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Conserved domains on  [gi|6321552|ref|NP_011631|]
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chromatin-remodeling histone chaperone SPT6 [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SH2_2 pfam14633
SH2 domain;
1232-1436 1.25e-85

SH2 domain;


:

Pssm-ID: 464227 [Multi-domain]  Cd Length: 206  Bit Score: 277.88  E-value: 1.25e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552    1232 EDAEEERKLMMAEARAKRTHRVINHPYYFPFNGRQAEDYLRSKERGEFVIRQSSRGDDHLVITWKLDKDLFQHIDIQELE 1311
Cdd:pfam14633    2 ADKEELKKKKKAKARKTYVKRVIKHPLFHNFNYAQAEEYLASQDRGDVVIRPSSKGPDHLTVTWKVADGVYQHIDVLELD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552    1312 KENPLALGKVLIVDNQKYNDLDQIIVEYLQNKVRLLNEMTSSEKFKSGTKKDVVKFIEDYSRVNPNKSVYYFSLNHDNPG 1391
Cdd:pfam14633   82 KENEFSLGKTLRIGGEEYEDLDELIARHVQPMARKVEEMMNHRKFKDGTKEEVEEWLREEKKANPKRSPYAFCLSHKHPG 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 6321552    1392 WFYLMFKINANSKLYTWNVKLTNTGYFLVNYNYPSVIQLCNGFKT 1436
Cdd:pfam14633  162 YFLLSFKANKNSRVHHWYVKVTPDGFRLRGQQFPDVDALCNGFKK 206
YqgF pfam14639
Holliday-junction resolvase-like of SPT6; The YqgF domain of SPT6 proteins is homologous to ...
 744-895 5.29e-78

Holliday-junction resolvase-like of SPT6; The YqgF domain of SPT6 proteins is homologous to the E.coli RuvC but its putative catalytic site lacks the carboxylate side chains critical for coordinating magnesium ions that mediate phosphodiester bond-cleavage


:

Pssm-ID: 258777  Cd Length: 150  Bit Score: 254.02  E-value: 5.29e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     744 DPKIPKILSLTCGQGRFgADAIIAVYVNRKGDFIRDYKIVDNPFDKTNPEKFEDTLDNIIQSCQPNAIGINGPNPKTQKF 823
Cdd:pfam14639    1 QGKIPRVLGVAFGSGRF-DDAIICVLVNGEGEVTDFLKLAWREFDRENKAQFEETLKKFLLSKKPHVIGVSGENRDAQKF 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321552     824 YKRLQEVLHKKQiVDSRGHTIPIIYVEDEVAIRYQNSERAAQEFPNKPPLVKYCIALARYMHSPLLEYANLT 895
Cdd:pfam14639   80 YEDVQRVLHELE-QDSRLHTIGVILVDDEVAILYQNSKRAEAEFPDYPPLLRYCVALARYIQDPLLEYAQVC 150
HHH_7 pfam14635
Helix-hairpin-helix motif;
897-1000 8.32e-55

Helix-hairpin-helix motif;


:

Pssm-ID: 291309  Cd Length: 104  Bit Score: 185.83  E-value: 8.32e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     897 EEVRSLSIHPHQNLLSSEQLSWALETAFVDIVNLVSVEVNKATDNNYYASALKYISGFGKRKAIDFLQSLQRLNEPLLAR 976
Cdd:pfam14635    1 EDILSLSFHPLQELLPKEELLKALETAFVDIVNLVGVDVNEAIANKYEAAILPYIAGLGPRKADHLLKILAANNGRLDNR 80

                           90       100
                   ....*....|....*....|....
gi 6321552     977 QQLITHNILHKTIFMNSAGFLYIS 1000
Cdd:pfam14635   81 SQLITKCIMGPKVFMNCAGFLIID 104
HTH_44 pfam14641
Helix-turn-helix DNA-binding domain of SPT6; This helix-turn-helix represents the first of two ...
 336-445 9.74e-50

Helix-turn-helix DNA-binding domain of SPT6; This helix-turn-helix represents the first of two DNA-binding domains on the SPT6 proteins.


