score: 42.73  E-value: 2.17e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985651394  711 LVVGRHPDCDILLTHPSISRFHLEIRSISSRQKLSVTDLSSVHGTWV--RDLRVEpHTCMEVEEGDTIRIGGSTRIY 785
Cdd:cd22678     25 LTIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVngESISPN-GRPVVLSSGDVITLGSETKIL 100
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
2374-2575 3.87e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.91  E-value: 3.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2374 KDID---------IKSARVKEEKSDSSeAGESTVDDHGDIEKCEPGFSVDQAQPVQVQNTYAKREP----GSEFSGGRDA 2440
Cdd:pfam03154  135 KDIDqdnrstspsIPSPQDNESDSDSS-AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPtpsaPSVPPQGSPA 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2441 SRFEPRSPNQHVNPQRPRFQAPNQQPTGRIDPQSPNQP--PSAPRPQFPNQQ-PTGRFDPQFPNQP------------PG 2505
Cdd:pfam03154  214 TSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPmtQPPPPSQVSPQPlPQPSLHGQMPPMPhslqtgpshmqhPV 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2506 PPRrQFPDQAPNQQPTGRFNPQFPNKSPSPP--------QSPFPDQAPNQQPSGPSPNR--HIDrqgPPPRFQ-NQAPNQ 2574
Cdd:pfam03154  294 PPQ-PFPLTPQSSQSQVPPGPSPAAPGQSQQrihtppsqSQLQSQQPPREQPLPPAPLSmpHIK---PPPTTPiPQLPNP 369

                   .
gi 1985651394 2575 Q 2575
Cdd:pfam03154  370 Q 370
PHA03379 PHA03379
EBNA-3A; Provisional
2430-2576 4.07e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 45.82  E-value: 4.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2430 PGSEFSGGRDASRfEPRSPNQhvnpQRPRFQAPNQQPTGRIDPQSPNQPPSAPRPQFPNQQPTgRFDPQFpNQP--PGPP 2507
Cdd:PHA03379   634 PGSPFSQVADVMR-AGGVPAM----QPQYFDLPLQQPISQGAPLAPLRASMGPVPPVPATQPQ-YFDIPL-TEPinQGAS 706
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985651394 2508 RRQFPDQAPNQQPtgRFNPQFPNKSPSPPQSPFPDQAPNQQPSGPSpNRHIDRQGPPPRFQNQAPNQQP 2576
Cdd:PHA03379   707 AAHFLPQQPMEGP--LVPERWMFQGATLSQSVRPGVAQSQYFDLPL-TQPINHGAPAAHFLHQPPMEGP 772
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
712-788 4.35e-04

forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.


Pssm-ID: 438734 [Multi-domain]  Cd Length: 96  Bit Score: 41.74  E-value: 4.35e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985651394  712 VVGRHPDCDILLTHPSISRFH--LEIrsisSRQKLSVTDLSSVHGTWVRDLRVEPHTCMEVEEGDTIRIGGStrIYRLH 788
Cdd:cd22682     23 VIGRSVESQVQIDDDSVSRYHakLAV----NPSAVSIIDLGSTNGTIVNGKKIPKLASCDLQNGDQIKIGNT--IFKFH 95
FHA_DDL-like cd22719
forkhead associated (FHA) domain found in Arabidopsis thaliana FHA domain-containing protein ...
703-787 6.02e-04

forkhead associated (FHA) domain found in Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins; DDL, also called protein DAWDLE, is involved in microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438771 [Multi-domain]  Cd Length: 130  Bit Score: 42.09  E-value: 6.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  703 DDDEVEEILVVGRHpDC----------DILLTHPSISRFHLEIR-----------SISSRQKLSVTDLSSVHGTWVRDLR 761
Cdd:cd22719     23 DGEPLNEPLHIHRQ-SCylfgrerkvaDIPTDHPSCSKQHAVIQyrltekeggdgMMGKAVRPYIMDLGSTNGTFLNGER 101
                           90       100
                   ....*....|....*....|....*.
gi 1985651394  762 VEPHTCMEVEEGDTIRIGGSTRIYRL 787
Cdd:cd22719    102 IEPQRYYELLEKDTIKFGNSSREYVL 127
YppG pfam14179
YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which ...
2462-2525 6.75e-04

YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 115 and 181 amino acids in length. There are two completely conserved residues (F and G) that may be functionally important.


