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Conserved domains on  [gi|2201678600|ref|XP_046797001|]
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MAP7 domain-containing protein 3 isoform X17 [Gallus gallus]

Protein Classification

MAP7 domain-containing protein( domain architecture ID 12064852)

MAP7 domain-containing protein such as MAP7D1 (microtubule-associated protein 7 domain containing 1) identified as a novel substrate of doublecortin-like kinase 1 (DCLK1)

Gene Ontology:  GO:0005737

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 441-593 6.92e-28

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


:

Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 109.75  E-value: 6.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 441 KAAAGTTTAEEAAKILAEKRRLAREQREREDQERIQRQEEERIREEEMAKRAVEEKARREEELRKQEEEKRLIYEEQQRQ 520
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201678600 521 AEEERIRREQEEQEKLAELQHQREEAEAKAQEEAERQRLERERIMQQNMQERLERKKRIEEIMKRTRKSDQNE 593
Cdd:pfam05672  81 AEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIMKRTRKSDQAE 153
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 112-168 2.59e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


:

Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 48.11  E-value: 2.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2201678600 112 LEERQRKLKEQKQKDEQRRAAVEEKRKQKIEEEKERHEAALHRTLERSQRLETRQKR 168
Cdd:pfam05672  16 LAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR 72
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 176-470 3.17e-06

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 3.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  176 TPDSESkTEQQTTDEGETGASKRSTSTANLKPTEAAMNKRLSSSAALLNASDRTRRSQVSPLDSSVISRLLAPTQASLAR 255
Cdd:PHA03307   110 GPSSPD-PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  256 SKSAATLSADGQDPSASASSINSPVPAPKVPMRSRSIDRLKSSVSSSDASSPDPAQKSEAEKPSPGSGLRRPSSPSVSAR 335
Cdd:PHA03307   189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  336 RRSPSPANLVKRPPSPSAVRQKTRPPSPgiskqRPPSPTPVSKPAPIQRPPLTP--GVINITKKKTEAESKPKEKSTEGA 413
Cdd:PHA03307   269 IWEASGWNGPSSRPGPASSSSSPRERSP-----SPSPSSPGSGPAPSSPRASSSssSSRESSSSSTSSSSESSRGAAVSP 343

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2201678600  414 GHEHGAPSALDRDAVAANTKTKEESGSKAAAGTTTAEEAAKILAEKRR--LAREQRERE 470
Cdd:PHA03307   344 GPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARaaVAGRARRRD 402
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 441-593 6.92e-28

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 109.75  E-value: 6.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 441 KAAAGTTTAEEAAKILAEKRRLAREQREREDQERIQRQEEERIREEEMAKRAVEEKARREEELRKQEEEKRLIYEEQQRQ 520
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201678600 521 AEEERIRREQEEQEKLAELQHQREEAEAKAQEEAERQRLERERIMQQNMQERLERKKRIEEIMKRTRKSDQNE 593
Cdd:pfam05672  81 AEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIMKRTRKSDQAE 153
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 112-168 2.59e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 48.11  E-value: 2.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2201678600 112 LEERQRKLKEQKQKDEQRRAAVEEKRKQKIEEEKERHEAALHRTLERSQRLETRQKR 168
Cdd:pfam05672  16 LAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR 72
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 176-470 3.17e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 3.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  176 TPDSESkTEQQTTDEGETGASKRSTSTANLKPTEAAMNKRLSSSAALLNASDRTRRSQVSPLDSSVISRLLAPTQASLAR 255
Cdd:PHA03307   110 GPSSPD-PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  256 SKSAATLSADGQDPSASASSINSPVPAPKVPMRSRSIDRLKSSVSSSDASSPDPAQKSEAEKPSPGSGLRRPSSPSVSAR 335
Cdd:PHA03307   189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  336 RRSPSPANLVKRPPSPSAVRQKTRPPSPgiskqRPPSPTPVSKPAPIQRPPLTP--GVINITKKKTEAESKPKEKSTEGA 413
Cdd:PHA03307   269 IWEASGWNGPSSRPGPASSSSSPRERSP-----SPSPSSPGSGPAPSSPRASSSssSSRESSSSSTSSSSESSRGAAVSP 343