:

Pssm-ID: 464230  Cd Length: 115  Bit Score: 171.59  E-value: 9.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     336 YGNMSSEDQELERNWIAEKISVDKNFDANYDLTEFKEAIGNAIKFITKENLEVPFIYAYRRNYISSREKDGF-----LLT 410
Cdd:pfam14641    1 YIDLTDEELEEEANWISNRLLVEKNDDFERLLEPFKEAVGNVLEFISKDNLEVPFIWQHRRDYLLHSEKDGFeighkLLN 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 6321552     411 EDDLWDIVSLDIEFHSLVNKKDYVQRFYAELHIDD 445
Cdd:pfam14641   81 EDDLWRIVQLDIKFHSLIEKRNNLEKLYEKLGIDD 115
SPT6_acidic pfam14632
Acidic N-terminal SPT6; The N-terminus of SPT6 is highly acidic. The full SPT6 protein is a ...
 28-128 2.17e-15

Acidic N-terminal SPT6; The N-terminus of SPT6 is highly acidic. The full SPT6 protein is a transcription regulator, but the exact function of this acidic region is not certain.


:

Pssm-ID: 464226  Cd Length: 89  Bit Score: 72.89  E-value: 2.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552      28 SEEEEGEDvfdsseededideDEDEARKVQEGFIVNDDDENEDPGTSISKKRRKH---KRREREEDDRLSEDDLDLLMEN 104
Cdd:pfam14632    2 SSEEEDDD-------------DEEEARKVREGFIVDDDEEEEEEEEDDEERRRRKkkrKRREEEEDDRLDEDDLDLIEEN 68

                           90       100
                   ....*....|....*....|....
gi 6321552     105 AGVERTKASSssgKFKRLKRVGDE 128
Cdd:pfam14632   69 TGVKRRRSSS---KFKRLKRGHDD 89
 
Name Accession Description Interval E-value
SH2_2 pfam14633
SH2 domain;
1232-1436 1.25e-85

SH2 domain;


Pssm-ID: 464227 [Multi-domain]  Cd Length: 206  Bit Score: 277.88  E-value: 1.25e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552    1232 EDAEEERKLMMAEARAKRTHRVINHPYYFPFNGRQAEDYLRSKERGEFVIRQSSRGDDHLVITWKLDKDLFQHIDIQELE 1311
Cdd:pfam14633    2 ADKEELKKKKKAKARKTYVKRVIKHPLFHNFNYAQAEEYLASQDRGDVVIRPSSKGPDHLTVTWKVADGVYQHIDVLELD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552    1312 KENPLALGKVLIVDNQKYNDLDQIIVEYLQNKVRLLNEMTSSEKFKSGTKKDVVKFIEDYSRVNPNKSVYYFSLNHDNPG 1391
Cdd:pfam14633   82 KENEFSLGKTLRIGGEEYEDLDELIARHVQPMARKVEEMMNHRKFKDGTKEEVEEWLREEKKANPKRSPYAFCLSHKHPG 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 6321552    1392 WFYLMFKINANSKLYTWNVKLTNTGYFLVNYNYPSVIQLCNGFKT 1436
Cdd:pfam14633  162 YFLLSFKANKNSRVHHWYVKVTPDGFRLRGQQFPDVDALCNGFKK 206
YqgF pfam14639
Holliday-junction resolvase-like of SPT6; The YqgF domain of SPT6 proteins is homologous to ...
 744-895 5.29e-78

Holliday-junction resolvase-like of SPT6; The YqgF domain of SPT6 proteins is homologous to the E.coli RuvC but its putative catalytic site lacks the carboxylate side chains critical for coordinating magnesium ions that mediate phosphodiester bond-cleavage


