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Conserved domains on  [gi|2044114687|ref|XP_041627604|]
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centrosomal protein of 104 kDa isoform X1 [Vulpes lagopus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA03418 super family cl25519
hypothetical E4 protein; Provisional
 305-418 2.49e-05

hypothetical E4 protein; Provisional


The actual alignment was detected with superfamily member PHA03418:

Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 46.66  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 305 LPLQPLTHSASPRH-KQQVPSLPPQEESAPESRfAEPFLQEKPP-AHPPGPSQHSTADQSPPATDPhlkthlqsvpyDER 382
Cdd:PHA03418   33 LPLLPAPHHPNPQEdPDKNPSPPPDPPLTPRPP-AQPNGHNKPPvTKQPGGEGTEEDHQAPLAADA-----------DDD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2044114687 383 PLPATRKQ-------PAAAALEPEKSDSDvsEAPKRGAPGEPE 418
Cdd:PHA03418  101 PRPGKRSKadehgpaPGRAALAPFKLDLD--QDPLHGDPDPPP 141
 
Name Accession Description Interval E-value
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 305-418 2.49e-05

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 46.66  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 305 LPLQPLTHSASPRH-KQQVPSLPPQEESAPESRfAEPFLQEKPP-AHPPGPSQHSTADQSPPATDPhlkthlqsvpyDER 382
Cdd:PHA03418   33 LPLLPAPHHPNPQEdPDKNPSPPPDPPLTPRPP-AQPNGHNKPPvTKQPGGEGTEEDHQAPLAADA-----------DDD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2044114687 383 PLPATRKQ-------PAAAALEPEKSDSDvsEAPKRGAPGEPE 418
Cdd:PHA03418  101 PRPGKRSKadehgpaPGRAALAPFKLDLD--QDPLHGDPDPPP 141
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 298-428 1.75e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 298 PIRRPSDLP----LQPL----TH---SASPRHKQqvpsLPPQEESAPESRFAEPFL---QEKPPA---HPPGPSQHSTAD 360
Cdd:pfam03154 383 PFQMNSNLPpppaLKPLsslsTHhppSAHPPPLQ----LMPQSQQLPPPPAQPPVLtqsQSLPPPaasHPPTSGLHQVPS 458

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044114687 361 QSPPATDPHLKTHLQSVPYDERPLPATrkQPAAAALEPEKSDSDVSEAPKRGAPGEPEP---LTEKALREA 428
Cdd:pfam03154 459 QSPFPQHPFVPGGPPPITPPSGPPTST--SSAMPGIQPPSSASVSSSGPVPAAVSCPLPpvqIKEEALDEA 527
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 306-398 5.27e-04

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


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 41.70  E-value: 5.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687  306 PLQPLTHSASPRHkqQVPSLPPQEESAPEsrfaEPFLQEkPPAHPPGPSQHSTADQSPPATDPHLKTHLQSVPyderPLP 385
Cdd:smart00818  44 QQHPPTHTLQPHH--HIPVLPAQQPVVPQ----QPLMPV-PGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQ----PQQ 112

                           90
                   ....*....|...
gi 2044114687  386 ATRKQPAAAALEP 398
Cdd:smart00818 113 PMQPQPPVHPIPP 125
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 316-438 1.93e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 41.68  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 316 PRHKQQVPSLPPQEESAPESRFAEPFLQEKPPAHPPGPSQHSTADQSPPATDPHLKTHLQSVPYDERPLPATRKQPAAAA 395
Cdd:NF040712  190 PDFGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAE 269

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2044114687 396 LEPEKSDSDVSEAPKRGAPGEPEPLTEKALREASPAVEVLGES 438
Cdd:NF040712  270 PDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEE 312
 
Name Accession Description Interval E-value
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 305-418 2.49e-05