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2201678600  414 GHEHGAPSALDRDAVAANTKTKEESGSKAAAGTTTAEEAAKILAEKRR--LAREQRERE 470
Cdd:PHA03307   344 GPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARaaVAGRARRRD 402
PRK12704 PRK12704
phosphodiesterase; Provisional
 90-167 6.72e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  90 NAAKESQILE-KER--KAKLQYEKQLEERQRKLKEQKQKDEQRRAAVeEKRKQKIEEEKERHEAALHRTLERSQRLETRQ 166
Cdd:PRK12704   52 EAIKKEALLEaKEEihKLRNEFEKELRERRNELQKLEKRLLQKEENL-DRKLELLEKREEELEKKEKELEQKQQELEKKE 130


                  .
gi 2201678600 167 K 167
Cdd:PRK12704  131 E 131
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 325-389 4.14e-03

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 39.25  E-value: 4.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201678600 325 RRPSSPSVSArrrSPSPANLVKRPPSPSAvrqktRPPSPGISKQRPPSPTPVSKPAPIQRPPLTP 389
Cdd:cd21577    28 KRSSPPSSSS---SSSSSSSSSSSPSSRA-----SPPSPYSKSSPPSPPQQRPLSPPLSLPPPVA 84
SWIRM-assoc_2 pfam16496
SWIRM-associated domain at the N-terminal; Much of the higher eukaryote SWI/SNF complex ...
 314-369 5.48e-03

SWIRM-associated domain at the N-terminal; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 proteins is of low-complexity and or disordered. However, there are several short regions that are quite highly conserved. This is one of these regions. The function of the individual regions is not known.


Pssm-ID: 465143  Cd Length: 412  Bit Score: 40.02  E-value: 5.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2201678600 314 EAEKPSPGSGLRRPSSPSVSARRRSPSPanlvkrPPSPSAVRQKTRPPSPGISKQR 369
Cdd:pfam16496 272 EDEMSSPDPDRKDKKSSPGKKRKRSPSP------PPTPVGKKKSGRKGSPARRKKR 321
PTZ00121 PTZ00121
MAEBL; Provisional
 92-214 6.47e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 6.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600   92 AKESQILEKERKAKLQYEKQLEERQRKLKEQKQKDEQRRAAvEEKRKQKIEEEKERHEAALHRTLERSQRLETRQKRwsw 171
Cdd:PTZ00121  1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK--- 1386

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2201678600  172 ggsvtpdsesKTEQQTTDEGETGASKRSTSTANLKPTEAAMNK 214
Cdd:PTZ00121  1387 ----------AEEKKKADEAKKKAEEDKKKADELKKAAAAKKK 1419
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 88-167 8.11e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.68  E-value: 8.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  88 KQNAAKESQILEKERKAKLqyEKQLEERQRKLKEQKQKDEQRRAAVEEKR--KQKIEEEKERHEAALHRTLERSQRLETR 165
Cdd:COG0542   427 KEALKKEQDEASFERLAEL--RDELAELEEELEALKARWEAEKELIEEIQelKEELEQRYGKIPELEKELAELEEELAEL 504


                  ..
gi 2201678600 166 QK 167
Cdd:COG0542   505 AP 506
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 441-593 6.92e-28

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 109.75  E-value: 6.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 441 KAAAGTTTAEEAAKILAEKRRLAREQREREDQERIQRQEEERIREEEMAKRAVEEKARREEELRKQEEEKRLIYEEQQRQ 520
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201678600 521 AEEERIRREQEEQEKLAELQHQREEAEAKAQEEAERQRLERERIMQQNMQERLERKKRIEEIMKRTRKSDQNE 593
Cdd:pfam05672  81 AEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIMKRTRKSDQAE 153
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 112-168 2.59e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 48.11  E-value: 2.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2201678600 112 LEERQRKLKEQKQKDEQRRAAVEEKRKQKIEEEKERHEAALHRTLERSQRLETRQKR 168
Cdd:pfam05672  16 LAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR 72
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 176-470 3.17e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 3.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  176 TPDSESkTEQQTTDEGETGASKRSTSTANLKPTEAAMNKRLSSSAALLNASDRTRRSQVSPLDSSVISRLLAPTQASLAR 255
Cdd:PHA03307   110 GPSSPD-PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  256 SKSAATLSADGQDPSASASSINSPVPAPKVPMRSRSIDRLKSSVSSSDASSPDPAQKSEAEKPSPGSGLRRPSSPSVSAR 335
Cdd:PHA03307   189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  336 RRSPSPANLVKRPPSPSAVRQKTRPPSPgiskqRPPSPTPVSKPAPIQRPPLTP--GVINITKKKTEAESKPKEKSTEGA 413
Cdd:PHA03307   269 IWEASGWNGPSSRPGPASSSSSPRERSP-----SPSPSSPGSGPAPSSPRASSSssSSRESSSSSTSSSSESSRGAAVSP 343