Pssm-ID: 258777  Cd Length: 150  Bit Score: 254.02  E-value: 5.29e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     744 DPKIPKILSLTCGQGRFgADAIIAVYVNRKGDFIRDYKIVDNPFDKTNPEKFEDTLDNIIQSCQPNAIGINGPNPKTQKF 823
Cdd:pfam14639    1 QGKIPRVLGVAFGSGRF-DDAIICVLVNGEGEVTDFLKLAWREFDRENKAQFEETLKKFLLSKKPHVIGVSGENRDAQKF 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321552     824 YKRLQEVLHKKQiVDSRGHTIPIIYVEDEVAIRYQNSERAAQEFPNKPPLVKYCIALARYMHSPLLEYANLT 895
Cdd:pfam14639   80 YEDVQRVLHELE-QDSRLHTIGVILVDDEVAILYQNSKRAEAEFPDYPPLLRYCVALARYIQDPLLEYAQVC 150
HHH_7 pfam14635
Helix-hairpin-helix motif;
897-1000 8.32e-55

Helix-hairpin-helix motif;


Pssm-ID: 291309  Cd Length: 104  Bit Score: 185.83  E-value: 8.32e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     897 EEVRSLSIHPHQNLLSSEQLSWALETAFVDIVNLVSVEVNKATDNNYYASALKYISGFGKRKAIDFLQSLQRLNEPLLAR 976
Cdd:pfam14635    1 EDILSLSFHPLQELLPKEELLKALETAFVDIVNLVGVDVNEAIANKYEAAILPYIAGLGPRKADHLLKILAANNGRLDNR 80

                           90       100
                   ....*....|....*....|....
gi 6321552     977 QQLITHNILHKTIFMNSAGFLYIS 1000
Cdd:pfam14635   81 SQLITKCIMGPKVFMNCAGFLIID 104
HTH_44 pfam14641
Helix-turn-helix DNA-binding domain of SPT6; This helix-turn-helix represents the first of two ...
 336-445 9.74e-50

Helix-turn-helix DNA-binding domain of SPT6; This helix-turn-helix represents the first of two DNA-binding domains on the SPT6 proteins.


Pssm-ID: 464230  Cd Length: 115  Bit Score: 171.59  E-value: 9.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     336 YGNMSSEDQELERNWIAEKISVDKNFDANYDLTEFKEAIGNAIKFITKENLEVPFIYAYRRNYISSREKDGF-----LLT 410
Cdd:pfam14641    1 YIDLTDEELEEEANWISNRLLVEKNDDFERLLEPFKEAVGNVLEFISKDNLEVPFIWQHRRDYLLHSEKDGFeighkLLN 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 6321552     411 EDDLWDIVSLDIEFHSLVNKKDYVQRFYAELHIDD 445
Cdd:pfam14641   81 EDDLWRIVQLDIKFHSLIEKRNNLEKLYEKLGIDD 115
SH2_Nterm_SPT6_like cd09918
N-terminal Src homology 2 (SH2) domain found in Spt6; N-terminal SH2 domain in Spt6. Spt6 is ...
 1255-1339 1.68e-38

N-terminal Src homology 2 (SH2) domain found in Spt6; N-terminal SH2 domain in Spt6. Spt6 is an essential transcription elongation factor and histone chaperone that binds the C-terminal repeat domain (CTD) of RNA polymerase II. Spt6 contains a tandem SH2 domain with a novel structure and CTD-binding mode. The tandem SH2 domain binds to a serine 2-phosphorylated CTD peptide in vitro, whereas its N-terminal SH2 subdomain does not. CTD binding requires a positively charged crevice in the C-terminal SH2 subdomain, which lacks the canonical phospho-binding pocket of SH2 domains. The tandem SH2 domain is apparently required for transcription elongation in vivo as its deletion in cells is lethal in the presence of 6-azauracil. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198174  Cd Length: 85  Bit Score: 138.52  E-value: 1.68e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552  1255 NHPYYFPFNGRQAEDYLRSKERGEFVIRQSSRGDDHLVITWKLDKDLFQHIDIQELEKENPLALGKVLIVDNQKYNDLDQ 1334
Cdd:cd09918    1 RHPLFKNVNYKQAEAYLKSKDVGEVVIRPSSKGVDHLTVTWKVADGVYQHIDIEELNKENPFSLGKELIIGGEEYEDLDE 80