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 46.66  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 305 LPLQPLTHSASPRH-KQQVPSLPPQEESAPESRfAEPFLQEKPP-AHPPGPSQHSTADQSPPATDPhlkthlqsvpyDER 382
Cdd:PHA03418   33 LPLLPAPHHPNPQEdPDKNPSPPPDPPLTPRPP-AQPNGHNKPPvTKQPGGEGTEEDHQAPLAADA-----------DDD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2044114687 383 PLPATRKQ-------PAAAALEPEKSDSDvsEAPKRGAPGEPE 418
Cdd:PHA03418  101 PRPGKRSKadehgpaPGRAALAPFKLDLD--QDPLHGDPDPPP 141
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 313-442 1.64e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 313 SASPRHKQQVPSLPPQEESAPESRFAEPFLQEKPPAHPPGPSQHSTADQSPPATDPHLKTHLQSVPYDERPLPATRKQPA 392
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2044114687 393 AAALEPEKSDSDVSEAPKRGAPGEPEPLT----EKALREASPAV--EVLGESLVAG 442
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPpseeEEMAEDDAPSMddEDRRDAEEVA 805
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 298-428 1.75e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 298 PIRRPSDLP----LQPL----TH---SASPRHKQqvpsLPPQEESAPESRFAEPFL---QEKPPA---HPPGPSQHSTAD 360
Cdd:pfam03154 383 PFQMNSNLPpppaLKPLsslsTHhppSAHPPPLQ----LMPQSQQLPPPPAQPPVLtqsQSLPPPaasHPPTSGLHQVPS 458

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2044114687 361 QSPPATDPHLKTHLQSVPYDERPLPATrkQPAAAALEPEKSDSDVSEAPKRGAPGEPEP---LTEKALREA 428
Cdd:pfam03154 459 QSPFPQHPFVPGGPPPITPPSGPPTST--SSAMPGIQPPSSASVSSSGPVPAAVSCPLPpvqIKEEALDEA 527
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 306-398 5.27e-04

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


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 41.70  E-value: 5.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687  306 PLQPLTHSASPRHkqQVPSLPPQEESAPEsrfaEPFLQEkPPAHPPGPSQHSTADQSPPATDPHLKTHLQSVPyderPLP 385
Cdd:smart00818  44 QQHPPTHTLQPHH--HIPVLPAQQPVVPQ----QPLMPV-PGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQ----PQQ 112

                           90
                   ....*....|...
gi 2044114687  386 ATRKQPAAAALEP 398
Cdd:smart00818 113 PMQPQPPVHPIPP 125
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 294-427 5.28e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 294 VDAEPIRRPSDLPLQPLTHSASPRHKQQVPSLPPQEESAPE-----SRFAEPFLQEKPPAHPPGPSQHSTADQSPPATDP 368
Cdd:PRK07764  666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAatppaGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEP 745

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044114687 369 HLKTHLQSVPYD-------ERPLPATRKQPAAAALEPEKSDSDVSEAPKRGAPGEPEPLTEKALRE 427
Cdd:PRK07764  746 DDPPDPAGAPAQpppppapAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMELLEE 811
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
296-431 6.93e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 6.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 296 AEPIRRPSDLPLQPLTHSASPRHKQQVPSlppqEESAPESRFAEPFLQEKPPAHPPGPSQHSTADQSPPATDPHLKTHLQ 375
Cdd:PRK07003  407 GAALAPKAAAAAAATRAEAPPAAPAPPAT----ADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPAS 482

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2044114687 376 SVPYDERPLPATRKQPAAAALEPEKSDSDVSEAPKRgaPGEPEPLTEKALREASPA 431
Cdd:PRK07003  483 DAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASR--EDAPAAAAPPAPEARPPT 536
PHA03247 PHA03247
large tegument protein UL36; Provisional
 298-428 1.76e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687  298 PIRRPSDLPLQPLTHSASPRhkqqvPSLPPQEESaPESRFAEPFLQEKPPAHPPGPSQHSTADQSPPATDPHLKTHLQSV 377
Cdd:PHA03247  2569 PPPRPAPRPSEPAVTSRARR-----PDAPPQSAR-PRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHP 2642