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2201678600  414 GHEHGAPSALDRDAVAANTKTKEESGSKAAAGTTTAEEAAKILAEKRR--LAREQRERE 470
Cdd:PHA03307   344 GPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARaaVAGRARRRD 402
PHA03247 PHA03247
large tegument protein UL36; Provisional
 220-452 4.78e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 4.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  220 AALLNASDR---TRRSQVSPLDSSVISRLLAPTQAslARSKSAATLSADGQDPSASASSINSP--VPAPKVPMRSRSidr 294
Cdd:PHA03247  2558 AAPPAAPDRsvpPPRPAPRPSEPAVTSRARRPDAP--PQSARPRAPVDDRGDPRGPAPPSPLPpdTHAPDPPPPSPS--- 2632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  295 lkssvsssdASSPDPAQKSEAEKPSPGSGLRRPSSPSVSARRRSPSPAnlvkRPPSPSAVRQKTRPPS------PGISKQ 368
Cdd:PHA03247  2633 ---------PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG----RAAQASSPPQRPRRRAarptvgSLTSLA 2699

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  369 RPPSPTPVSKPAPIQRPPLTPGVINITKKKTEAESKPKEKSTEGAGHEHGAPSALDRDAVAANTKTKEESGSKAAAGTTT 448
Cdd:PHA03247  2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP 2779


                   ....
gi 2201678600  449 AEEA 452
Cdd:PHA03247  2780 PRRL 2783
PHA03247 PHA03247
large tegument protein UL36; Provisional
 244-389 9.81e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 9.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  244 RLLAPTQASLARSKSAATLSADGQDPSASASSINSPVPAPKVPMRSRSIDRLKSSVSSSDASSPDPAQKSEAEKPSPGSG 323
Cdd:PHA03247  2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD 2861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  324 LRR-------PSSPSVSARRR---------SPSPANLVKRPPSPSAVRQKTRP--PSPGISKQRPPSPTPVSKPAPIQRP 385
Cdd:PHA03247  2862 VRRrppsrspAAKPAAPARPPvrrlarpavSRSTESFALPPDQPERPPQPQAPppPQPQPQPPPPPQPQPPPPPPPRPQP 2941


                   ....
gi 2201678600  386 PLTP 389
Cdd:PHA03247  2942 PLAP 2945
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 312-416 3.63e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 47.38  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 312 KSEAEKPSPGSGlRRPSSPSVSARRRSPSPANLVKRPPSPSAVRQKTRPPSPgISKQRPPSP--------TPVSKPAPIQ 383
Cdd:PTZ00449  586 KHPKDPEEPKKP-KRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRP-PPPQRPSSPerpegpkiIKSPKPPKSP 663

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2201678600 384 RPPLTPGVinitKKK-----TEAESKPKEKSTEGAGHE 416
Cdd:PTZ00449  664 KPPFDPKF----KEKfyddyLDAAAKSKETKTTVVLDE 697
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 272-423 1.29e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 45.49  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 272 SASSINSPVPAPKVpmrsrsidRLKSSVSSSDASSPDPAQKSEAEKPS--PGSGLRRPSSPSVSarrrsPSPANLVKRPP 349
Cdd:PHA03269   18 IIANLNTNIPIPEL--------HTSAATQKPDPAPAPHQAASRAPDPAvaPTSAASRKPDLAQA-----PTPAASEKFDP 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201678600 350 SPSAVRQKTRPPSPGISKQRPPSPTPVSKPAPIQRPPLTPGVINitkKKTEAESKpkeKSTEGAGHEHGAPSAL 423
Cdd:PHA03269   85 APAPHQAASRAPDPAVAPQLAAAPKPDAAEAFTSAAQAHEAPAD---AGTSAASK---KPDPAAHTQHSPPPFA 152
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 174-387 1.88e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  174 SVTPDSESKTEQQTTDEGETGASKRSTSTANLKPT-----EAAMNKRLSSSAALLNASDRTRRSQVSPLDSSVISrllAP 248
Cdd:PHA03307   233 GASSSDSSSSESSGCGWGPENECPLPRPAPITLPTriweaSGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGP---AP 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  249 TQASLARSKSAATLSADGQDPSASASSINSPVPAPKVPMRSRSIDRlkssvsssDASSPDPAQKSEAEKPSPGSGLRRPS 328
Cdd:PHA03307   310 SSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSR--------PPPPADPSSPRKRPRPSRAPSSPAAS 381

