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Conserved domains on  [gi|1889952546|ref|XP_035691771|]
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transcription elongation factor SPT6-like isoform X2 [Branchiostoma floridae]

Protein Classification

DLD and SH2_Cterm_SPT6_like domain-containing protein( domain architecture ID 13863247)

protein containing domains YqgFc, DLD, SH2_Nterm_SPT6_like, and SH2_Cterm_SPT6_like

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SH2_2 pfam14633
SH2 domain;
1344-1548 4.27e-109

SH2 domain;


:

Pssm-ID: 464227 [Multi-domain]  Cd Length: 206  Bit Score: 345.67  E-value: 4.27e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1344 DRKADDEAKKKQARTTYVKRVIVHPCFHNISYKQAVKLMESQDQGDVIVRPSSKGPDHLTVTWKVDDGIYQHIDVREEGK 1423
Cdd:pfam14633    3 DKEELKKKKKAKARKTYVKRVIKHPLFHNFNYAQAEEYLASQDRGDVVIRPSSKGPDHLTVTWKVADGVYQHIDVLELDK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1424 ENAFSLGQSLWINNEEFEDLDEIIARHIQPMASFVRDLTNHKYYQAaegGKREAIEKIIRDEKKKAPSKIPYIISASKEY 1503
Cdd:pfam14633   83 ENEFSLGKTLRIGGEEYEDLDELIARHVQPMARKVEEMMNHRKFKD---GTKEEVEEWLREEKKANPKRSPYAFCLSHKH 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1889952546 1504 PGKFLLSYQPKTSPR--HEFVTVTPDGFRFRQLIHHSVNALFRWFKE 1548
Cdd:pfam14633  160 PGYFLLSFKANKNSRvhHWYVKVTPDGFRLRGQQFPDVDALCNGFKK 206
RuvC-like super family cl21482
Crossover junction endodeoxyribonuclease RuvC and similar proteins; The RuvC-like family ...
811-965 5.08e-49

Crossover junction endodeoxyribonuclease RuvC and similar proteins; The RuvC-like family consists of bacterial RuvC, fungal Cruciform cutting endonuclease 1 (CCE1), bacterial YqgF and monokaryotic chloroplast 1 protein (MOC1). RuvC, CCE1 and MOC1 are Holliday junction resolvases (HJRs), endonucleases that specifically resolve Holliday junction DNA intermediates during homologous recombination. RuvC is part of the RuvABC pathway in Escherichia coli and other Gram-negative bacteria that is involved in processing Holliday junctions, which are formed by the reciprocal exchange of strands between two DNA duplexes. CCE1 is a HJR specific for 4-way junctions; it is involved in the maintenance of mitochondrial DNA. Escherichia coli YqgF has been shown to act as a pre-16S rRNA nuclease, presumably as a monomer. It is involved in the processing of pre-16S rRNA during ribosome maturation. HJRs occur in archaea, bacteria, and in the mitochondria of certain fungi. RuvC and its orthologs are homodimers and display structural similarity to RNase H and Hsp70.


The actual alignment was detected with superfamily member pfam14639:

Pssm-ID: 473878  Cd Length: 150  Bit Score: 171.59  E-value: 5.08e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  811 KGLRVMGLAYSS-DWDTASFAAVIDGEGDVVDFLRLAhlmkrrnaYREADRENKLSDMESIKNLILNKKPHVIVIGAENR 889
Cdd:pfam14639    3 KIPRVLGVAFGSgRFDDAIICVLVNGEGEVTDFLKLA--------WREFDRENKAQFEETLKKFLLSKKPHVIGVSGENR 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889952546  890 DAQSVIDDVKLCVKELEEEEQLAPIAVELLDNELSRFIMNSPRAEAEHRDYPPLLRQALSLARRMQDPLIEFSQLC 965
Cdd:pfam14639   75 DAQKFYEDVQRVLHELEQDSRLHTIGVILVDDEVAILYQNSKRAEAEFPDYPPLLRYCVALARYIQDPLLEYAQVC 150
HHH_5 super family cl22429
Helix-hairpin-helix domain;
969-1072 8.84e-45

Helix-hairpin-helix domain;


The actual alignment was detected with superfamily member pfam14635:

Pssm-ID: 473956  Cd Length: 104  Bit Score: 157.32  E-value: 8.84e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  969 DDLLCLRFHTLQEQVSREDLLHALELEFINRVNEVGVDINRCVANNHTTTLAQFVCGLGPRKAAYILKVLKQNNARLENR 1048
Cdd:pfam14635    1 EDILSLSFHPLQELLPKEELLKALETAFVDIVNLVGVDVNEAIANKYEAAILPYIAGLGPRKADHLLKILAANNGRLDNR 80
                           90       100
                   ....*....|....*....|....
gi 1889952546 1049 NQLVMMCHMGPKVFMNCAGFIKID 1072
Cdd:pfam14635   81 SQLITKCIMGPKVFMNCAGFLIID 104
Tex super family cl34417
Transcriptional accessory protein Tex/SPT6 [Transcription];
599-1163 5.47e-31

Transcriptional accessory protein Tex/SPT6 [Transcription];


The actual alignment was detected with superfamily member COG2183:

Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 132.07  E-value: 5.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  599 DQYPAEPNDLSKEFVNS--QFPSEEKVLQGARHMVAMQLSREPLVRQCVRQTYFERAKVSTKPTKKGRKEID--EMHYGY 674
Cdd:COG2183    131 AQPTGDPEAEAAKYINEekGVADVEAALDGARDILAERISEDAELRGKLRELLWKEGVLVSKVKKGKEEEGAkfRDYFDY 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  675 tfkylkNKPVKDLTGDQFLKMSIAEDEGLLKTHVSIDGETTQSYfeeIKQLYYRDEFShlvqEWNTQRTMVLERMLKFIL 754
Cdd:COG2183    211 ------SEPLKKIPSHRILALNRGEKEGVLKVKLEPDEEEAEAY---IARRFIKDQGR----PADEWLKEAVRDAYKRLL 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  755 YPQMEKELRSKLVQESKDGIIKSCCRKLYNWLKVAPYqpeqqieeedeyiegmgssKGLRVMGLayssdwD----TASFA 830
Cdd:COG2183    278 APSLERELRNELKEKAEEEAIKVFAENLRDLLLAAPA-------------------GGKVVLGL------DpgfrTGCKV 332
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  831 AVIDGEGDVVD----FLrlaHlmKRRNAYREAdrenklsdMESIKNLILNKKPHVIVIGaeN----Rdaqsviddvklcv 902
Cdd:COG2183    333 AVVDETGKLLDtatiYP---H--PPQNKWEEA--------AKTLAALIKKYKVELIAIG--NgtasR------------- 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  903 keleEEEQLAPIAVELLDNELSRFIMN---------SPRAEAEHRDYPPLLRQALSLARRMQDPLIEfsqlcvnnddllc 973
Cdd:COG2183    385 ----ETEQFVAELIKELDLKVQYVIVSeagasvysaSELAREEFPDLDVTVRGAVSIARRLQDPLAE------------- 447
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  974 lrfhtL-----------QEQ--VSREDLLHALELEFINRVNEVGVDINrcvannhtT---TLAQFVCGLGPRKAAYILKV 1037
Cdd:COG2183    448 -----LvkidpksigvgQYQhdVNQKKLKRSLDAVVEDCVNAVGVDLN--------TasaPLLSYVSGLNPTLAKNIVAY 514
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1038 LKQNNArLENRNQLVMMCHMGPKVFMNCAGFIKIDtkslgDSEqyiELLDGSRVHPETYDWARKMavdaleydesAEDAN 1117
Cdd:COG2183    515 RDENGA-FKSRKELLKVPRLGPKAFEQAAGFLRIR-----DGD---NPLDNSAVHPESYPVVEKI----------LKDLG 575
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1889952546 1118 paAALEEILETPERLKDLDLDAFAEELerqgFGnkSITLYDIRAEL 1163
Cdd:COG2183    576 --VSVKDLIGNKELLKKLDPEKYADEL----FG--LPTLRDILKEL 613
HTH_44 pfam14641
Helix-turn-helix DNA-binding domain of SPT6; This helix-turn-helix represents the first of two ...
367-441 4.24e-25