Pssm-ID: 372950 [Multi-domain]  Cd Length: 101  Bit Score: 41.33  E-value: 6.75e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985651394 2462 PNQQPTGRIdPQSPNQPPSAPR-PQFPNQQptgrfdpQFPnQPPGPPRRQFPDQAPNQQPTGRFN 2525
Cdd:pfam14179    3 HNSQPYPYF-SQQVYQQPVQPQyPPFAPQQ-------YMP-QPPMPYMNPYPKQQPQQQQPSQFQ 58
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
2410-2563 7.59e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2410 GFSVDQAQPVQVQNTYAKREPGSEFSGGRDASRFEPRSPNQHVNPQRPRfQAPNQQPTGRIDPQSPNQPPSAPRPQFPNQ 2489
Cdd:PRK07764   386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPA-PAPAPAPPSPAGNAPAGGAPSPPPAAAPSA 464
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985651394 2490 QPTGRfdPQFPNQPPGPPRRQFPDQAPNQQPTgrfnpqfpnkspsppqspfpdQAPNQ--QPSGPSPNRHIDRQGP 2563
Cdd:PRK07764   465 QPAPA--PAAAPEPTAAPAPAPPAAPAPAAAP---------------------AAPAApaAPAGADDAATLRERWP 517
FHA_PML1-like cd22681
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ...
703-776 8.01e-04

forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438733 [Multi-domain]  Cd Length: 129  Bit Score: 41.66  E-value: 8.01e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985651394  703 DDDEVEEILVvgrhpdCDILLTHPSISRFH--LEIRSISSRQKLSVTDLSSVHGTWVRDLRVEPHTCMEVEEGDTI 776
Cdd:cd22681     47 EKGESTEIVV------ADIGIPEETCSKQHcvIQFRNVKGILKPYIMDLDSSNGTCLNDNVIPSSRYVELRSGDVI 116
DUF1720 pfam08226
Domain of unknown function (DUF1720); This domain is found in different combinations with ...
2454-2522 8.24e-04

Domain of unknown function (DUF1720); This domain is found in different combinations with cortical patch components EF hand, SH3 and ENTH and is therefore likely to be involved in cytoskeletal processes. This family contains many hypothetical proteins.


Pssm-ID: 369766 [Multi-domain]  Cd Length: 75  Bit Score: 40.12  E-value: 8.24e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985651394 2454 PQRPRFQAPNQQPTGRIDPQSPNQP----PSAPRPQFPNQQPTGrfDPQFPNQPPGPPRRQFPDQAPNQ-QPTG 2522
Cdd:pfam08226    3 PQQTGYMPPQQQQPQQTQQPLQPQPtgfmPQQQTGQGLQPQPTG--MGQFQPLQPQQTGFQPQAQQGLQpQATG 74
FHA_Ct664-like cd22696
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ...
712-781 8.69e-04

forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Chlamydia trachomatis Ct664 protein. Ct664 situates within the type III secretion system cluster that also encodes an STPK (CT673 in C. trachomatis), suggesting a role of CT664 in the chlamydial type III secretion system by mediating phosphorylation-dependent protein-protein interactions. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438748 [Multi-domain]  Cd Length: 97  Bit Score: 40.94  E-value: 8.69e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985651394  712 VVGRHPD-CDILLTHPSISRFHLEIrSISSRQKLSVTDLSSVHGTWVRDLRVEPHTcmEVEEGDTIRIGGS 781
Cdd:cd22696     24 FIGKDPTvCDIVLQDPSISRQHARL-SIDQDNRVFIEDLSSKNGVLVNGKPIEGKE--EISGSDVISLGTT 91
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
713-787 1.00e-03

forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438752 [Multi-domain]  Cd Length: 96  Bit Score: 40.70  E-value: 1.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985651394  713 VGRHpDCDILLTHPSISRFHLEIRSISSRQKLSVTDLSSVHGTWVRDLRVEpHTCMEVEEGDTIRIGGSTRIYRL 787
Cdd:cd22700     20 IGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQ-NAAVRLAPGDVLRFGFGGLPYEL 92
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
2444-2576 1.08e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.08  E-value: 1.08e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394  2444 EPRSPNQHVNPQRPRFQAPNQQPtgrIDPQSPNQPPSAPRPQFPNQQptgrFDPQFPNQPPGPPRRQFPDQAPNQQPTgr 2523
Cdd:smart00818   44 QQHPPTHTLQPHHHIPVLPAQQP---VVPQQPLMPVPGQHSMTPTQH----HQPNLPQPAQQPFQPQPLQPPQPQQPM-- 114
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1985651394  2524 fNPQfpnkspsppqspfPDQAPnQQPSGPSPNrhidrqgPPPRFQNQAPNQQP 2576
Cdd:smart00818  115 -QPQ-------------PPVHP-IPPLPPQPP-------LPPMFPMQPLPPLL 145
PRR20 pfam15708
Proline-rich protein family 20; This family of proteins is found in eukaryotes. Proteins in ...
2444-2523 1.27e-03

Proline-rich protein family 20; This family of proteins is found in eukaryotes. Proteins in this family are typically between 73 and 221 amino acids in length. There is a conserved AYV sequence motif.


