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Conserved domains on  [gi|909136023|gb|KNE61952|]
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FCP1-like phosphatase, phosphatase domain-containing protein [Allomyces macrogynus ATCC 38327]

Protein Classification

HAD_FCP1-like and BRCT_CTDP1 domain-containing protein( domain architecture ID 12856661)

HAD_FCP1-like and BRCT_CTDP1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FCP1_euk TIGR02250
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ...
 162-329 4.22e-67

FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the humanRNA polymerase II subunit A C-terminal domain phosphatase (FCP1) and closely related phosphatases from eukaryotes including plants, fungi, and slime mold. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDDppphW). This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in the human NLI interacting factor-like phosphatases, and together both are detected by the pfam03031.


:

Pssm-ID: 131304  Cd Length: 156  Bit Score: 217.92  E-value: 4.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  162 LLRERRLSIILDLDQTLIHATADPGVGTWidHESAKQSPDSsgtprpamaTPLRDLYRFRLadDPHEYYLRLRPHLHEFL 241
Cdd:TIGR02250   1 LLREKKLHLVLDLDQTLIHTTKDPTLSEW--EKYDIEEPNS---------ETRRDLRKFNL--GTMWYLTKLRPFLHEFL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  242 AGLSSLFEMHIYTMGSRPYANKVAAIIDPDKRYFSERILSRDESGSFHKKSLQRLFPCDQSMVVAIDDRGDVWGWA-DNV 320
Cdd:TIGR02250  68 KEASKLYEMHVYTMGTRAYAQAIAKLIDPDGKYFGDRIISRDESGSPHTKSLLRLFPADESMVVIIDDREDVWPWHkRNL 147


                  ....*....
gi 909136023  321 IRVHPYSYF 329
Cdd:TIGR02250 148 IQIEPYNYF 156
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 395-490 2.62e-38

BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins; CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.


:

Pssm-ID: 349361 [Multi-domain]  Cd Length: 97  Bit Score: 137.28  E-value: 2.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023 395 DVRQILPRMKRQVLAGCELVFSGIIPRHVNELESDVWKLATSFGARCTSAVTKTTTHVVATRSGTAKVRQAHAQGTT-VV 473
Cdd:cd17729    1 DVKDILPELRSKVLKGCVIVFSGVIPTGIDPERSRLWKLAESLGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMPGIhVV 80

                         90
                 ....*....|....*..
gi 909136023 474 TPGWLFTSIAYWKRLEE 490
Cdd:cd17729   81 HPDWLWACAERWERVDE 97
 
Name Accession Description Interval E-value
FCP1_euk TIGR02250
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ...
 162-329 4.22e-67

FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the humanRNA polymerase II subunit A C-terminal domain phosphatase (FCP1) and closely related phosphatases from eukaryotes including plants, fungi, and slime mold. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDDppphW). This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in the human NLI interacting factor-like phosphatases, and together both are detected by the pfam03031.


Pssm-ID: 131304  Cd Length: 156  Bit Score: 217.92  E-value: 4.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  162 LLRERRLSIILDLDQTLIHATADPGVGTWidHESAKQSPDSsgtprpamaTPLRDLYRFRLadDPHEYYLRLRPHLHEFL 241
Cdd:TIGR02250   1 LLREKKLHLVLDLDQTLIHTTKDPTLSEW--EKYDIEEPNS---------ETRRDLRKFNL--GTMWYLTKLRPFLHEFL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  242 AGLSSLFEMHIYTMGSRPYANKVAAIIDPDKRYFSERILSRDESGSFHKKSLQRLFPCDQSMVVAIDDRGDVWGWA-DNV 320
Cdd:TIGR02250  68 KEASKLYEMHVYTMGTRAYAQAIAKLIDPDGKYFGDRIISRDESGSPHTKSLLRLFPADESMVVIIDDREDVWPWHkRNL 147


                  ....*....
gi 909136023  321 IRVHPYSYF 329
Cdd:TIGR02250 148 IQIEPYNYF 156
CPDc smart00577
catalytic domain of ctd-like phosphatases;
166-333 4.53e-41