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: 101.49  E-value: 4.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  367 YSRKEPSTVGKIRDALNFIRNQHFEVPFIAFYRKEYVE-----------PELNINDLWRIWQWDEKWTQLRNRKRNMTRL 435
Cdd:pfam14641   28 FERLLEPFKEAVGNVLEFISKDNLEVPFIWQHRRDYLLhsekdgfeighKLLNEDDLWRIVQLDIKFHSLIEKRNNLEKL 107

                   ....*.
gi 1889952546  436 FEKMQT 441
Cdd:pfam14641  108 YEKLGI 113
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
1262-1316 6.64e-12

S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.


:

Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 62.69  E-value: 6.64e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSC 1316
Cdd:pfam00575   18 GAFVDLGNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
SPT6_acidic pfam14632
Acidic N-terminal SPT6; The N-terminus of SPT6 is highly acidic. The full SPT6 protein is a ...
84-140 1.77e-04

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: 42.08  E-value: 1.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889952546   84 EASAGEDSEGEIGGKK--RRRRSSIDDRLEDEDYDLIEENLGVKVKR--KRFRRVQALSDD 140
Cdd:pfam14632   29 EEEEEEDDEERRRRKKkrKRREEEEDDRLDEDDLDLIEENTGVKRRRssSKFKRLKRGHDD 89
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1552-1805 5.16e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1552 DPIPGATPVNVRhrTPMAPSRPENTPAPSGinlqgvdPAQLSQLQKAISNFPSNLSTQQVFSALAAATGQGSSATPAqwg 1631
Cdd:PHA03247  2738 APAPPAVPAGPA--TPGGPARPARPPTTAG-------PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA--- 2805
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1632 sqgygqsqgqyhagagysgaagsSSYQTFATPNPMATPMMTPAYPSATPAQGQPQTTPRYQPTPQSSWGHGhGRAAASAS 1711
Cdd:PHA03247  2806 -----------------------DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG-GSVAPGGD 2861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1712 TSGATPSRAAPTprasTSAASAGTDWGKAALAWVQQQRNK--QRGGDTPKVRTPGHHTPGHHTPSHHTPSHRTPSHRTPT 1789
Cdd:PHA03247  2862 VRRRPPSRSPAA----KPAAPARPPVRRLARPAVSRSTESfaLPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937
                          250
                   ....*....|....*.
gi 1889952546 1790 HRAPTMSPSPMVEGTP 1805
Cdd:PHA03247  2938 RPQPPLAPTTDPAGAG 2953
 
Name Accession Description Interval E-value
SH2_2 pfam14633
SH2 domain;
1344-1548 4.27e-109

SH2 domain;


Pssm-ID: 464227 [Multi-domain]  Cd Length: 206  Bit Score: 345.67  E-value: 4.27e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1344 DRKADDEAKKKQARTTYVKRVIVHPCFHNISYKQAVKLMESQDQGDVIVRPSSKGPDHLTVTWKVDDGIYQHIDVREEGK 1423
Cdd:pfam14633    3 DKEELKKKKKAKARKTYVKRVIKHPLFHNFNYAQAEEYLASQDRGDVVIRPSSKGPDHLTVTWKVADGVYQHIDVLELDK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1424 ENAFSLGQSLWINNEEFEDLDEIIARHIQPMASFVRDLTNHKYYQAaegGKREAIEKIIRDEKKKAPSKIPYIISASKEY 1503
Cdd:pfam14633   83 ENEFSLGKTLRIGGEEYEDLDELIARHVQPMARKVEEMMNHRKFKD---GTKEEVEEWLREEKKANPKRSPYAFCLSHKH 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1889952546 1504 PGKFLLSYQPKTSPR--HEFVTVTPDGFRFRQLIHHSVNALFRWFKE 1548
Cdd:pfam14633  160 PGYFLLSFKANKNSRvhHWYVKVTPDGFRLRGQQFPDVDALCNGFKK 206
YqgF pfam14639
Holliday-junction resolvase-like of SPT6; The YqgF domain of SPT6 proteins is homologous to ...
811-965 5.08e-49

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: 171.59  E-value: 5.08e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  811 KGLRVMGLAYSS-DWDTASFAAVIDGEGDVVDFLRLAhlmkrrnaYREADRENKLSDMESIKNLILNKKPHVIVIGAENR 889
Cdd:pfam14639    3 KIPRVLGVAFGSgRFDDAIICVLVNGEGEVTDFLKLA--------WREFDRENKAQFEETLKKFLLSKKPHVIGVSGENR 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889952546  890 DAQSVIDDVKLCVKELEEEEQLAPIAVELLDNELSRFIMNSPRAEAEHRDYPPLLRQALSLARRMQDPLIEFSQLC 965
Cdd:pfam14639   75 DAQKFYEDVQRVLHELEQDSRLHTIGVILVDDEVAILYQNSKRAEAEFPDYPPLLRYCVALARYIQDPLLEYAQVC 150
HHH_7 pfam14635
Helix-hairpin-helix motif;
969-1072 8.84e-45

Helix-hairpin-helix motif;


Pssm-ID: 291309  Cd Length: 104  Bit Score: 157.32  E-value: 8.84e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  969 DDLLCLRFHTLQEQVSREDLLHALELEFINRVNEVGVDINRCVANNHTTTLAQFVCGLGPRKAAYILKVLKQNNARLENR 1048
Cdd:pfam14635    1 EDILSLSFHPLQELLPKEELLKALETAFVDIVNLVGVDVNEAIANKYEAAILPYIAGLGPRKADHLLKILAANNGRLDNR 80
                           90       100
                   ....*....|....*....|....
gi 1889952546 1049 NQLVMMCHMGPKVFMNCAGFIKID 1072
Cdd:pfam14635   81 SQLITKCIMGPKVFMNCAGFLIID 104
SH2_Nterm_SPT6_like cd09918
N-terminal Src homology 2 (SH2) domain found in Spt6; N-terminal SH2 domain in Spt6. Spt6 is ...
1367-1450 1.17e-44

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: 156.24  E-value: 1.17e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1367 HPCFHNISYKQAVKLMESQDQGDVIVRPSSKGPDHLTVTWKVDDGIYQHIDVREEGKENAFSLGQSLWINNEEFEDLDEI 1446
Cdd:cd09918      2 HPLFKNVNYKQAEAYLKSKDVGEVVIRPSSKGVDHLTVTWKVADGVYQHIDIEELNKENPFSLGKELIIGGEEYEDLDEI 81

                   ....
gi 1889952546 1447 IARH 1450
Cdd:cd09918     82 IARF 85
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
599-1163 5.47e-31