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2201678600  329 SPSVSARRRSPSPAnlvkrppsPSAVRQKTRPPSPGISKQRPPSPTPVSKPAPIQRPPL 387
Cdd:PHA03307   382 AGRPTRRRARAAVA--------GRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPL 432
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 251-389 1.91e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  251 ASLARSKSAATLSADGQDPSASASSINSPVPAPKVPMRSRSIDRLKSSVSSSDASSPDPAQKSEAEKPSPGSGLRRPSSP 330
Cdd:PHA03307   770 EALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPAR 849

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201678600  331 SVSARRRSPSPA------NLVKRPPSPSAVRQKTRPPSPGISKQRPPSPT-PVSKPAPIQRPPLTP 389
Cdd:PHA03307   850 SSESSKSKPAAAggrargKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGaPAPRPRPAPRVKLGP 915
PHA03247 PHA03247
large tegument protein UL36; Provisional
 175-420 2.57e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  175 VTPDSESKTEQQTTDEGETGASKRSTSTANLKPT----EAAMNKRLSSSAALLNASDrTRRSQVSPLDSSVISRLLAPTQ 250
Cdd:PHA03247  2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAppaaPAAGPPRRLTRPAVASLSE-SRESLPSPWDPADPPAAVLAPA 2815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  251 ASLARSKSAATLSADGQDPSASASSINSPVPAPKVPM----------RSRSIDRLKSSVSSSDASSPDPAQKSEAEKPSP 320
Cdd:PHA03247  2816 AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLggsvapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRST 2895

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  321 GSGLRRPSSPsvsARRRSPSPANLVKRPPSPSAVRQKTRPPSPGISKQRPPSPTPVSKPAPIQRPP--------LTPGVI 392
Cdd:PHA03247  2896 ESFALPPDQP---ERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvpqpwlgaLVPGRV 2972

                          250       260       270
                   ....*....|....*....|....*....|
gi 2201678600  393 NITKKKT--EAESKPKEKSTEGAGHEHGAP 420
Cdd:PHA03247  2973 AVPRFRVpqPAPSREAPASSTPPLTGHSLS 3002
PRK12704 PRK12704
phosphodiesterase; Provisional
 90-167 6.72e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  90 NAAKESQILE-KER--KAKLQYEKQLEERQRKLKEQKQKDEQRRAAVeEKRKQKIEEEKERHEAALHRTLERSQRLETRQ 166
Cdd:PRK12704   52 EAIKKEALLEaKEEihKLRNEFEKELRERRNELQKLEKRLLQKEENL-DRKLELLEKREEELEKKEKELEQKQQELEKKE 130


                  .
gi 2201678600 167 K 167
Cdd:PRK12704  131 E 131
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 283-408 1.14e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.75  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 283 PKVPMRSRSIDRLKSSVSSSDASSPDPAQKSEAE-----KPSPGSGLRRPSSPSVSARRRSPSPANLVKRPPSPSAVR-- 355
Cdd:PTZ00449  521 PKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEgevgkKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKKPKrp 600

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201678600 356 ----QKTRPPSPGI--------SKQRPPSPTPVSKPAPIQRP-----PLTPGVINITKK----KTEAESKPKEK 408
Cdd:PTZ00449  601 rsaqRPTRPKSPKLpelldipkSPKRPESPKSPKRPPPPQRPssperPEGPKIIKSPKPpkspKPPFDPKFKEK 674
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 318-407 1.32e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.10  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 318 PSPGSGLRRPSSPSVSARRRSPSPANlvkRPPSPSAVRQKTRPPSPGISKQRPPSPTPVSKPAPIQR---PPLTPGVINI 394
Cdd:PRK14950  362 PVPAPQPAKPTAAAPSPVRPTPAPST---RPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPesaPKLTRAAIPV 438