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 146.99  E-value: 4.53e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023   166 RRLSIILDLDQTLIHatadpgvgtwidhesakqspdsSGTPRPAMATPLRDLYRFRLADDPHEYYLRLRPHLHEFLAGLS 245
Cdd:smart00577   1 KKKTLVLDLDETLVH----------------------STHRSFKEWTNRDFIVPVLIDGHPHGVYVKKRPGVDEFLKRAS 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023   246 SLFEMHIYTMGSRPYANKVAAIIDPdKRYFSERILSRDESGSF---HKKSLqRLFPCDQSMVVAIDDRGDVWGWA-DNVI 321
Cdd:smart00577  59 ELFELVVFTAGLRMYADPVLDLLDP-KKYFGYRRLFRDECVFVkgkYVKDL-SLLNRDLSKVIIIDDSPDSWPFHpENLI 136

                          170
                   ....*....|..
gi 909136023   322 RVHPYSYFLRTG 333
Cdd:smart00577 137 PIKPWFGDPDDT 148
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 395-490 2.62e-38

BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins; CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.


Pssm-ID: 349361 [Multi-domain]  Cd Length: 97  Bit Score: 137.28  E-value: 2.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023 395 DVRQILPRMKRQVLAGCELVFSGIIPRHVNELESDVWKLATSFGARCTSAVTKTTTHVVATRSGTAKVRQAHAQGTT-VV 473
Cdd:cd17729    1 DVKDILPELRSKVLKGCVIVFSGVIPTGIDPERSRLWKLAESLGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMPGIhVV 80

                         90
                 ....*....|....*..
gi 909136023 474 TPGWLFTSIAYWKRLEE 490
Cdd:cd17729   81 HPDWLWACAERWERVDE 97
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 167-323 1.85e-35

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319823  Cd Length: 134  Bit Score: 130.79  E-value: 1.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023 167 RLSIILDLDQTLIHATadpgvgtWidhesakqspdssgTPRPAMATPLRDLYRFRladdPHEYYLRLRPHLHEFLAGLSS 246
Cdd:cd07521    1 KLTLVLDLDETLVHST-------W--------------KPVLSEDFKIPVLPDGR----EHGYYVKKRPGVDEFLERLSK 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023 247 LFEMHIYTMGSRPYANKVAAIIDPDKRYFSeRILSRDESGSF---HKKSLQRLFPCDqSMVVAIDD-RGDVWGWADNVIR 322
Cdd:cd07521   56 LYEIVIFTAGTRAYADPVADKLDPNGLFID-RRLFRDSCVYVdgnYVKDLSKLFRDL-SKVVIIDDsPGSYWLQPENAIP 133


                 .
gi 909136023 323 V 323
Cdd:cd07521  134 I 134
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 168-397 9.61e-30

NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain.


Pssm-ID: 397254  Cd Length: 160  Bit Score: 115.41  E-value: 9.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  168 LSIILDLDQTLIHATADPgvgtwidhesakqspdssgtprpamatPLRDLYRFRLADDPHEYYLRLRPHLHEFLAGLSSL 247
Cdd:pfam03031   1 KTLVLDLDETLVHSSFEP---------------------------PLKSDFILPVPGETHGGYVKKRPGLDEFLKELSKY 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  248 FEMHIYTMGSRPYANKVAAIIDPDKRYFSERiLSRDES---GSFHKKSLQRLFPcDQSMVVAIDDRGDVWGW-ADNVIRV 323
Cdd:pfam03031  54 YEIVIFTASSKEYADPVLDILDPNGKLFSHR-LYRESCkfeDGVYVKDLSLLGR-DLSRVVIVDNSPDSFLLqPDNGIPI 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909136023  324 HPYsyflrTGDinaplgardtppipgsapapdaekrrlpipvrvvDDDKELKILLTKLQELHQEfyggpnRDVR 397
Cdd:pfam03031 132 PPF-----FGD----------------------------------PDDNELLKLLPFLEGLAGV------DDVR 160
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 404-482 1.34e-08