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 132.07  E-value: 5.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  599 DQYPAEPNDLSKEFVNS--QFPSEEKVLQGARHMVAMQLSREPLVRQCVRQTYFERAKVSTKPTKKGRKEID--EMHYGY 674
Cdd:COG2183    131 AQPTGDPEAEAAKYINEekGVADVEAALDGARDILAERISEDAELRGKLRELLWKEGVLVSKVKKGKEEEGAkfRDYFDY 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  675 tfkylkNKPVKDLTGDQFLKMSIAEDEGLLKTHVSIDGETTQSYfeeIKQLYYRDEFShlvqEWNTQRTMVLERMLKFIL 754
Cdd:COG2183    211 ------SEPLKKIPSHRILALNRGEKEGVLKVKLEPDEEEAEAY---IARRFIKDQGR----PADEWLKEAVRDAYKRLL 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  755 YPQMEKELRSKLVQESKDGIIKSCCRKLYNWLKVAPYqpeqqieeedeyiegmgssKGLRVMGLayssdwD----TASFA 830
Cdd:COG2183    278 APSLERELRNELKEKAEEEAIKVFAENLRDLLLAAPA-------------------GGKVVLGL------DpgfrTGCKV 332
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  831 AVIDGEGDVVD----FLrlaHlmKRRNAYREAdrenklsdMESIKNLILNKKPHVIVIGaeN----Rdaqsviddvklcv 902
Cdd:COG2183    333 AVVDETGKLLDtatiYP---H--PPQNKWEEA--------AKTLAALIKKYKVELIAIG--NgtasR------------- 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  903 keleEEEQLAPIAVELLDNELSRFIMN---------SPRAEAEHRDYPPLLRQALSLARRMQDPLIEfsqlcvnnddllc 973
Cdd:COG2183    385 ----ETEQFVAELIKELDLKVQYVIVSeagasvysaSELAREEFPDLDVTVRGAVSIARRLQDPLAE------------- 447
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  974 lrfhtL-----------QEQ--VSREDLLHALELEFINRVNEVGVDINrcvannhtT---TLAQFVCGLGPRKAAYILKV 1037
Cdd:COG2183    448 -----LvkidpksigvgQYQhdVNQKKLKRSLDAVVEDCVNAVGVDLN--------TasaPLLSYVSGLNPTLAKNIVAY 514
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1038 LKQNNArLENRNQLVMMCHMGPKVFMNCAGFIKIDtkslgDSEqyiELLDGSRVHPETYDWARKMavdaleydesAEDAN 1117
Cdd:COG2183    515 RDENGA-FKSRKELLKVPRLGPKAFEQAAGFLRIR-----DGD---NPLDNSAVHPESYPVVEKI----------LKDLG 575
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1889952546 1118 paAALEEILETPERLKDLDLDAFAEELerqgFGnkSITLYDIRAEL 1163
Cdd:COG2183    576 --VSVKDLIGNKELLKKLDPEKYADEL----FG--LPTLRDILKEL 613
HTH_44 pfam14641
Helix-turn-helix DNA-binding domain of SPT6; This helix-turn-helix represents the first of two ...
367-441 4.24e-25

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: 101.49  E-value: 4.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  367 YSRKEPSTVGKIRDALNFIRNQHFEVPFIAFYRKEYVE-----------PELNINDLWRIWQWDEKWTQLRNRKRNMTRL 435
Cdd:pfam14641   28 FERLLEPFKEAVGNVLEFISKDNLEVPFIWQHRRDYLLhsekdgfeighKLLNEDDLWRIVQLDIKFHSLIEKRNNLEKL 107

                   ....*.
gi 1889952546  436 FEKMQT 441
Cdd:pfam14641  108 YEKLGI 113
YqgFc smart00732
Likely ribonuclease with RNase H fold; YqgF proteins are likely to function as an alternative ...
814-925 5.88e-12

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: 63.74  E-value: 5.88e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546   814 RVMGLAYSsdwDTASFAAVIDGEGDVVDFLRLAHlmkrrnayreadRENKLSDMESIKNLILNKKPHVIVIGAENRDAQS 893
Cdd:smart00732    2 RVLGLDPG---RKGIGVAVVDETGKLADPLEVIP------------RTNKEADAARLKKLIKKYQPDLIVIGLPLNMNGT 66
                            90       100       110
                    ....*....|....*....|....*....|..
gi 1889952546   894 VIDDVKLCVKELEEEeqLAPIAVELLDNELSR 925
Cdd:smart00732   67 ASRETEEAFAELLKE--RFNLPVVLVDERLAT 96
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
1262-1316 6.64e-12

S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 62.69  E-value: 6.64e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSC 1316
Cdd:pfam00575   18 GAFVDLGNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
1262-1317 1.00e-10

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 59.15  E-value: 1.00e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889952546  1262 GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCR 1317
Cdd:smart00316   17 GAFVDLGNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
1259-1315 2.43e-09

S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of RNA-associated proteins. Originally identified in S1 ribosomal protein. This superfamily also contains the Cold Shock Domain (CSD), which is a homolog of the S1 domain. Both domains are members of the Oligonucleotide/oligosaccharide Binding (OB) fold.


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 55.08  E-value: 2.43e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1889952546 1259 QATGAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:cd00164      9 TKFGVFVELEDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
rpsA PRK07899
30S ribosomal protein S1; Reviewed
1248-1333 4.97e-08

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 57.75  E-value: 4.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1248 WNHFDSSECPGQAT----------GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLScr 1317
Cdd:PRK07899   284 WQQFARTHAIGQIVpgkvtklvpfGAFVRVEEGIEGLVHISELAERHVEVPEQVVQVGDEVFVKVIDIDLERRRISLS-- 361
                           90
                   ....*....|....*.
gi 1889952546 1318 ssdLADTNGDYRPARD 1333
Cdd:PRK07899   362 ---LKQANEGVTPESE 374
HHH_9 pfam17674
HHH domain;
1086-1177 1.62e-07

HHH domain;


Pssm-ID: 465451 [Multi-domain]  Cd Length: 70  Bit Score: 49.84  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1086 LDGSRVHPETYDWARKMAVDAleydesaedanpAAALEEILETPERLKDLDLDAFAEElerqGFGnkSITLYDIRAElns 1165
Cdd:pfam17674    3 LDNTAIHPESYPLAEKILKDL------------GLDLKDLIGNSALLKKLDPKKLAEE----EVG--LPTLKDILEE--- 61
                           90
                   ....*....|..
gi 1889952546 1166 mykdLRTPFRSP 1177
Cdd:pfam17674   62 ----LAKPGRDP 69
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
1262-1315 9.06e-05

Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 46.96  E-value: 9.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMIS-DKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:COG0539    289 GAFVELEPGVEGLVHISEMSwTKRVAHPSDVVKVGDEVEVKVLDIDPEERRISLS 343
SPT6_acidic pfam14632
Acidic N-terminal SPT6; The N-terminus of SPT6 is highly acidic. The full SPT6 protein is a ...
84-140 1.77e-04

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: 42.08  E-value: 1.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889952546   84 EASAGEDSEGEIGGKK--RRRRSSIDDRLEDEDYDLIEENLGVKVKR--KRFRRVQALSDD 140
Cdd:pfam14632   29 EEEEEEDDEERRRRKKkrKRREEEEDDRLDEDDLDLIEENTGVKRRRssSKFKRLKRGHDD 89
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
1270-1317 4.77e-04