                          90
                  ....*....|....
gi 2201678600 395 -TKKKTEAESKPKE 407
Cdd:PRK14950  439 dEKPKYTPPAPPKE 452
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 88-163 1.92e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  88 KQNAAKESQILEKERKAKLQYEkqleERQRKLKEQKQKDEQRRAAVEEKRK---QKIEEEKERH-EAALHRTLERSQRLE 163
Cdd:pfam17380 388 QQKNERVRQELEAARKVKILEE----ERQRKIQQQKVEMEQIRAEQEEARQrevRRLEEERAREmERVRLEEQERQQQVE 463
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
227-431 3.46e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 227 DRTRRSQVSPLDSSVISRLLAPTQASLARSKSAAT-----LSADGQDPSASASSINSPVPAPKVPMRSRSIDRlksSVSS 301
Cdd:PRK12323  371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAApaaapAAAAAARAVAAAPARRSPAPEALAAARQASARG---PGGA 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 302 SDASSPDPAQKSEAEKPSPGSGLRRPSSPSVSARRRSPSPANLVKRPPSPSAVRQKTRPPSPGISKQRP--------PSP 373
Cdd:PRK12323  448 PAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAapagwvaeSIP 527

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 374 TPVSKPAPIQRPPLTPGVINITKKKTEAESKPKEKSTEGAGHEHGAPSALDRD--AVAAN 431
Cdd:PRK12323  528 DPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDwpALAAR 587
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 243-390 3.67e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 243 SRLLAP--------TQASLARSKSAATLSADGQDPSASASSINSPVPAPKVPmrsrsidrlkSSVSSSDASSPDPAQKSE 314
Cdd:PRK07764  360 ARMLLPsasddergLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPA----------PAAAAPAAAAAPAPAAAP 429

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201678600 315 AEKPSPGSGLRRPSSPSVSARRRSPSPAnlvkRPPSPSAVRQKTRPPSPGISKQRPPSPTPVSKPAPIQRPPLTPG 390
Cdd:PRK07764  430 QPAPAPAPAPAPPSPAGNAPAGGAPSPP----PAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPA 501
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 254-432 3.90e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 254 ARSKSAATLSADGQDPSASASSINSPVPAPKVPMRSRSIDRLKSSVSSSDASSPDPAQKSEAEKPSPGSGlRRPSSPSVS 333
Cdd:PRK07764  625 AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA-GAAPAQPAP 703

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 334 ARRRSPSPANLVKRPPSPSAVRQKTRPPSPGISKQRPPSPTPVSKPAPIQRP-PLTPGVINITKKKTEAESKPKEKSTEG 412
Cdd:PRK07764  704 APAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPaQPPPPPAPAPAAAPAAAPPPSPPSEEE 783

                         170       180
                  ....*....|....*....|
gi 2201678600 413 AGHEHGAPSALDRDAVAANT 432
Cdd:PRK07764  784 EMAEDDAPSMDDEDRRDAEE 803
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 325-389 4.14e-03

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 39.25  E-value: 4.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201678600 325 RRPSSPSVSArrrSPSPANLVKRPPSPSAvrqktRPPSPGISKQRPPSPTPVSKPAPIQRPPLTP 389
Cdd:cd21577    28 KRSSPPSSSS---SSSSSSSSSSSPSSRA-----SPPSPYSKSSPPSPPQQRPLSPPLSLPPPVA 84
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 88-168 5.29e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  88 KQNAAKESQILEKERKaklQYEKQLEERQRKLKEQKQKDEQRRAAVEEKRKQKI-EEEKERHEAALHRTLERSQRLETRQ 166
Cdd:pfam17380 467 QQEEERKRKKLELEKE---KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLlEKEMEERQKAIYEEERRREAEEERR 543


                  ..
gi 2201678600 167 KR 168
Cdd:pfam17380 544 KQ 545
SWIRM-assoc_2 pfam16496
SWIRM-associated domain at the N-terminal; Much of the higher eukaryote SWI/SNF complex ...
 314-369 5.48e-03

SWIRM-associated domain at the N-terminal; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 proteins is of low-complexity and or disordered. However, there are several short regions that are quite highly conserved. This is one of these regions. The function of the individual regions is not known.