                 ....*
gi 6321552  1335 IIVEY 1339
Cdd:cd09918   81 IIARF 85
SPT6_acidic pfam14632
Acidic N-terminal SPT6; The N-terminus of SPT6 is highly acidic. The full SPT6 protein is a ...
 28-128 2.17e-15

Acidic N-terminal SPT6; The N-terminus of SPT6 is highly acidic. The full SPT6 protein is a transcription regulator, but the exact function of this acidic region is not certain.


Pssm-ID: 464226  Cd Length: 89  Bit Score: 72.89  E-value: 2.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552      28 SEEEEGEDvfdsseededideDEDEARKVQEGFIVNDDDENEDPGTSISKKRRKH---KRREREEDDRLSEDDLDLLMEN 104
Cdd:pfam14632    2 SSEEEDDD-------------DEEEARKVREGFIVDDDEEEEEEEEDDEERRRRKkkrKRREEEEDDRLDEDDLDLIEEN 68

                           90       100
                   ....*....|....*....|....
gi 6321552     105 AGVERTKASSssgKFKRLKRVGDE 128
Cdd:pfam14632   69 TGVKRRRSSS---KFKRLKRGHDD 89
YqgFc smart00732
Likely ribonuclease with RNase H fold; YqgF proteins are likely to function as an alternative ...
 760-858 1.60e-11

Likely ribonuclease with RNase H fold; YqgF proteins are likely to function as an alternative to RuvC in most bacteria, and could be the principal holliday junction resolvases in low-GC Gram-positive bacteria. In Spt6p orthologues, the catalytic residues are substituted indicating that they lack enzymatic functions.


Pssm-ID: 128971  Cd Length: 99  Bit Score: 62.20  E-value: 1.60e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552      760 FGADAIIAVYVNRKGDFIRDYKIVDNpfdkTNPEKFEDTLDNIIQSCQPNAIGINGPNP----KTQKFYKRLQEVLHKKq 835
Cdd:smart00732    8 PGRKGIGVAVVDETGKLADPLEVIPR----TNKEADAARLKKLIKKYQPDLIVIGLPLNmngtASRETEEAFAELLKER- 82

                            90       100
                    ....*....|....*....|...
gi 6321552      836 ivdsrgHTIPIIYVEDEVAIRYQ 858
Cdd:smart00732   83 ------FNLPVVLVDERLATVYA 99
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
 1256-1343 8.25e-11

Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae.


Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 59.55  E-value: 8.25e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     1256 HPYYFPF-NGRQAEDYLRSKERGEFVIRQSSRGDDHLVITWKlDKDLFQHIDIQELEKenplalGKVLIVDNQKYNDLDQ 1334
Cdd:smart00252    1 QPWYHGFiSREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVR-VKGKVKHYRIRRNED------GKFYLEGGRKFPSLVE 73


                    ....*....
gi 6321552     1335 IIVEYLQNK 1343
Cdd:smart00252   74 LVEHYQKNS 82
 
Name Accession Description Interval E-value
SH2_2 pfam14633
SH2 domain;
1232-1436 1.25e-85

SH2 domain;