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 52.30  E-value: 1.34e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909136023  404 KRQVLAGCELVFSGIIPRHVNELEsdvwKLATSFGARCTSAVTKTTTHVVATRsGTAKVRQAHAQGTTVVTPGWLFTSI 482
Cdd:pfam00533   2 KEKLFSGKTFVITGLDGLERDELK----ELIEKLGGKVTDSLSKKTTHVIVEA-RTKKYLKAKELGIPIVTEEWLLDCI 75
BRCT smart00292
breast cancer carboxy-terminal domain;
407-482 1.72e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 48.91  E-value: 1.72e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909136023   407 VLAGCELVFSGIIPrhvNELESDVWKLATSFGARCTSAVT-KTTTHVVATRSGTAKVRQAHAQ--GTTVVTPGWLFTSI 482
Cdd:smart00292   3 LFKGKTFYITGSFD---KEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKLELLKAIalGIPIVKEEWLLDCL 78
 
Name Accession Description Interval E-value
FCP1_euk TIGR02250
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ...
 162-329 4.22e-67

FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the humanRNA polymerase II subunit A C-terminal domain phosphatase (FCP1) and closely related phosphatases from eukaryotes including plants, fungi, and slime mold. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDDppphW). This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in the human NLI interacting factor-like phosphatases, and together both are detected by the pfam03031.


Pssm-ID: 131304  Cd Length: 156  Bit Score: 217.92  E-value: 4.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  162 LLRERRLSIILDLDQTLIHATADPGVGTWidHESAKQSPDSsgtprpamaTPLRDLYRFRLadDPHEYYLRLRPHLHEFL 241
Cdd:TIGR02250   1 LLREKKLHLVLDLDQTLIHTTKDPTLSEW--EKYDIEEPNS---------ETRRDLRKFNL--GTMWYLTKLRPFLHEFL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  242 AGLSSLFEMHIYTMGSRPYANKVAAIIDPDKRYFSERILSRDESGSFHKKSLQRLFPCDQSMVVAIDDRGDVWGWA-DNV 320
Cdd:TIGR02250  68 KEASKLYEMHVYTMGTRAYAQAIAKLIDPDGKYFGDRIISRDESGSPHTKSLLRLFPADESMVVIIDDREDVWPWHkRNL 147


                  ....*....
gi 909136023  321 IRVHPYSYF 329
Cdd:TIGR02250 148 IQIEPYNYF 156
CPDc smart00577
catalytic domain of ctd-like phosphatases;
166-333 4.53e-41

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 146.99  E-value: 4.53e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023   166 RRLSIILDLDQTLIHatadpgvgtwidhesakqspdsSGTPRPAMATPLRDLYRFRLADDPHEYYLRLRPHLHEFLAGLS 245
Cdd:smart00577   1 KKKTLVLDLDETLVH----------------------STHRSFKEWTNRDFIVPVLIDGHPHGVYVKKRPGVDEFLKRAS 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023   246 SLFEMHIYTMGSRPYANKVAAIIDPdKRYFSERILSRDESGSF---HKKSLqRLFPCDQSMVVAIDDRGDVWGWA-DNVI 321
Cdd:smart00577  59 ELFELVVFTAGLRMYADPVLDLLDP-KKYFGYRRLFRDECVFVkgkYVKDL-SLLNRDLSKVIIIDDSPDSWPFHpENLI 136

                          170
                   ....*....|..
gi 909136023   322 RVHPYSYFLRTG 333
Cdd:smart00577 137 PIKPWFGDPDDT 148
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 395-490 2.62e-38

BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins; CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.


Pssm-ID: 349361 [Multi-domain]  Cd Length: 97  Bit Score: 137.28  E-value: 2.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023 395 DVRQILPRMKRQVLAGCELVFSGIIPRHVNELESDVWKLATSFGARCTSAVTKTTTHVVATRSGTAKVRQAHAQGTT-VV 473
Cdd:cd17729    1 DVKDILPELRSKVLKGCVIVFSGVIPTGIDPERSRLWKLAESLGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMPGIhVV 80

                         90
                 ....*....|....*..
gi 909136023 474 TPGWLFTSIAYWKRLEE 490
Cdd:cd17729   81 HPDWLWACAERWERVDE 97
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 167-323 1.85e-35