Pssm-ID: 465143  Cd Length: 412  Bit Score: 40.02  E-value: 5.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2201678600 314 EAEKPSPGSGLRRPSSPSVSARRRSPSPanlvkrPPSPSAVRQKTRPPSPGISKQR 369
Cdd:pfam16496 272 EDEMSSPDPDRKDKKSSPGKKRKRSPSP------PPTPVGKKKSGRKGSPARRKKR 321
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
108-199 5.98e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 108 YEKQLEERQRKLKEQKQKDEQRRAAVEEKRKQKIEEEKERHEAALHRTLERSQRLETRQKRwswggsVTPDSESKTEQQT 187
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQ------VEEKLDELREERD 677

                          90
                  ....*....|..
gi 2201678600 188 TDEGETGASKRS 199
Cdd:PRK02224  678 DLQAEIGAVENE 689
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
 100-168 6.09e-03

Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.


Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 37.22  E-value: 6.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201678600 100 KERKAKLQYEKQLEERQRKLKEQKQKD-EQRRAAVEEKRKQKieEEKERHE---AALHRtlERSQRLETRQKR 168
Cdd:pfam03879  33 EKRQEKRLELKAIKAKEKELKDEKEAErQRRIQAIKERREAK--EEKERYEelaAKMHA--KKVERLKRKEKR 101
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
 324-424 6.18e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 39.49  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 324 LRRPSSPSVSARRRSPSPANlvKRPPSPSAVRQKTrPPSPGISKQRPPSPTPVSKPAPIQRPPLTP-GVinitkkkTEAE 402
Cdd:PHA03201    1 MKRARSRSPSPPRRPSPPRP--TPPRSPDASPEET-PPSPPGPGAEPPPGRAAGPAAPRRRPRGCPaGV-------TFSS 70

                          90       100
                  ....*....|....*....|..
gi 2201678600 403 SKPKEKSTEGAGHEHGAPSALD 424
Cdd:PHA03201   71 SAPPRPPLGLDDAPAATPPPLD 92
PTZ00121 PTZ00121
MAEBL; Provisional
 92-214 6.47e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 6.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600   92 AKESQILEKERKAKLQYEKQLEERQRKLKEQKQKDEQRRAAvEEKRKQKIEEEKERHEAALHRTLERSQRLETRQKRwsw 171
Cdd:PTZ00121  1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK--- 1386

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2201678600  172 ggsvtpdsesKTEQQTTDEGETGASKRSTSTANLKPTEAAMNK 214
Cdd:PTZ00121  1387 ----------AEEKKKADEAKKKAEEDKKKADELKKAAAAKKK 1419
PTZ00121 PTZ00121
MAEBL; Provisional
 396-682 7.16e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  396 KKKTEAESKP---KEKSTEGAGHEHGAPSALDRDAVAANTKTKEESGSKA-----AAGTTTAEEAAKilAEKRRLAREQR 467
Cdd:PTZ00121  1463 KKKAEEAKKAdeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdeakkAEEAKKADEAKK--AEEAKKADEAK 1540

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  468 EREDQERIQRQEEERIREEEMAKRAVEEKARREEELRKQEEEKRLIYEEQQRQAEEERIRREQEEQEKLAELqhqREEAE 547
Cdd:PTZ00121  1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA---KKAEE 1617