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 44.72  E-value: 4.77e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1889952546 1270 GVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCR 1317
Cdd:TIGR00717  209 GVDGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFDKEKGRISLSLK 256
PHA03247 PHA03247
large tegument protein UL36; Provisional
1552-1805 5.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1552 DPIPGATPVNVRhrTPMAPSRPENTPAPSGinlqgvdPAQLSQLQKAISNFPSNLSTQQVFSALAAATGQGSSATPAqwg 1631
Cdd:PHA03247  2738 APAPPAVPAGPA--TPGGPARPARPPTTAG-------PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA--- 2805
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1632 sqgygqsqgqyhagagysgaagsSSYQTFATPNPMATPMMTPAYPSATPAQGQPQTTPRYQPTPQSSWGHGhGRAAASAS 1711
Cdd:PHA03247  2806 -----------------------DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG-GSVAPGGD 2861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1712 TSGATPSRAAPTprasTSAASAGTDWGKAALAWVQQQRNK--QRGGDTPKVRTPGHHTPGHHTPSHHTPSHRTPSHRTPT 1789
Cdd:PHA03247  2862 VRRRPPSRSPAA----KPAAPARPPVRRLARPAVSRSTESfaLPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937
                          250
                   ....*....|....*.
gi 1889952546 1790 HRAPTMSPSPMVEGTP 1805
Cdd:PHA03247  2938 RPQPPLAPTTDPAGAG 2953
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
1618-1741 2.80e-03

Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD domain carries a regular nonapeptide repeat that can be present in up to 18 copies, as in S. pombe. The repeat has a characteristic TPA motif.


Pssm-ID: 215026 [Multi-domain]  Cd Length: 121  Bit Score: 39.43  E-value: 2.80e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  1618 ATGQGSSATPAqWGSQG-----YGQSQGQYHAGAgysgaagsssyqtfATPNPMATPMMTPA------YPSATPAQGQPQ 1686
Cdd:smart01104    6 AWGASGSKTPA-WGSRTpgtaaGGAPTARGGSGS--------------RTPAWGGAGSRTPAwggagpTGSRTPAWGGAS 70
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1889952546  1687 TTPRY-QPTPQSSWGHGHGraaasastsgatPSRAAPTP--RASTSAASAGTDWGKAA 1741
Cdd:smart01104   71 AWGNKsSEGSASSWAAGPG------------GAYGAPTPgyGGTPSAYGPATPGGGAM 116
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
1659-1811 3.05e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 41.96  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1659 TFATPNPMATPMMTPAYPSatpaqgqpQTTPRYQPTPQ----SSWGHGHGRAAASASTSGATPSRAAP--TPRASTSAAS 1732
Cdd:pfam05539  173 TTSKTTSWPTEVSHPTYPS--------QVTPQSQPATQghqtATANQRLSSTEPVGTQGTTTSSNPEPqtEPPPSQRGPS 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1733 AGTdwgKAALAWVQQQRNKQRGGD--TPKVRTPGHHTPGHHTPSHHTPSHRTPSHRT--PTHRaPT----MSPSPMVEGT 1804
Cdd:pfam05539  245 GSP---QHPPSTTSQDQSTTGDGQehTQRRKTPPATSNRRSPHSTATPPPTTKRQETgrPTPR-PTattqSGSSPPHSSP 320

                   ....*..
gi 1889952546 1805 PMIESTP 1811
Cdd:pfam05539  321 PGVQANP 327
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1618-1820 5.45e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.55  E-value: 5.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1618 ATGQGSSATPAQWGSQGYGQSQGQyhagagysgaaGSSSYQTFATPNPMATPMMTPA--YPSATPAQGQPQTTPRYQPTP 1695
Cdd:COG5164     21 AGSQGSTKPAQNQGSTRPAGNTGG-----------TRPAQNQGSTTPAGNTGGTRPAgnQGATGPAQNQGGTTPAQNQGG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1696 QSSWGHGHGraaasastSGATPSRAAPTPRASTSAASAGTDWGKAALAWVQQQRNKQRGGDTPKvrTPGHHTPGHHTPSH 1775
Cdd:COG5164     90 TRPAGNTGG--------TTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPP--GPGSTGPGGSTTPP 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1889952546 1776 HTPSHRTPSHRTPTHRAP----TMSPSPMVEGTPMIESTPISAMGDATP 1820
Cdd:COG5164    160 GDGGSTTPPGPGGSTTPPddggSTTPPNKGETGTDIPTGGTPRQGPDGP 208
 
Name Accession Description Interval E-value
SH2_2 pfam14633
SH2 domain;
1344-1548 4.27e-109

SH2 domain;


Pssm-ID: 464227 [Multi-domain]  Cd Length: 206  Bit Score: 345.67  E-value: 4.27e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1344 DRKADDEAKKKQARTTYVKRVIVHPCFHNISYKQAVKLMESQDQGDVIVRPSSKGPDHLTVTWKVDDGIYQHIDVREEGK 1423
Cdd:pfam14633    3 DKEELKKKKKAKARKTYVKRVIKHPLFHNFNYAQAEEYLASQDRGDVVIRPSSKGPDHLTVTWKVADGVYQHIDVLELDK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1424 ENAFSLGQSLWINNEEFEDLDEIIARHIQPMASFVRDLTNHKYYQAaegGKREAIEKIIRDEKKKAPSKIPYIISASKEY 1503
Cdd:pfam14633   83 ENEFSLGKTLRIGGEEYEDLDELIARHVQPMARKVEEMMNHRKFKD---GTKEEVEEWLREEKKANPKRSPYAFCLSHKH 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1889952546 1504 PGKFLLSYQPKTSPR--HEFVTVTPDGFRFRQLIHHSVNALFRWFKE 1548
Cdd:pfam14633  160 PGYFLLSFKANKNSRvhHWYVKVTPDGFRLRGQQFPDVDALCNGFKK 206
YqgF pfam14639
Holliday-junction resolvase-like of SPT6; The YqgF domain of SPT6 proteins is homologous to ...
811-965 5.08e-49

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: 171.59  E-value: 5.08e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  811 KGLRVMGLAYSS-DWDTASFAAVIDGEGDVVDFLRLAhlmkrrnaYREADRENKLSDMESIKNLILNKKPHVIVIGAENR 889
Cdd:pfam14639    3 KIPRVLGVAFGSgRFDDAIICVLVNGEGEVTDFLKLA--------WREFDRENKAQFEETLKKFLLSKKPHVIGVSGENR 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889952546  890 DAQSVIDDVKLCVKELEEEEQLAPIAVELLDNELSRFIMNSPRAEAEHRDYPPLLRQALSLARRMQDPLIEFSQLC 965
Cdd:pfam14639   75 DAQKFYEDVQRVLHELEQDSRLHTIGVILVDDEVAILYQNSKRAEAEFPDYPPLLRYCVALARYIQDPLLEYAQVC 150
HHH_7 pfam14635
Helix-hairpin-helix motif;
969-1072 8.84e-45

Helix-hairpin-helix motif;


Pssm-ID: 291309  Cd Length: 104  Bit Score: 157.32  E-value: 8.84e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  969 DDLLCLRFHTLQEQVSREDLLHALELEFINRVNEVGVDINRCVANNHTTTLAQFVCGLGPRKAAYILKVLKQNNARLENR 1048
Cdd:pfam14635    1 EDILSLSFHPLQELLPKEELLKALETAFVDIVNLVGVDVNEAIANKYEAAILPYIAGLGPRKADHLLKILAANNGRLDNR 80
                           90       100
                   ....*....|....*....|....
gi 1889952546 1049 NQLVMMCHMGPKVFMNCAGFIKID 1072
Cdd:pfam14635   81 SQLITKCIMGPKVFMNCAGFLIID 104
SH2_Nterm_SPT6_like cd09918
N-terminal Src homology 2 (SH2) domain found in Spt6; N-terminal SH2 domain in Spt6. Spt6 is ...
1367-1450 1.17e-44