Pssm-ID: 464227 [Multi-domain]  Cd Length: 206  Bit Score: 277.88  E-value: 1.25e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552    1232 EDAEEERKLMMAEARAKRTHRVINHPYYFPFNGRQAEDYLRSKERGEFVIRQSSRGDDHLVITWKLDKDLFQHIDIQELE 1311
Cdd:pfam14633    2 ADKEELKKKKKAKARKTYVKRVIKHPLFHNFNYAQAEEYLASQDRGDVVIRPSSKGPDHLTVTWKVADGVYQHIDVLELD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552    1312 KENPLALGKVLIVDNQKYNDLDQIIVEYLQNKVRLLNEMTSSEKFKSGTKKDVVKFIEDYSRVNPNKSVYYFSLNHDNPG 1391
Cdd:pfam14633   82 KENEFSLGKTLRIGGEEYEDLDELIARHVQPMARKVEEMMNHRKFKDGTKEEVEEWLREEKKANPKRSPYAFCLSHKHPG 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 6321552    1392 WFYLMFKINANSKLYTWNVKLTNTGYFLVNYNYPSVIQLCNGFKT 1436
Cdd:pfam14633  162 YFLLSFKANKNSRVHHWYVKVTPDGFRLRGQQFPDVDALCNGFKK 206
YqgF pfam14639
Holliday-junction resolvase-like of SPT6; The YqgF domain of SPT6 proteins is homologous to ...
 744-895 5.29e-78

Holliday-junction resolvase-like of SPT6; The YqgF domain of SPT6 proteins is homologous to the E.coli RuvC but its putative catalytic site lacks the carboxylate side chains critical for coordinating magnesium ions that mediate phosphodiester bond-cleavage


Pssm-ID: 258777  Cd Length: 150  Bit Score: 254.02  E-value: 5.29e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     744 DPKIPKILSLTCGQGRFgADAIIAVYVNRKGDFIRDYKIVDNPFDKTNPEKFEDTLDNIIQSCQPNAIGINGPNPKTQKF 823
Cdd:pfam14639    1 QGKIPRVLGVAFGSGRF-DDAIICVLVNGEGEVTDFLKLAWREFDRENKAQFEETLKKFLLSKKPHVIGVSGENRDAQKF 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321552     824 YKRLQEVLHKKQiVDSRGHTIPIIYVEDEVAIRYQNSERAAQEFPNKPPLVKYCIALARYMHSPLLEYANLT 895
Cdd:pfam14639   80 YEDVQRVLHELE-QDSRLHTIGVILVDDEVAILYQNSKRAEAEFPDYPPLLRYCVALARYIQDPLLEYAQVC 150
HHH_7 pfam14635
Helix-hairpin-helix motif;
897-1000 8.32e-55

Helix-hairpin-helix motif;


Pssm-ID: 291309  Cd Length: 104  Bit Score: 185.83  E-value: 8.32e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     897 EEVRSLSIHPHQNLLSSEQLSWALETAFVDIVNLVSVEVNKATDNNYYASALKYISGFGKRKAIDFLQSLQRLNEPLLAR 976
Cdd:pfam14635    1 EDILSLSFHPLQELLPKEELLKALETAFVDIVNLVGVDVNEAIANKYEAAILPYIAGLGPRKADHLLKILAANNGRLDNR 80

                           90       100
                   ....*....|....*....|....
gi 6321552     977 QQLITHNILHKTIFMNSAGFLYIS 1000
Cdd:pfam14635   81 SQLITKCIMGPKVFMNCAGFLIID 104
HTH_44 pfam14641
Helix-turn-helix DNA-binding domain of SPT6; This helix-turn-helix represents the first of two ...
 336-445 9.74e-50

Helix-turn-helix DNA-binding domain of SPT6; This helix-turn-helix represents the first of two DNA-binding domains on the SPT6 proteins.