Pssm-ID: 406199 [Multi-domain]  Cd Length: 221  Bit Score: 42.70  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2444 EPRSPnqhvnpQRPRFQAPNQQPTGriDPQSPNQPPSAPRPQFPNQQPTGRFDPQFPNQPPGPPRRQFPDQAPNQQPTGR 2523
Cdd:pfam15708    3 EPRPS------KRPRAVAPNQASGG--PPREPGCSGVDPEDPGEADGPVEPGQPAKPIAYVNPMRCEPPAHAEPAEPAQR 74
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
2447-2576 1.33e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 44.23  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2447 SPNQHVNPQRPRFQAPNQQPTGRIDPQSPNQP----------PSAPRPQFPNQQPTGRFDPQF--PNQPPGPPRRQFPDQ 2514
Cdd:pfam09606  299 SIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMnqsvgqggqvVALGGLNHLETWNPGNFGGLGanPMQRGQPGMMSSPSP 378
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2515 APNQQPTGRFNPQFPNkspsppqspfpdqaPNQQPSGPSP--------NRHIDRQGPPPRFQnQAPNQQP 2576
Cdd:pfam09606  379 VPGQQVRQVTPNQFMR--------------QSPQPSVPSPqgpgsqppQSHPGGMIPSPALI-PSPSPQM 433
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
2346-2579 1.48e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 43.90  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2346 PEADRKSAVVIVRHAKFGPPKKGGVKKLKDIDikSARVKEEKSDSSeagestvddhGDIEKcePGFSVDQAQPVQVQNTY 2425
Cdd:COG5180    188 PRDALKDSPEKLDRPKVEVKDEAQEEPPDLTG--GADHPRPEAASS----------PKVDP--PSTSEARSRPATVDAQP 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2426 AKREPGSEFSGGR--DASRFEPRSPNQHV--NPQRPRFQAPNQQPTGRIDPQSPNQPPSAPRPQFPNQqptGRFDP--QF 2499
Cdd:COG5180    254 EMRPPADAKERRRaaIGDTPAAEPPGLPVleAGSEPQSDAPEAETARPIDVKGVASAPPATRPVRPPG---GARDPgtPR 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2500 PNQPPGPPRRQFPDQAPNQQPTGRFNPQfpnkspsppqsPFPDQAPNQQPSGPSPNRHIDrQGPPPRFQNQAPNQQPTGR 2579
Cdd:COG5180    331 PGQPTERPAGVPEAASDAGQPPSAYPPA-----------EEAVPGKPLEQGAPRPGSSGG-DGAPFQPPNGAPQPGLGRR 398
PHA03247 PHA03247
large tegument protein UL36; Provisional
2409-2615 1.50e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2409 PGFSVDQAQPVQVQNTYAKREPGSEFSGGRDASRfEPRSPNQHVNPQRPRFQAPNQQPTgridPQSPNQPPSAPRPQFPn 2488
Cdd:PHA03247  2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLP-SPWDPADPPAAVLAPAAALPPAAS----PAGPLPPPTSAQPTAP- 2839
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2489 QQPTGRFDPQFPNQ----PPGPPRRQFPDQAPNQQPTGRFNPQFPNKSPSPPQSPFPDQA--PNQQPSGPSPNrhidrqg 2562
Cdd:PHA03247  2840 PPPPGPPPPSLPLGgsvaPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAlpPDQPERPPQPQ------- 2912
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1985651394 2563 PPPRFQNQAPNQQPTgrfEPQPPNPPRapprpqtrlPNDTPPTAPGRSGGPAS 2615
Cdd:PHA03247  2913 APPPPQPQPQPPPPP---QPQPPPPPP---------PRPQPPLAPTTDPAGAG 2953
PHA03378 PHA03378
EBNA-3B; Provisional
2460-2623 1.81e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.90  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2460 QAPNQQPTGRIDPQSPNQPPSAPRPQFPNQQPTG-RFDPQFPNQ----PPGPPRRQFPDQAPNQQPTgRFNPQFPNKSPS 2534
Cdd:PHA03378   594 QTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPlRPIPMRPLRmqpiTFNVLVFPTPHQPPQVEIT-PYKPTWTQIGHI 672
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2535 PPqspfpdqapNQQPSGPSPNRHID----RQGPPPRFQNQA-PNQQPTGRFEPQPPNPPRAPPRPQTRLPNDTPPTAPGR 2609
Cdd:PHA03378   673 PY---------QPSPTGANTMLPIQwapgTMQPPPRAPTPMrPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGR 743
                          170
                   ....*....|....
gi 1985651394 2610 SGGPASSYGIFSTP 2623
Cdd:PHA03378   744 ARPPAAAPGRARPP 757
PRK10263 PRK10263
DNA translocase FtsK; Provisional
2409-2567 2.49e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2409 PGFSVDQAQPVQVQNTYakrePGSEFSGGRDASRFEPRSPNQHVNPQRPRFQAPNQQPTGRIDP-------QSPNQPPSA 2481
Cdd:PRK10263   347 ASVDVPPAQPTVAWQPV----PGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPyyapaaeQPAQQPYYA 422
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2482 PRPQFPNQQPTgrFDPQfPNQPPGPPRRQFPDQAPNQQPTGRFNPQFPNKSPSPPQSPFPDQAPNQQPSGPSPNRHIDRQ 2561
Cdd:PRK10263   423 PAPEQPAQQPY--YAPA-PEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEET 499