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: 156.24  E-value: 1.17e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1367 HPCFHNISYKQAVKLMESQDQGDVIVRPSSKGPDHLTVTWKVDDGIYQHIDVREEGKENAFSLGQSLWINNEEFEDLDEI 1446
Cdd:cd09918      2 HPLFKNVNYKQAEAYLKSKDVGEVVIRPSSKGVDHLTVTWKVADGVYQHIDIEELNKENPFSLGKELIIGGEEYEDLDEI 81

                   ....
gi 1889952546 1447 IARH 1450
Cdd:cd09918     82 IARF 85
SH2_Cterm_SPT6_like cd09928
C-terminal Src homology 2 (SH2) domain found in Spt6; Spt6 is an essential transcription ...
1459-1550 9.31e-36

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: 131.19  E-value: 9.31e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1459 RDLTNHKYYQaaegGKREAIEKIIRDEKKKAPSKIPYIISASKEYPGKFLLSYQPK-TSPRHEFVTVTPDGFRFRQLIHH 1537
Cdd:cd09928      1 EMLNHHKYFR----GTKEEVEKLLKEEKKANPKRIPYAFCVSKKYPGKFLLSYLPAnTRVRHEYVKVTPDGFRFRGQVFP 76
                           90
                   ....*....|...
gi 1889952546 1538 SVNALFRWFKEHF 1550
Cdd:cd09928     77 SVDSLLNWFKEHF 89
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
599-1163 5.47e-31

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 132.07  E-value: 5.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  599 DQYPAEPNDLSKEFVNS--QFPSEEKVLQGARHMVAMQLSREPLVRQCVRQTYFERAKVSTKPTKKGRKEID--EMHYGY 674
Cdd:COG2183    131 AQPTGDPEAEAAKYINEekGVADVEAALDGARDILAERISEDAELRGKLRELLWKEGVLVSKVKKGKEEEGAkfRDYFDY 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  675 tfkylkNKPVKDLTGDQFLKMSIAEDEGLLKTHVSIDGETTQSYfeeIKQLYYRDEFShlvqEWNTQRTMVLERMLKFIL 754
Cdd:COG2183    211 ------SEPLKKIPSHRILALNRGEKEGVLKVKLEPDEEEAEAY---IARRFIKDQGR----PADEWLKEAVRDAYKRLL 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  755 YPQMEKELRSKLVQESKDGIIKSCCRKLYNWLKVAPYqpeqqieeedeyiegmgssKGLRVMGLayssdwD----TASFA 830
Cdd:COG2183    278 APSLERELRNELKEKAEEEAIKVFAENLRDLLLAAPA-------------------GGKVVLGL------DpgfrTGCKV 332
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  831 AVIDGEGDVVD----FLrlaHlmKRRNAYREAdrenklsdMESIKNLILNKKPHVIVIGaeN----Rdaqsviddvklcv 902
Cdd:COG2183    333 AVVDETGKLLDtatiYP---H--PPQNKWEEA--------AKTLAALIKKYKVELIAIG--NgtasR------------- 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  903 keleEEEQLAPIAVELLDNELSRFIMN---------SPRAEAEHRDYPPLLRQALSLARRMQDPLIEfsqlcvnnddllc 973
Cdd:COG2183    385 ----ETEQFVAELIKELDLKVQYVIVSeagasvysaSELAREEFPDLDVTVRGAVSIARRLQDPLAE------------- 447
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  974 lrfhtL-----------QEQ--VSREDLLHALELEFINRVNEVGVDINrcvannhtT---TLAQFVCGLGPRKAAYILKV 1037
Cdd:COG2183    448 -----LvkidpksigvgQYQhdVNQKKLKRSLDAVVEDCVNAVGVDLN--------TasaPLLSYVSGLNPTLAKNIVAY 514
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1038 LKQNNArLENRNQLVMMCHMGPKVFMNCAGFIKIDtkslgDSEqyiELLDGSRVHPETYDWARKMavdaleydesAEDAN 1117
Cdd:COG2183    515 RDENGA-FKSRKELLKVPRLGPKAFEQAAGFLRIR-----DGD---NPLDNSAVHPESYPVVEKI----------LKDLG 575
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1889952546 1118 paAALEEILETPERLKDLDLDAFAEELerqgFGnkSITLYDIRAEL 1163
Cdd:COG2183    576 --VSVKDLIGNKELLKKLDPEKYADEL----FG--LPTLRDILKEL 613
HTH_44 pfam14641
Helix-turn-helix DNA-binding domain of SPT6; This helix-turn-helix represents the first of two ...
367-441 4.24e-25

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: 101.49  E-value: 4.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  367 YSRKEPSTVGKIRDALNFIRNQHFEVPFIAFYRKEYVE-----------PELNINDLWRIWQWDEKWTQLRNRKRNMTRL 435
Cdd:pfam14641   28 FERLLEPFKEAVGNVLEFISKDNLEVPFIWQHRRDYLLhsekdgfeighKLLNEDDLWRIVQLDIKFHSLIEKRNNLEKL 107

                   ....*.
gi 1889952546  436 FEKMQT 441
Cdd:pfam14641  108 YEKLGI 113
YqgFc smart00732
Likely ribonuclease with RNase H fold; YqgF proteins are likely to function as an alternative ...
814-925 5.88e-12

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: 63.74  E-value: 5.88e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546   814 RVMGLAYSsdwDTASFAAVIDGEGDVVDFLRLAHlmkrrnayreadRENKLSDMESIKNLILNKKPHVIVIGAENRDAQS 893
Cdd:smart00732    2 RVLGLDPG---RKGIGVAVVDETGKLADPLEVIP------------RTNKEADAARLKKLIKKYQPDLIVIGLPLNMNGT 66
                            90       100       110
                    ....*....|....*....|....*....|..
gi 1889952546   894 VIDDVKLCVKELEEEeqLAPIAVELLDNELSR 925
Cdd:smart00732   67 ASRETEEAFAELLKE--RFNLPVVLVDERLAT 96
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
1262-1316 6.64e-12

S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 62.69  E-value: 6.64e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSC 1316
Cdd:pfam00575   18 GAFVDLGNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
1262-1317 1.00e-10

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 59.15  E-value: 1.00e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889952546  1262 GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCR 1317
Cdd:smart00316   17 GAFVDLGNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
1259-1315 2.43e-09

S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of RNA-associated proteins. Originally identified in S1 ribosomal protein. This superfamily also contains the Cold Shock Domain (CSD), which is a homolog of the S1 domain. Both domains are members of the Oligonucleotide/oligosaccharide Binding (OB) fold.