Pssm-ID: 464230  Cd Length: 115  Bit Score: 171.59  E-value: 9.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     336 YGNMSSEDQELERNWIAEKISVDKNFDANYDLTEFKEAIGNAIKFITKENLEVPFIYAYRRNYISSREKDGF-----LLT 410
Cdd:pfam14641    1 YIDLTDEELEEEANWISNRLLVEKNDDFERLLEPFKEAVGNVLEFISKDNLEVPFIWQHRRDYLLHSEKDGFeighkLLN 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 6321552     411 EDDLWDIVSLDIEFHSLVNKKDYVQRFYAELHIDD 445
Cdd:pfam14641   81 EDDLWRIVQLDIKFHSLIEKRNNLEKLYEKLGIDD 115
SH2_Nterm_SPT6_like cd09918
N-terminal Src homology 2 (SH2) domain found in Spt6; N-terminal SH2 domain in Spt6. Spt6 is ...
 1255-1339 1.68e-38

N-terminal Src homology 2 (SH2) domain found in Spt6; N-terminal SH2 domain in Spt6. Spt6 is an essential transcription elongation factor and histone chaperone that binds the C-terminal repeat domain (CTD) of RNA polymerase II. Spt6 contains a tandem SH2 domain with a novel structure and CTD-binding mode. The tandem SH2 domain binds to a serine 2-phosphorylated CTD peptide in vitro, whereas its N-terminal SH2 subdomain does not. CTD binding requires a positively charged crevice in the C-terminal SH2 subdomain, which lacks the canonical phospho-binding pocket of SH2 domains. The tandem SH2 domain is apparently required for transcription elongation in vivo as its deletion in cells is lethal in the presence of 6-azauracil. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198174  Cd Length: 85  Bit Score: 138.52  E-value: 1.68e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552  1255 NHPYYFPFNGRQAEDYLRSKERGEFVIRQSSRGDDHLVITWKLDKDLFQHIDIQELEKENPLALGKVLIVDNQKYNDLDQ 1334
Cdd:cd09918    1 RHPLFKNVNYKQAEAYLKSKDVGEVVIRPSSKGVDHLTVTWKVADGVYQHIDIEELNKENPFSLGKELIIGGEEYEDLDE 80


                 ....*
gi 6321552  1335 IIVEY 1339
Cdd:cd09918   81 IIARF 85
SH2_Cterm_SPT6_like cd09928
C-terminal Src homology 2 (SH2) domain found in Spt6; Spt6 is an essential transcription ...
 1349-1437 2.01e-31

C-terminal Src homology 2 (SH2) domain found in Spt6; Spt6 is an essential transcription elongation factor and histone chaperone that binds the C-terminal repeat domain (CTD) of RNA polymerase II. Spt6 contains a tandem SH2 domain with a novel structure and CTD-binding mode. The tandem SH2 domain binds to a serine 2-phosphorylated CTD peptide in vitro, whereas its N-terminal SH2 subdomain does not. CTD binding requires a positively charged crevice in the C-terminal SH2 subdomain, which lacks the canonical phospho-binding pocket of SH2 domains. The tandem SH2 domain is apparently required for transcription elongation in vivo as its deletion in cells is lethal in the presence of 6-azauracil. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198182  Cd Length: 89  Bit Score: 118.48  E-value: 2.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552  1349 EMTSSEKFKSGTKKDVVKFIEDYSRVNPNKSVYYFSLNHDNPGWFYLMFKInANSKLYTWNVKLTNTGYFLVNYNYPSVI 1428
Cdd:cd09928    1 EMLNHHKYFRGTKEEVEKLLKEEKKANPKRIPYAFCVSKKYPGKFLLSYLP-ANTRVRHEYVKVTPDGFRFRGQVFPSVD 79


                 ....*....
gi 6321552  1429 QLCNGFKTL 1437
Cdd:cd09928   80 SLLNWFKEH 88
SPT6_acidic pfam14632
Acidic N-terminal SPT6; The N-terminus of SPT6 is highly acidic. The full SPT6 protein is a ...
 28-128 2.17e-15

Acidic N-terminal SPT6; The N-terminus of SPT6 is highly acidic. The full SPT6 protein is a transcription regulator, but the exact function of this acidic region is not certain.