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319823  Cd Length: 134  Bit Score: 130.79  E-value: 1.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023 167 RLSIILDLDQTLIHATadpgvgtWidhesakqspdssgTPRPAMATPLRDLYRFRladdPHEYYLRLRPHLHEFLAGLSS 246
Cdd:cd07521    1 KLTLVLDLDETLVHST-------W--------------KPVLSEDFKIPVLPDGR----EHGYYVKKRPGVDEFLERLSK 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023 247 LFEMHIYTMGSRPYANKVAAIIDPDKRYFSeRILSRDESGSF---HKKSLQRLFPCDqSMVVAIDD-RGDVWGWADNVIR 322
Cdd:cd07521   56 LYEIVIFTAGTRAYADPVADKLDPNGLFID-RRLFRDSCVYVdgnYVKDLSKLFRDL-SKVVIIDDsPGSYWLQPENAIP 133


                 .
gi 909136023 323 V 323
Cdd:cd07521  134 I 134
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 168-397 9.61e-30

NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain.


Pssm-ID: 397254  Cd Length: 160  Bit Score: 115.41  E-value: 9.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  168 LSIILDLDQTLIHATADPgvgtwidhesakqspdssgtprpamatPLRDLYRFRLADDPHEYYLRLRPHLHEFLAGLSSL 247
Cdd:pfam03031   1 KTLVLDLDETLVHSSFEP---------------------------PLKSDFILPVPGETHGGYVKKRPGLDEFLKELSKY 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  248 FEMHIYTMGSRPYANKVAAIIDPDKRYFSERiLSRDES---GSFHKKSLQRLFPcDQSMVVAIDDRGDVWGW-ADNVIRV 323
Cdd:pfam03031  54 YEIVIFTASSKEYADPVLDILDPNGKLFSHR-LYRESCkfeDGVYVKDLSLLGR-DLSRVVIVDNSPDSFLLqPDNGIPI 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909136023  324 HPYsyflrTGDinaplgardtppipgsapapdaekrrlpipvrvvDDDKELKILLTKLQELHQEfyggpnRDVR 397
Cdd:pfam03031 132 PPF-----FGD----------------------------------PDDNELLKLLPFLEGLAGV------DDVR 160
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 167-330 3.21e-16

Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031.


Pssm-ID: 274055  Cd Length: 162  Bit Score: 76.56  E-value: 3.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  167 RLSIILDLDQTLIHatadpgvgtwidhesakqspdsSGTPRPamaTPLRDLYRFRLADD-PHEYYLRLRPHLHEFLAGLS 245
Cdd:TIGR02251   1 KKTLVLDLDETLVH----------------------STFKMP---KVDADFKVPVLIDGkIIQVYVFKRPHVDEFLERVS 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023  246 SLFEMHIYTMGSRPYANKVAAIIDPDKRYFSERiLSRD----ESGSfHKKSLQRLFPcDQSMVVAIDDrgdvwgwadnvi 321
Cdd:TIGR02251  56 KWYELVIFTASLEEYADPVLDILDRGGKVISRR-LYREscvfTNGK-YVKDLSLVGK-DLSKVIIIDN------------ 120


                  ....*....
gi 909136023  322 rvHPYSYFL 330
Cdd:TIGR02251 121 --SPYSYSL 127
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 411-481 3.25e-09

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 53.52  E-value: 3.25e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909136023 411 CELVFSGIIPRHVNELEsdvwKLATSFGARCTSAVTKTTTHVVATR-SGTAKVRQAHAQGTTVVTPGWLFTS 481
Cdd:cd00027    1 LVICFSGLDDEEREELK----KLIEALGGKVSESLSSKVTHLIAKSpSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 431-490 8.25e-09

second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the second BRCT domain.


Pssm-ID: 349342 [Multi-domain]  Cd Length: 81  Bit Score: 53.00  E-value: 8.25e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909136023 431 WKLATSFGARCTSAVTKTTTHVVATRSGTAKVRQAHA-QGTTVVTPGWLFTSIAYWKRLEE 490
Cdd:cd17710   21 WAMVTFHGGKCQLNLDKKCTHLVTGKASGAKYECALKhEGIKIVTPDWVTDCIKAKTLLDE 81
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 404-482 1.34e-08