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 55.08  E-value: 2.43e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1889952546 1259 QATGAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:cd00164      9 TKFGVFVELEDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
1368-1450 3.12e-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: 55.15  E-value: 3.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1368 PCFH-NISYKQAVKLMESQDQGDVIVRPSSKGPDHLTVTWKVDDGIYQHIDVREEGKENAFSLGQSLWinneeFEDLDEI 1446
Cdd:cd00173      1 PWFHgSISREEAERLLRGKPDGTFLVRESSSEPGDYVLSVRSGDGKVKHYLIERNEGGYYLLGGSGRT-----FPSLPEL 75

                   ....
gi 1889952546 1447 IARH 1450
Cdd:cd00173     76 VEHY 79
rpsA PRK07899
30S ribosomal protein S1; Reviewed
1248-1333 4.97e-08

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 57.75  E-value: 4.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1248 WNHFDSSECPGQAT----------GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLScr 1317
Cdd:PRK07899   284 WQQFARTHAIGQIVpgkvtklvpfGAFVRVEEGIEGLVHISELAERHVEVPEQVVQVGDEVFVKVIDIDLERRRISLS-- 361
                           90
                   ....*....|....*.
gi 1889952546 1318 ssdLADTNGDYRPARD 1333
Cdd:PRK07899   362 ---LKQANEGVTPESE 374
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
1002-1069 7.10e-08

Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 50.94  E-value: 7.10e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889952546 1002 EVGVDINRCvannhTTTLAQFVCGLGPRKAAYILKvLKQNNARLENRNQLVMMCHMGPKVFMNCAGFI 1069
Cdd:pfam12836    1 AVGVDINTA-----SAELLSRVPGLGPKLAKNIVE-YREENGPFRSREDLLKVKGLGPKTFEQLAGFL 62
HHH_9 pfam17674
HHH domain;
1086-1177 1.62e-07

HHH domain;


Pssm-ID: 465451 [Multi-domain]  Cd Length: 70  Bit Score: 49.84  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1086 LDGSRVHPETYDWARKMAVDAleydesaedanpAAALEEILETPERLKDLDLDAFAEElerqGFGnkSITLYDIRAElns 1165
Cdd:pfam17674    3 LDNTAIHPESYPLAEKILKDL------------GLDLKDLIGNSALLKKLDPKKLAEE----EVG--LPTLKDILEE--- 61
                           90
                   ....*....|..
gi 1889952546 1166 mykdLRTPFRSP 1177
Cdd:pfam17674   62 ----LAKPGRDP 69
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
1261-1315 1.41e-05

S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has been characterized in Bordetella pertussis and Pseudomonas aeruginosa. The tex gene is essential in Bortella pertusis and is named for its role in toxin expression. Tex has two functional domains, an N-terminal domain homologous to the Escherichia coli maltose repression protein, which is a poorly defined transcriptional factor, and a C-terminal S1 RNA-binding domain. Tex is found in prokaryotes, eukaryotes, and archaea.


Pssm-ID: 240190 [Multi-domain]  Cd Length: 68  Bit Score: 44.53  E-value: 1.41e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889952546 1261 TGAVTR-------LDNGV--SGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:cd05685      5 EGVVTNvtdfgafVDIGVkqDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISLS 68
rpsA PRK06676
30S ribosomal protein S1; Reviewed
1261-1315 2.00e-05

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 49.10  E-value: 2.00e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889952546 1261 TGAVTRLDN--------GVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:PRK06676   197 EGTVARLTDfgafvdigGVDGLVHISELSHERVEKPSEVVSVGQEVEVKVLSIDWETERISLS 259
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
1262-1315 2.12e-05

S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 4 (hs4) of the H. sapiens RPS1 homolog. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 44.20  E-value: 2.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDiERFRVDLS 1315
Cdd:cd05692     15 GAFVELGGGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSID-ARGRISLS 67
SH2 pfam00017
SH2 domain;
1370-1447 3.48e-05

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 43.74  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1370 FH-NISYKQAVK-LMESQDQGDVIVRPSSKGPDHLTVTWKVDDGIyQHIDVREEGKENAFSLGqslwinNEEFEDLDEII 1447
Cdd:pfam00017    2 YHgKISRQEAERlLLNGKPDGTFLVRESESTPGGYTLSVRDDGKV-KHYKIQSTDNGGYYISG------GVKFSSLAELV 74
rpsA PRK06299
30S ribosomal protein S1; Reviewed
1262-1323 4.33e-05

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 48.24  E-value: 4.33e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCRSSDLAD 1323
Cdd:PRK06299   475 GAFVELEDGVEGLIRASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAE 536
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
1262-1317 4.70e-05

bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 48.40  E-value: 4.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCR 1317
Cdd:PRK00087   577 GAFVELEPGVDGLVHISQISWKRIDKPEDVLSEGEEVKAKILEVDPEEKRIRLSIK 632
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
1262-1315 9.06e-05

Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 46.96  E-value: 9.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMIS-DKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:COG0539    289 GAFVELEPGVEGLVHISEMSwTKRVAHPSDVVKVGDEVEVKVLDIDPEERRISLS 343
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
1262-1317 1.01e-04

S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 6 (hs6) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 42.21  E-value: 1.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCR 1317
Cdd:cd05698     15 GCIVSFYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
1270-1315 1.13e-04

S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 3 (ec3) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240193 [Multi-domain]  Cd Length: 68  Bit Score: 41.85  E-value: 1.13e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1889952546 1270 GVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:cd05688     23 GVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
1261-1315 1.18e-04

Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 46.58  E-value: 1.18e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889952546 1261 TGAVTRLDN--------GVSGFIPtkmISD---KHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:COG0539    194 EGTVKNITDfgafvdlgGVDGLLH---ISEiswGRVKHPSEVLKVGDEVEVKVLKIDREKERISLS 256
SPT6_acidic pfam14632
Acidic N-terminal SPT6; The N-terminus of SPT6 is highly acidic. The full SPT6 protein is a ...
84-140 1.77e-04

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: 42.08  E-value: 1.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889952546   84 EASAGEDSEGEIGGKK--RRRRSSIDDRLEDEDYDLIEENLGVKVKR--KRFRRVQALSDD 140
Cdd:pfam14632   29 EEEEEEDDEERRRRKKkrKRREEEEDDRLDEDDLDLIEENTGVKRRRssSKFKRLKRGHDD 89
rpsA PRK06676
30S ribosomal protein S1; Reviewed
1262-1343 2.19e-04

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 45.64  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCRSSDLADTNGDYRPARDLYYDHETE 1341
Cdd:PRK06676   292 GAFVEVLPGVEGLVHISQISHKHIATPSEVLEEGQEVKVKVLEVNEEEKRISLSIKALEEAPAEEEDRREEYRQYELPEE 371

                   ..
gi 1889952546 1342 ET 1343
Cdd:PRK06676   372 ET 373
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
1270-1317 4.77e-04

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 44.72  E-value: 4.77e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1889952546 1270 GVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCR 1317
Cdd:TIGR00717  209 GVDGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFDKEKGRISLSLK 256
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
1259-1314 5.03e-04

S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 5 (hs5) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 40.30  E-value: 5.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889952546 1259 QATGAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDL 1314
Cdd:cd05697     12 RPSGIFVKLSDHIKGLVPPMHLADVRLKHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
PHA03247 PHA03247
large tegument protein UL36; Provisional
1552-1805 5.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1552 DPIPGATPVNVRhrTPMAPSRPENTPAPSGinlqgvdPAQLSQLQKAISNFPSNLSTQQVFSALAAATGQGSSATPAqwg 1631
Cdd:PHA03247  2738 APAPPAVPAGPA--TPGGPARPARPPTTAG-------PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA--- 2805
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1632 sqgygqsqgqyhagagysgaagsSSYQTFATPNPMATPMMTPAYPSATPAQGQPQTTPRYQPTPQSSWGHGhGRAAASAS 1711
Cdd:PHA03247  2806 -----------------------DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG-GSVAPGGD 2861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1712 TSGATPSRAAPTprasTSAASAGTDWGKAALAWVQQQRNK--QRGGDTPKVRTPGHHTPGHHTPSHHTPSHRTPSHRTPT 1789
Cdd:PHA03247  2862 VRRRPPSRSPAA----KPAAPARPPVRRLARPAVSRSTESfaLPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937
                          250
                   ....*....|....*.
gi 1889952546 1790 HRAPTMSPSPMVEGTP 1805
Cdd:PHA03247  2938 RPQPPLAPTTDPAGAG 2953
Tex_N pfam09371
Tex-like protein N-terminal domain; This presumed domain is found at the N-terminus of Swiss: ...
605-658 8.10e-04

Tex-like protein N-terminal domain; This presumed domain is found at the N-terminus of Swiss:Q45388. This protein defines a novel family of prokaryotic transcriptional accessory factors.