Pssm-ID: 464226  Cd Length: 89  Bit Score: 72.89  E-value: 2.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552      28 SEEEEGEDvfdsseededideDEDEARKVQEGFIVNDDDENEDPGTSISKKRRKH---KRREREEDDRLSEDDLDLLMEN 104
Cdd:pfam14632    2 SSEEEDDD-------------DEEEARKVREGFIVDDDEEEEEEEEDDEERRRRKkkrKRREEEEDDRLDEDDLDLIEEN 68

                           90       100
                   ....*....|....*....|....
gi 6321552     105 AGVERTKASSssgKFKRLKRVGDE 128
Cdd:pfam14632   69 TGVKRRRSSS---KFKRLKRGHDD 89
SH2 pfam00017
SH2 domain;
1258-1339 8.09e-13

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 64.93  E-value: 8.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552    1258 YYFPFNGR-QAEDYLRS-KERGEFVIRQSSRGDDHLVITWKlDKDLFQHIDIQELEKenplalGKVLIVDNQKYNDLDQI 1335
Cdd:pfam00017    1 WYHGKISRqEAERLLLNgKPDGTFLVRESESTPGGYTLSVR-DDGKVKHYKIQSTDN------GGYYISGGVKFSSLAEL 73


                   ....
gi 6321552    1336 IVEY 1339
Cdd:pfam00017   74 VEHY 77
YqgFc smart00732
Likely ribonuclease with RNase H fold; YqgF proteins are likely to function as an alternative ...
 760-858 1.60e-11

Likely ribonuclease with RNase H fold; YqgF proteins are likely to function as an alternative to RuvC in most bacteria, and could be the principal holliday junction resolvases in low-GC Gram-positive bacteria. In Spt6p orthologues, the catalytic residues are substituted indicating that they lack enzymatic functions.


Pssm-ID: 128971  Cd Length: 99  Bit Score: 62.20  E-value: 1.60e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552      760 FGADAIIAVYVNRKGDFIRDYKIVDNpfdkTNPEKFEDTLDNIIQSCQPNAIGINGPNP----KTQKFYKRLQEVLHKKq 835
Cdd:smart00732    8 PGRKGIGVAVVDETGKLADPLEVIPR----TNKEADAARLKKLIKKYQPDLIVIGLPLNmngtASRETEEAFAELLKER- 82

                            90       100
                    ....*....|....*....|...
gi 6321552      836 ivdsrgHTIPIIYVEDEVAIRYQ 858
Cdd:smart00732   83 ------FNLPVVLVDERLATVYA 99
SH2 smart00252
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ...
 1256-1343 8.25e-11

Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae.


Pssm-ID: 214585 [Multi-domain]  Cd Length: 84  Bit Score: 59.55  E-value: 8.25e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552     1256 HPYYFPF-NGRQAEDYLRSKERGEFVIRQSSRGDDHLVITWKlDKDLFQHIDIQELEKenplalGKVLIVDNQKYNDLDQ 1334
Cdd:smart00252    1 QPWYHGFiSREEAEKLLKNEGDGDFLVRDSESSPGDYVLSVR-VKGKVKHYRIRRNED------GKFYLEGGRKFPSLVE 73


                    ....*....
gi 6321552     1335 IIVEYLQNK 1343
Cdd:smart00252   74 LVEHYQKNS 82
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
 1257-1339 1.15e-09

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


Pssm-ID: 198173 [Multi-domain]  Cd Length: 79  Bit Score: 56.31  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552  1257 PYYFPFNGR-QAEDYLRSKERGEFVIRQSSRGDDHLVITWKLDKDLFQHIDIQELEKEnplalGKVLIVDNQKYNDLDQI 1335
Cdd:cd00173    1 PWFHGSISReEAERLLRGKPDGTFLVRESSSEPGDYVLSVRSGDGKVKHYLIERNEGG-----YYLLGGSGRTFPSLPEL 75