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 52.30  E-value: 1.34e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909136023  404 KRQVLAGCELVFSGIIPRHVNELEsdvwKLATSFGARCTSAVTKTTTHVVATRsGTAKVRQAHAQGTTVVTPGWLFTSI 482
Cdd:pfam00533   2 KEKLFSGKTFVITGLDGLERDELK----ELIEKLGGKVTDSLSKKTTHVIVEA-RTKKYLKAKELGIPIVTEEWLLDCI 75
BRCT smart00292
breast cancer carboxy-terminal domain;
407-482 1.72e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 48.91  E-value: 1.72e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909136023   407 VLAGCELVFSGIIPrhvNELESDVWKLATSFGARCTSAVT-KTTTHVVATRSGTAKVRQAHAQ--GTTVVTPGWLFTSI 482
Cdd:smart00292   3 LFKGKTFYITGSFD---KEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKLELLKAIalGIPIVKEEWLLDCL 78
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 446-495 3.85e-07

BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.


Pssm-ID: 349351 [Multi-domain]  Cd Length: 87  Bit Score: 48.33  E-value: 3.85e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 909136023 446 TKTTTHVVATRSGTAKVRQ-AHAQGTTVVTPGWLFTSIAYWKRLEEARFLV 495
Cdd:cd17719   37 RSRVTHIIATNLPGSKIKKlKKARNYKVVRPEWIVDSIKAGRLLPEAPYLL 87
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 428-477 4.53e-06

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 44.50  E-value: 4.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 909136023  428 SDVWKLATSFGARCTSAVTKTTTHVVATRSGTAKVRQAHAQGTTVVTPGW 477
Cdd:pfam12738  14 EGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT_XRCC1_rpt1 cd17725
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ...
 410-493 2.24e-05

First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar proteins; XRCC1 is a DNA repair protein that corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. It forms homodimers and interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB), DNA ligase III (LIG3), APTX, APLF, and APEX1. XRCC1 contains an N-terminal XRCC1-specific domain and two BRCT domains. This family corresponds to the first one.


Pssm-ID: 349357 [Multi-domain]  Cd Length: 80  Bit Score: 43.03  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023 410 GCELVFSGIiprhVNELESDVWKLATSFGARCTSAVTKTTTHVVATRSGTAKVRQAHAQGTTVVTPGWLFTSIAYWKRLE 489
Cdd:cd17725    1 GVVFVLSGF----QNPFRGELRDKALEMGAKYRPDWTADCTHLICAFANTPKYKQVKGAGGIIVSKEWILDCYKKKKRLP 76


                 ....
gi 909136023 490 EARF 493
Cdd:cd17725   77 WKRY 80
BRCT_PARP1 cd17747
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ...
 408-478 9.10e-05

BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism.


Pssm-ID: 349378 [Multi-domain]  Cd Length: 76  Bit Score: 41.36  E-value: 9.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909136023 408 LAGCELVFSGIIPRHVNELESDVWKLatsfGARCTSAVTKTTTHVVATR----SGTAKVRQAHAQGTTVVTPGWL 478
Cdd:cd17747    1 LTGMKFALIGKLSKSKDELKKLIEKL----GGKVASKVTKKVTLCISTKaeveKMSKKMKEAKEAGVPVVSEDFL 71
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 419-479 1.84e-04

sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the sixth BRCT domain.


Pssm-ID: 349359 [Multi-domain]  Cd Length: 75  Bit Score: 40.27  E-value: 1.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909136023 419 IPRHVNELESDVWKLATSFGARCTSAVTKTTTHVVA--TRSGTAK-VRQAHAQGTTVVTPGWLF 479
Cdd:cd17727    8 VSKKLSKRQGELNKIAASLGAEYRWTYDESCTHFIYqgKANDTNReYKSAKEQGKFIVSPHWLY 71
BRCT_Rad4_rpt1 cd17740
first BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar ...
 408-479 2.46e-04

first BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins; Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples the S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the first one.


Pssm-ID: 349371  Cd Length: 82  Bit Score: 40.15  E-value: 2.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909136023 408 LAGCELVFSGIIPRHvnelESDVWKLATSFGARCTSAVTKTTTHVVATRSGTAKVRQA--HAQGTTVVTPGWLF 479
Cdd:cd17740    3 LSGIVLCCTSIPAEQ----RTEIATKASKMGAAYTADLTSDVTHLVAGQVNTTKYKFAarSRPDIKVMTVEWVE 72
BRCT_Rad4_rpt2 cd17746
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ...
 425-493 5.11e-04

second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins; Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the second one.