Pssm-ID: 462777  Cd Length: 183  Bit Score: 42.39  E-value: 8.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1889952546  605 PNDLSKEFVNS--QFPSEEKVLQGARHMVAMQLSREPLVRQCVRQTYFERAKVSTK 658
Cdd:pfam09371  127 PEEEAAKYINPekGVADVEEALAGARDIIAERISEDAELRKKLRELLWREGVIVSK 182
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
1262-1315 8.76e-04

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 43.95  E-value: 8.76e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMIS-DKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:TIGR00717  287 GVFVEIEEGIEGLVHVSEMSwVKKNSHPSKVVKKGDEVEVMILDIDPERRRLSLG 341
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
1269-1317 1.39e-03

S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain.While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 2 of the Escherichia coli and Homo sapiens RPS1 (ec2 and hs2, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 239911 [Multi-domain]  Cd Length: 67  Bit Score: 38.98  E-value: 1.39e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1889952546 1269 NGVSGFIPTKMISDKHVKSPEERVKPGMEVytRIIKIDIERFRVDLSCR 1317
Cdd:cd04465     21 EGVRAFLPASQVDLRPVEDLDEYVGKELKF--KIIEIDRERNNIVLSRR 67
rpsA PRK06299
30S ribosomal protein S1; Reviewed
1262-1315 1.57e-03

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 43.23  E-value: 1.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMIS-DKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:PRK06299   301 GAFVELEEGIEGLVHVSEMSwTKKNKHPSKVVSVGQEVEVMVLEIDEEKRRISLG 355
PHA03247 PHA03247
large tegument protein UL36; Provisional
1551-1806 1.71e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1551 RDPIPGATPVNVRHRTPMAPSRPENTPAPSGINLQGVDPAQLSQLQKAISN-FPSNLSTQQVFSALAAATgqGSSATPAQ 1629
Cdd:PHA03247  2605 RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDpAPGRVSRPRRARRLGRAA--QASSPPQR 2682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1630 WGSQGYGQSQGQYHAGAGYSGAAGSSSYQTFATPNPMATPMMTPAYPSATPAqgqPQTTPRYQPTPQSSWGHGHGRAAAS 1709
Cdd:PHA03247  2683 PRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPA---LPAAPAPPAVPAGPATPGGPARPAR 2759
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1710 ASTSGATPSRAAPTPRASTSAASAGTDWGKAALAWVQQQRNKQRGGDTPKVRTPghhtPGHHTPSHHTPSHRTPSHRTPT 1789
Cdd:PHA03247  2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLA----PAAALPPAASPAGPLPPPTSAQ 2835
                          250
                   ....*....|....*..
gi 1889952546 1790 HRAPTMSPSPMVEGTPM 1806
Cdd:PHA03247  2836 PTAPPPPPGPPPPSLPL 2852
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
1618-1741 2.80e-03

Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD domain carries a regular nonapeptide repeat that can be present in up to 18 copies, as in S. pombe. The repeat has a characteristic TPA motif.


Pssm-ID: 215026 [Multi-domain]  Cd Length: 121  Bit Score: 39.43  E-value: 2.80e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  1618 ATGQGSSATPAqWGSQG-----YGQSQGQYHAGAgysgaagsssyqtfATPNPMATPMMTPA------YPSATPAQGQPQ 1686
Cdd:smart01104    6 AWGASGSKTPA-WGSRTpgtaaGGAPTARGGSGS--------------RTPAWGGAGSRTPAwggagpTGSRTPAWGGAS 70
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1889952546  1687 TTPRY-QPTPQSSWGHGHGraaasastsgatPSRAAPTP--RASTSAASAGTDWGKAA 1741
Cdd:smart01104   71 AWGNKsSEGSASSWAAGPG------------GAYGAPTPgyGGTPSAYGPATPGGGAM 116
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
1659-1811 3.05e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 41.96  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1659 TFATPNPMATPMMTPAYPSatpaqgqpQTTPRYQPTPQ----SSWGHGHGRAAASASTSGATPSRAAP--TPRASTSAAS 1732
Cdd:pfam05539  173 TTSKTTSWPTEVSHPTYPS--------QVTPQSQPATQghqtATANQRLSSTEPVGTQGTTTSSNPEPqtEPPPSQRGPS 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1733 AGTdwgKAALAWVQQQRNKQRGGD--TPKVRTPGHHTPGHHTPSHHTPSHRTPSHRT--PTHRaPT----MSPSPMVEGT 1804
Cdd:pfam05539  245 GSP---QHPPSTTSQDQSTTGDGQehTQRRKTPPATSNRRSPHSTATPPPTTKRQETgrPTPR-PTattqSGSSPPHSSP 320

                   ....*..
gi 1889952546 1805 PMIESTP 1811
Cdd:pfam05539  321 PGVQANP 327
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
1262-1315 4.97e-03

bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 41.86  E-value: 4.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889952546 1262 GAVTRLD--------NGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLS 1315
Cdd:PRK00087   483 GEVKRLTdfgafvdiGGVDGLLHVSEISWGRVEKPSDVLKVGDEIKVYILDIDKENKKLSLS 544
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
1262-1314 5.06e-03

S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 5 (ec5) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 37.47  E-value: 5.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1889952546 1262 GAVTRLDNGVSGFIPTKMIS-DKHVKSPEERVKPGMEVYTRIIKIDIERFRVDL 1314
Cdd:cd05690     15 GIFVGLDGGIDGLVHISDISwTQRVRHPSEIYKKGQEVEAVVLNIDVERERISL 68
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1618-1820 5.45e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.55  E-value: 5.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1618 ATGQGSSATPAQWGSQGYGQSQGQyhagagysgaaGSSSYQTFATPNPMATPMMTPA--YPSATPAQGQPQTTPRYQPTP 1695
Cdd:COG5164     21 AGSQGSTKPAQNQGSTRPAGNTGG-----------TRPAQNQGSTTPAGNTGGTRPAgnQGATGPAQNQGGTTPAQNQGG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1696 QSSWGHGHGraaasastSGATPSRAAPTPRASTSAASAGTDWGKAALAWVQQQRNKQRGGDTPKvrTPGHHTPGHHTPSH 1775
Cdd:COG5164     90 TRPAGNTGG--------TTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPP--GPGSTGPGGSTTPP 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1889952546 1776 HTPSHRTPSHRTPTHRAP----TMSPSPMVEGTPMIESTPISAMGDATP 1820
Cdd:COG5164    160 GDGGSTTPPGPGGSTTPPddggSTTPPNKGETGTDIPTGGTPRQGPDGP 208
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
1662-1798 6.53e-03

Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD domain carries a regular nonapeptide repeat that can be present in up to 18 copies, as in S. pombe. The repeat has a characteristic TPA motif.