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  548 AKAQEEAERQRLERERIMQQNMQERLERKKRIEEIMKRTR----KSDQNESKLQNEGKSACEVMEGEDIEEEEELGLEKA 623
Cdd:PTZ00121  1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201678600  624 DQPGKlngidLTQEVKGETEGCVQTARSLMCTESEQHAVTES---KASEVFMNGSDLKSDEG 682
Cdd:PTZ00121  1698 AEEAK-----KAEELKKKEAEEKKKAEELKKAEEENKIKAEEakkEAEEDKKKAEEAKKDEE 1754
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 244-384 7.17e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  244 RLLAPTQASLARSKSAATLSADGQDPSASASSinSPVPAPKVPMRSRSIDRLKSSVSSSDASSPDPAQKSEAEKPSPGSG 323
Cdd:PHA03307    91 SLSTLAPASPAREGSPTPPGPSSPDPPPPTPP--PASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAAS 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201678600  324 LRRPSSPSVSARRRSPSPAN-LVKRPPSPSAVRQKTRPPSPGISkQRPPSPTPVSKPAPIQR 384
Cdd:PHA03307   169 SRQAALPLSSPEETARAPSSpPAEPPPSTPPAAASPRPPRRSSP-ISASASSPAPAPGRSAA 229
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 87-147 7.39e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 38.48  E-value: 7.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201678600  87 EKQNAAKESQILEKERKaKLQYEKQLEERQRKLKEQKQKDEQRRAAVEEKRKQKIEEEKER 147
Cdd:pfam09756  18 RQQREAEEEEREEREKL-EEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEK 77
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 239-387 7.58e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.70  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 239 SSVISRLLA------PTQASLARSKSAATLSADGQDPSASASSINSPVPAPKVPMRSRSidrlkssvsssdasSPDPAQK 312
Cdd:PRK14951  355 TMVLLRLLAfkpaaaAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASA--------------PAAPPAA 420

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201678600 313 SEAEKPSPGSGLRRPSSPSVSARRRSPSPANLVKRPPSPSAVRQKTRPPSPGISKQRPPSPTPVskPAPIQRPPL 387
Cdd:PRK14951  421 APPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPA--AARLTPTEE 493
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 98-333 7.97e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.03  E-value: 7.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600   98 LEKERKAklqYEKQLEERQRKLKEQKQKDEQRRAAVEEKRKQKIEEEKERHEAALHRTLERSQRLETRQKRWSWGGSVTP 177
Cdd:PTZ00108  1134 LDKFEEA---LEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLD 1210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  178 DSESKTEQQTTDEGETGASKRSTSTANLKPTEAAMNKRLSSSAALLNASDRTRRSQVSPLDSSVISRllapTQASLARSK 257
Cdd:PTZ00108  1211 DKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKR----VSAVQYSPP 1286

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201678600  258 SAATLSADGQDPSASASSINSPVPAPKVPMRSRSIDRLKSSVSSSDASSPDPAQKSEAEKPSPGSGLRRPSSPSVS 333
Cdd:PTZ00108  1287 PPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSD 1362
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 88-167 8.11e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.68  E-value: 8.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600  88 KQNAAKESQILEKERKAKLqyEKQLEERQRKLKEQKQKDEQRRAAVEEKR--KQKIEEEKERHEAALHRTLERSQRLETR 165
Cdd:COG0542   427 KEALKKEQDEASFERLAEL--RDELAELEEELEALKARWEAEKELIEEIQelKEELEQRYGKIPELEKELAELEEELAEL 504


                  ..
gi 2201678600 166 QK 167
Cdd:COG0542   505 AP 506
PTZ00121 PTZ00121
MAEBL; Provisional
 92-168 8.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 8.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600   92 AKESQILEKERKAKLQYEKQLEERQRKLKEQKQ--------KDEQRRAAVEEKRK----QKIEEEKERHEAALHRTLERS 159
Cdd:PTZ00121  1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenkikAAEEAKKAEEDKKKaeeaKKAEEDEKKAAEALKKEAEEA 1701


                   ....*....
gi 2201678600  160 QRLETRQKR 168
Cdd:PTZ00121  1702 KKAEELKKK 1710
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
313-438 9.70e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 39.37  E-value: 9.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201678600 313 SEAEKPSPGSGLRRPSSPSVSARRRSPSPANLVKRPPSPSAVRQKTRPPSPGISKQRPPSPTPVSKPAPIQ--------- 383
Cdd:PRK14971  364 QKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAvpvnppsta 443

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2201678600 384 RPPLTPGVINITKKKTEAESKPKEKSTEGAGHEHGApsALDRDAVAANTKTKEES 438
Cdd:PRK14971  444 PQAVRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAE--QATGNIKEAPTGTQKEI 496
PRK12704 PRK12704
phosphodiesterase; Provisional
 100-163 9.72e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 9.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201678600 100 KERKAKLQY-EKQLEERQRKLKEQKQKDEQRRAAVEEKRK---QKIEEEKERHEAALHRTLERSQRLE 163
Cdd:PRK12704   78 RERRNELQKlEKRLLQKEENLDRKLELLEKREEELEKKEKeleQKQQELEKKEEELEELIEEQLQELE 145
 
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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