Pssm-ID: 349377 [Multi-domain]  Cd Length: 91  Bit Score: 39.53  E-value: 5.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909136023 425 ELESDVWKLATSFGARCTSAVTKTTTHVVATRSGTAKVRQAHAQGTTVVTPGWLFTSIAYWKRLEEARF 493
Cdd:cd17746   20 PERSRIENYVLKHGGTFCPDLTRDVTHLIAGTSSGRKYEYALKWKINVVCVEWLWQSIQRNAVLEPQYF 88
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 407-485 8.58e-04

second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.


Pssm-ID: 349363 [Multi-domain]  Cd Length: 77  Bit Score: 38.68  E-value: 8.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909136023 407 VLAGCELVFSGIIPRHVNELESDVWKLatsfGARCTSAVTKTTTHVVATRSGTAKVRQAHAQGT-TVVTPGWLFTSIAYW 485
Cdd:cd17731    2 PFKGLVICVTGFDSEERKEIQQLVEQN----GGSYSPDLSKNCTHLIAGSPSGQKYEFARKWNSiHIVTPEWLYDSIEAG 77
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 410-486 1.72e-03

third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the third BRCT domain.


Pssm-ID: 349343  Cd Length: 81  Bit Score: 38.01  E-value: 1.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909136023 410 GCELVFSGIIPRHVNELESDVWKLATSFGARCTSAVTKTTTHVVATRSGTAKVRQAHAQGTTVVTPGWLFTSIAYWK 486
Cdd:cd17711    1 GCVFFIADYPEQMGDQEIATWKKVIEEHGGEVVDEYSPRVTHVICESQDSPEYQQALRDGKRVVTAYWLNDVLKRGK 77
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 413-482 1.81e-03

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 37.57  E-value: 1.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909136023 413 LVFSGIIPRHVNELESDVWKLatsFGARCTSAVTKTTTHVVA-TRSGTAKVRQAHAQGTTVVTPGWLFTSI 482
Cdd:cd17736    3 LVMTSVHSEEQELLESVVKKL---GGFRVEDSVTEKTTHVVVgSPRRTLNVLLGIARGCWILSPDWVLESL 70
BRCT_CHS5_like cd17742
BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed ...
 416-479 4.99e-03

BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed protein CAL3, is a component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. It is also involved in targeting FUS1 to sites of polarized growth.


Pssm-ID: 349373 [Multi-domain]  Cd Length: 77  Bit Score: 36.54  E-value: 4.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909136023 416 SGII----PRHVNELESDVWKLATSFGARCTSAVTKTTTHVVATRSGTAKVRQAHAQGTTVVTPGWLF 479
Cdd:cd17742    1 SGITvclgPLDPPESVDELEQCLERIGAKPTDRVAIDTTHFVCTVPSGPEYEKAKEMNIPIVRPEWLR 68
BRCT_DNA_ligase_like cd17748
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ...
 408-454 5.11e-03

BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also called NAD(+)-dependent polydeoxyribonucleotide synthase, catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.


Pssm-ID: 349379 [Multi-domain]  Cd Length: 76  Bit Score: 36.31  E-value: 5.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 909136023 408 LAGCELVFSGI---IPRhvneleSDVWKLATSFGARCTSAVTKTTTHVVA 454
Cdd:cd17748    1 LAGKTFVFTGTlssMSR------DEAEELIEALGGKVQSSVSKKTDYLVV 44
BRCT_PAXIP1_rpt5 cd17712
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 415-478 6.56e-03

fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the fifth BRCT domain.


Pssm-ID: 349344  Cd Length: 75  Bit Score: 36.06  E-value: 6.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909136023 415 FSGIIPRHVNELESDVWKLatsfGARCTSAVTKtTTHVVATR-SGTAKVRQAHAQGTTVVTPGWL 478
Cdd:cd17712    6 FTGFDPVQVRKLTKKVTIL----GGEVVESPQE-CTHLVAPKvSRTVKFLTAISVCKHIVTPEWL 65
 
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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