Pssm-ID: 215026 [Multi-domain]  Cd Length: 121  Bit Score: 38.66  E-value: 6.53e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  1662 TPNPMATPMMTPAYPSATPAQ--GQPQTTPRYQPTPQSSWGHGHGRaaasastsgaTPSRAAPTPRASTSAASAGTDWGK 1739
Cdd:smart01104    4 TPAWGASGSKTPAWGSRTPGTaaGGAPTARGGSGSRTPAWGGAGSR----------TPAWGGAGPTGSRTPAWGGASAWG 73
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546  1740 AALAWvqqqrnkqrGGDTPKVRTPGhHTPGHHTPSH-HTPSHRTPShrTPTHRAPTMSPS 1798
Cdd:smart01104   74 NKSSE---------GSASSWAAGPG-GAYGAPTPGYgGTPSAYGPA--TPGGGAMAGSAS 121
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
1262-1317 6.65e-03

S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Eukaryotic and archaeal Initiation Factor 2 (e- and aIF2, respectively) are heterotrimeric proteins with three subunits (alpha, beta, and gamma). IF2 plays a crucial role in the process of translation initiation. The IF2 gamma subunit contains a GTP-binding site. The IF2 beta and gamma subunits together are thought to be responsible for binding methionyl-initiator tRNA. The ternary complex consisting of IF2, GTP, and the methionyl-initiator tRNA binds to the small subunit of the ribosome, as part of a pre-initiation complex that scans the mRNA to find the AUG start codon. The IF2-bound GTP is hydrolyzed to GDP when the methionyl-initiator tRNA binds the AUG start codon, at which time the IF2 is released with its bound GDP. The large ribosomal subunit then joins with the small subunit to complete the initiation complex, which is competent to begin translation. The IF2a subunit is a major site of control of the translation initiation process, via phosphorylation of a specific serine residue. This alpha subunit is well conserved in eukaryotes and archaea but is not present in bacteria. IF2 is a cold-shock-inducible protein.


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 37.18  E-value: 6.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1889952546 1262 GAVTRLD--NGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCR 1317
Cdd:cd04452     18 GAYVSLLeyGNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKK 75
PHA03378 PHA03378
EBNA-3B; Provisional
1553-1811 6.80e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 6.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1553 PIPGATPVNVRHRTPMAPSRPENT-PAPSGINLQGVDPAQLSQLQKAISNFPSNLSTQQVFSALAAATGQGSSATPAQWG 1631
Cdd:PHA03378   565 PAPGLGPLQIQPLTSPTTSQLASSaPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFN 644
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1632 SQGYGQSQGQYHAGAGYSGAAGSSSYQTFATPNPMATPMMTPayPSATPAQGQPqttPRYQPTPQSSWGHGHGRAAasas 1711
Cdd:PHA03378   645 VLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLP--IQWAPGTMQP---PPRAPTPMRPPAAPPGRAQ---- 715
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1712 tsgatPSRAAPTPrASTSAASAGTDWGKAALAWVQQQRNKQRGGDTPKVRTPGHHTPGHHTPSHHTPSHRTPSHRTPTHR 1791
Cdd:PHA03378   716 -----RPAAATGR-ARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQR 789
                          250       260
                   ....*....|....*....|...
gi 1889952546 1792 ---APTMSPSPMVEGTPMIESTP 1811
Cdd:PHA03378   790 prgAPTPQPPPQAGPTSMQLMPR 812
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
1259-1320 7.58e-03

S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 6 (ec6) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 36.86  E-value: 7.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889952546 1259 QATGAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCRSSD 1320
Cdd:cd05691     12 DAKGATVKLGDGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAKE 73
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
1557-1820 7.71e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 41.10  E-value: 7.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1557 ATPVNVRHRTPMAPSRPEN--TPAPSGinlQGVDPAQLSQLQKAISNFPSNLStQQVFSALAAATGQGSSATPAQWGSQG 1634
Cdd:pfam17823   78 AAHLNSTEVTAEHTPHGTDlsEPATRE---GAADGAASRALAAAASSSPSSAA-QSLPAAIAALPSEAFSAPRAAACRAN 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1635 YGQSqgqyhagagYSGAAGSSSYQTFATPNPMATPMMTPAYPSATPAQGQPQT---------TPrYQPTPQSSWGHGHgr 1705
Cdd:pfam17823  154 ASAA---------PRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTaassapatlTP-ARGISTAATATGH-- 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1706 aAASASTSGATPSrAAPTPRASTSAASAGTDWGKAALAWVQQQRNKQRGgdTPKVRTPGHHTPghhTPSHHTPSHRTPSH 1785
Cdd:pfam17823  222 -PAAGTALAAVGN-SSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAG--TINMGDPHARRL---SPAKHMPSDTMARN 294
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1889952546 1786 RTPTHRAPTMSPS-------PMVEGTPmiESTPISAMGDATP 1820
Cdd:pfam17823  295 PAAPMGAQAQGPIiqvstdqPVHNTAG--EPTPSPSNTTLEP 334
PHA03247 PHA03247
large tegument protein UL36; Provisional
1551-1827 7.71e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 7.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1551 RDPIPGATPvnvRHRTPMAPSRPENTPAPsginLQGVDPAQLSQLQKAISNF---PSNLSTQqvfsalAAATGQGSSATP 1627
Cdd:PHA03247  2654 DDPAPGRVS---RPRRARRLGRAAQASSP----PQRPRRRAARPTVGSLTSLadpPPPPPTP------EPAPHALVSATP 2720
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1628 AQWGSQGYGQSQGQyhAGAGYSGAAGSSSYQTFATPNPMATPMMTPAYPSATPAQGQPQTTPRYQPTPQSSwghghgrAA 1707
Cdd:PHA03247  2721 LPPGPAAARQASPA--LPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA-------SL 2791
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1708 ASASTSGATPSRAAPTPRASTSAASAGTDWGKAA------LAWVQQQRNKQRGGDTPKVRTPGHHTPG----HHTPSHHT 1777
Cdd:PHA03247  2792 SESRESLPSPWDPADPPAAVLAPAAALPPAASPAgplpppTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvrRRPPSRSP 2871
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1889952546 1778 PSHRTPSHRTPTHR--APTMSPSPMVEGTPMIESTPISAMGDATPLIDEPQE 1827
Cdd:PHA03247  2872 AAKPAAPARPPVRRlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQP 2923
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
1260-1317 8.01e-03

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 40.87  E-value: 8.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1889952546 1260 ATGAVTRLDNGVSGFIPTKMISDKHVKSPEERVKPGMEVYTRIIKIDIERFRVDLSCR 1317
Cdd:TIGR00717  459 DFGAFVELPGGVEGLIRNSELSENRDEDKTDEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1658-1810 8.56e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 8.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1658 QTFATPNPMATPmmTPAYPSATPAQGQP----QTTP--------------RYQPTPQsswghgHGRAAASASTSGATPSR 1719
Cdd:PRK10263   331 QSWAAPVEPVTQ--TPPVASVDVPPAQPtvawQPVPgpqtgepviapapeGYPQQSQ------YAQPAVQYNEPLQQPVQ 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889952546 1720 AAPTPRASTSAASAGTDWGKAALAWVQQQRNKQRGGDTPKVRTPGHHTPgHHTPSHHTPSHRT------PSHRTPTHRAP 1793
Cdd:PRK10263   403 PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEE-QQSTFAPQSTYQTeqtyqqPAAQEPLYQQP 481
                          170
                   ....*....|....*...
gi 1889952546 1794 -TMSPSPMVEGTPMIEST 1810
Cdd:PRK10263   482 qPVEQQPVVEPEPVVEET 499
 
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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