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2044114687  378 PYDERPLPATRKQPAAAALEPEKSDSDVSEAPKRGAPgePEPLTEKALREA 428
Cdd:PHA03247  2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP--PQRPRRRAARPT 2691
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 316-438 1.93e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 41.68  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 316 PRHKQQVPSLPPQEESAPESRFAEPFLQEKPPAHPPGPSQHSTADQSPPATDPHLKTHLQSVPYDERPLPATRKQPAAAA 395
Cdd:NF040712  190 PDFGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAE 269

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2044114687 396 LEPEKSDSDVSEAPKRGAPGEPEPLTEKALREASPAVEVLGES 438
Cdd:NF040712  270 PDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEE 312
PHA03247 PHA03247
large tegument protein UL36; Provisional
 296-435 1.95e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687  296 AEPIRRPSDLPLQP---LTHSASPRHKQQVPSLPPQEESAPESR--------FAEPFLQEKPPAHPPGPSQHSTADQSPP 364
Cdd:PHA03247  2646 VPPPERPRDDPAPGrvsRPRRARRLGRAAQASSPPQRPRRRAARptvgsltsLADPPPPPPTPEPAPHALVSATPLPPGP 2725

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044114687  365 ATDPHLKTHLQSVPYdERPLPATRKQPAAAA--LEPEKSDSDVSEAPKRGAPGEPEP-LTEKALREASPAVEVL 435
Cdd:PHA03247  2726 AAARQASPALPAAPA-PPAVPAGPATPGGPArpARPPTTAGPPAPAPPAAPAAGPPRrLTRPAVASLSESRESL 2798
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 279-399 3.89e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.95  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 279 QFRNQVYEQLQLH-SLVDAEPIRRPSDLPLQPLTHSASPRHKQQVPSLPPQEESAPESRFAEPFLQekpPAHPPGPSQHS 357
Cdd:PRK14950  340 QLRTTSYGQLPLElAVIEALLVPVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRE---TATPPPVPPRP 416

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2044114687 358 TADQSPPATDPHLKTHLQSVPYDERPL---PATRKQPAAAALEPE 399
Cdd:PRK14950  417 VAPPVPHTPESAPKLTRAAIPVDEKPKytpPAPPKEEEKALIADG 461
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 298-428 5.45e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 40.62  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 298 PIRRPSDLPLQPLTHSASPRHKQQVPSLPPQEESAPESR------FAEPFLQEKPPAHPPGPSQHSTADQSPPATDPHlk 371
Cdd:PRK07994  379 ASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPEttsqllAARQQLQRAQGATKAKKSEPAAASRARPVNSAL-- 456

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2044114687 372 thlqsvpydERpLPATRKQPAAAALEPEKSDSDVSEAPKRGAPGEPEPLTEKALREA 428
Cdd:PRK07994  457 ---------ER-LASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKA 503
dnaA PRK14086
chromosomal replication initiator protein DnaA;
285-431 5.75e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 40.58  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 285 YEQLQLHSLVDAEPiRRPSDLPLQPLTHSASPRhkqqVPSLPPQEESAPESRFAEPFLQEKPPAHPPGPSQHSTA-DQSP 363
Cdd:PRK14086  146 YPAYQQRPEPGAWP-RAADDYGWQQQRLGFPPR----APYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRpDWDR 220

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044114687 364 PATDPHlkthlqsvpydERPLPAtrkqPAAaalepeksdsdvsEAPKRGAPGEPEPLTEKALREASPA 431
Cdd:PRK14086  221 PRRDRT-----------DRPEPP----PGA-------------GHVHRGGPGPPERDDAPVVPIRPSA 260
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 309-441 8.49e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 39.85  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044114687 309 PLTHSASPRHKQQVPSLPPQEESAPESRFAEPFLQEKPPAHPPGPSQHSTADQSPPATDPHLKTHLQSVPYDERPLPATR 388
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKK 440

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2044114687 389 KQPAAAALEPEKSDSDVSEAPKRGAP--GEPEPLTEKALR-EASPAVEVLGESLVA 441
Cdd:PRK07994  441 SEPAAASRARPVNSALERLASVRPAPsaLEKAPAKKEAYRwKATNPVEVKKEPVAT 496
 
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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