                 ....
gi 6321552  1336 IVEY 1339
Cdd:cd00173   76 VEHY 79
SH2_SH2D7 cd10417
Src homology 2 domain found in the SH2 domain containing protein 7 (SH2D7); SH2D7 contains a ...
 1265-1353 2.06e-03

Src homology 2 domain found in the SH2 domain containing protein 7 (SH2D7); SH2D7 contains a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 199832  Cd Length: 102  Bit Score: 39.11  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552  1265 RQAEDYLRSKERGEFVIRQSSRGDDHlVITWKlDKDLFQHIDIQELEKENPLALGkvlivDNQKYNDLDQIIVEYLQNKV 1344
Cdd:cd10417   17 KQTEQLLRDKALGSFLIRLSDRATGY-ILSYR-GSDRCRHFVINQLRNRRYLISG-----DTSSHSTLAELVRHYQEVQL 89


                 ....*....
gi 6321552  1345 RLLNEMTSS 1353
Cdd:cd10417   90 EPFGETLTA 98
SH2_ABL cd09935
Src homology 2 (SH2) domain found in Abelson murine lymphosarcoma virus (ABL) proteins; ...
 1256-1342 4.06e-03

Src homology 2 (SH2) domain found in Abelson murine lymphosarcoma virus (ABL) proteins; ABL-family proteins are highly conserved tyrosine kinases. Each ABL protein contains an SH3-SH2-TK (Src homology 3-Src homology 2-tyrosine kinase) domain cassette, which confers autoregulated kinase activity and is common among nonreceptor tyrosine kinases. Several types of posttranslational modifications control ABL catalytic activity, subcellular localization, and stability, with consequences for both cytoplasmic and nuclear ABL functions. Binding partners provide additional regulation of ABL catalytic activity, substrate specificity, and downstream signaling. By combining this cassette with actin-binding and -bundling domain, ABL proteins are capable of connecting phosphoregulation with actin-filament reorganization. Vertebrate paralogs, ABL1 and ABL2, have evolved to perform specialized functions. ABL1 includes nuclear localization signals and a DNA binding domain which is used to mediate DNA damage-repair functions, while ABL2 has additional binding capacity for actin and for microtubules to enhance its cytoskeletal remodeling functions. SH2 is involved in several autoinhibitory mechanism that constrain the enzymatic activity of the ABL-family kinases. In one mechanism SH2 and SH3 cradle the kinase domain while a cap sequence stabilizes the inactive conformation resulting in a locked inactive state. Another involves phosphatidylinositol 4,5-bisphosphate (PIP2) which binds the SH2 domain through residues normally required for phosphotyrosine binding in the linker segment between the SH2 and kinase domains. The SH2 domain contributes to ABL catalytic activity and target site specificity. It is thought that the ABL catalytic site and SH2 pocket have coevolved to recognize the same sequences. Recent work now supports a hierarchical processivity model in which the substrate target site most compatible with ABL kinase domain preferences is phosphorylated with greatest efficiency. If this site is compatible with the ABL SH2 domain specificity, it will then reposition and dock in the SH2 pocket. This mechanism also explains how ABL kinases phosphorylates poor targets on the same substrate if they are properly positioned and how relatively poor substrate proteins might be recruited to ABL through a complex with strong substrates that can also dock with the SH2 pocket. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198189  Cd Length: 94  Bit Score: 38.14  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321552  1256 HPYYFPFNGRQAEDY-LRSKERGEFVIRQSSRGDDHLVITWKLDKDLFqHIDIQElekENPlalGKVLIVDNQKYNDLDQ 1334
Cdd:cd09935    3 HSWYHGPISRNAAEYlLSSGINGSFLVRESESSPGQYSISLRYDGRVY-HYRISE---DSD---GKVYVTQEHRFNTLAE 75


                 ....*...
gi 6321552  1335 IIVEYLQN 1342
Cdd:cd09935   76 LVHHHSKN 83
 
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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