                   ....*...
gi 1985651394 2562 GP--PPRF 2567
Cdd:PRK10263   500 KParPPLY 507
PRK10263 PRK10263
DNA translocase FtsK; Provisional
2367-2617 7.07e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 7.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2367 KGGVKKLKDIDIKSARVKEEKSDSSEAGESTVDDHGDIEKCEPGFSVDqaqPVQVQntyakrepgseFSGGR----DASR 2442
Cdd:PRK10263   241 RGALARRKRLAEKFINPMGRQTDAALFSGKRMDDDEEITYTARGVAAD---PDDVL-----------FSGNRatqpEYDE 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2443 FEPRSPNQHVNPQRPRFQAPNQQPTGRIDPQSPNQP-PSAPRPQFPNQQPTGRFDPQfpnqpPGPprrQFPDQAPNQQPT 2521
Cdd:PRK10263   307 YDPLLNGAPITEPVAVAAAATTATQSWAAPVEPVTQtPPVASVDVPPAQPTVAWQPV-----PGP---QTGEPVIAPAPE 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2522 GrFNPQfpnksPSPPQSPFPDQAPNQQPSGPSPNRHIDRQGPPPRFQNQAPNQQPTGRFEPQPPNPPRAPPRPQTRLPND 2601
Cdd:PRK10263   379 G-YPQQ-----SQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQ 452
                          250
                   ....*....|....*.
gi 1985651394 2602 TPPTAPGRSGGPASSY 2617
Cdd:PRK10263   453 QSTFAPQSTYQTEQTY 468
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
2386-2576 7.60e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 7.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2386 EKSDSSEAGESTVDDHGDIEKCEPGFSVDQAQPvqvqntyAKREPGSEFSGGRDASRFEP---RSPNQHVNPQRPRFQAP 2462
Cdd:pfam03154  119 ESSDGRSVNDEGSSDPKDIDQDNRSTSPSIPSP-------QDNESDSDSSAQQQILQTQPpvlQAQSGAASPPSPPPPGT 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2463 NQQPTGRIDPQSPNQPP--SAPRPQFPNQ-----------QPTGRFDPQ-FPNqpPGPPRRQFPDQAPNQQPTGRFNPQF 2528
Cdd:pfam03154  192 TQAATAGPTPSAPSVPPqgSPATSQPPNQtqstaaphtliQQTPTLHPQrLPS--PHPPLQPMTQPPPPSQVSPQPLPQP 269
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2529 PNKSPSPPQSPFPDQAPN--QQPSGPSP----NRHIDRQGPP----------------PRFQNQAPNQQP 2576
Cdd:pfam03154  270 SLHGQMPPMPHSLQTGPShmQHPVPPQPfpltPQSSQSQVPPgpspaapgqsqqrihtPPSQSQLQSQQP 339
PHA03418 PHA03418
hypothetical E4 protein; Provisional
2454-2527 7.68e-03

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 40.49  E-value: 7.68e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985651394 2454 PQRPRFQAPNQQPTGRIDPQSPNQPPSAPRPQfpnQQPTGRFDPQFPNQPPGPPRRQfPDQAPnQQPTGRFNPQ 2527
Cdd:PHA03418    34 PLLPAPHHPNPQEDPDKNPSPPPDPPLTPRPP---AQPNGHNKPPVTKQPGGEGTEE-DHQAP-LAADADDDPR 102
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
2414-2499 8.22e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.60  E-value: 8.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2414 DQAQPVQVQNTYAKREPGSEFSGGRDASRFEPRSPNQHVNPQRPRFQAPNQQPTGRIDPQSPNQPPSAPRPQFPnQQPtg 2493
Cdd:PTZ00449   590 DPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSP-KPP-- 666

                   ....*.
gi 1985651394 2494 rFDPQF 2499
Cdd:PTZ00449   667 -FDPKF 671
PHA03379 PHA03379
EBNA-3A; Provisional
2445-2574 9.42e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.58  E-value: 9.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985651394 2445 PRSPNQHVNPQRPRF--QAPNQQPTgridpQSPNQPPSAPRPQFPNQQ------------PTGRFDPQFP-NQPPGPPRR 2509
Cdd:PHA03379   416 PRPPVEKPRPEVPQSleTATSHGSA-----QVPEPPPVHDLEPGPLHDqhsmapcpvaqlPPGPLQDLEPgDQLPGVVQD 490
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985651394 2510 QFPDQAPNQQPTGRFNPQFPNKSPSPPQSPFPDQAPNQQPSGPSPNRHIDRQGP----PPRFQNQAPNQ 2574
Cdd:PHA03379   491 GRPACAPVPAPAGPIVRPWEASLSQVPGVAFAPVMPQPMPVEPVPVPTVALERPvcpaPPLIAMQGPGE 559
FHA_EmbR-like cd22669
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ...
708-779 9.95e-03

forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438721 [Multi-domain]  Cd Length: 89  Bit Score: 37.78  E-value: 9.95e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985651394  708 EEILVVGRHPDCDILLTHPSISRFHLEIRSISSrqKLSVTDLSSVHGTWVRDLRVEPhtCMEVEEGDTIRIG 779
Cdd:cd22669     15 AAATRIGRLHDNDIVLDSANVSRHHAVIVDTGT--NYVINDLRSSNGVHVQHERIRS--AVTLNDGDHIRIC 82
 
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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