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Conserved domains on  [gi|432959303|ref|XP_004086249|]
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Fanconi anemia core complex-associated protein 24 [Oryzias latipes]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
XPF_nuclease_FAAP24 cd20076
XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also ...
 16-140 2.41e-55

XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also called Fanconi anemia core complex-associated protein 24, plays a role in DNA repair through recruitment of the Fanconi anemia (FA) core complex to damaged DNA. It regulates FANCD2 monoubiquitination upon DNA damage and induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. FAAP24 may possess a high affinity toward single-stranded DNA (ssDNA). The nuclease domain of FAAP24 lacks the catalytic motif. The FANCM/FAAP24 complex is related to XPF/MUS81 endonucleases but lacks endonucleolytic activity. It binds branched DNA structures containing ssDNA regions, such as splayed-arm and 3'-flap DNA structures, and anchors the FA core complex to chromatin in repairing DNA interstrand crosslinks.


:

Pssm-ID: 410852  Cd Length: 123  Bit Score: 172.00  E-value: 2.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303  16 GHVLCSGKWKDSALVRALRGaGLKILFENELHVADFLLPNKSSILYVSESDIIAGSSYRRKLVRYRNAsNRFQELVLVER 95
Cdd:cd20076    1 GHILVNEKWRGSELVKSLQG-KVKVIFEDGLGVVDFYPSNDCAVIYISEADLVAGNGYKRKLVKLRKA-NYLRGIVIAEK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 432959303  96 TGLSEQYFGSLQRFVVLELGLPLLPVGGQTEASQLIAQMVQADGR 140
Cdd:cd20076   79 TPMSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVNEETK 123
UvrC super family cl33836
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
162-209 1.74e-09

Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0322:

Pssm-ID: 440091 [Multi-domain]  Cd Length: 603  Bit Score: 56.67  E-value: 1.74e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 432959303 162 QIPGVGRVKALALLQHFSSIQQLCSAAPEQLEPVVG--QAVAQQIHSFFH 209
Cdd:COG0322  552 EIPGIGPKRRKALLKHFGSLKAIKEASVEELAAVPGisKKLAEAIYEYLH 601
 
Name Accession Description Interval E-value
XPF_nuclease_FAAP24 cd20076
XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also ...
 16-140 2.41e-55

XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also called Fanconi anemia core complex-associated protein 24, plays a role in DNA repair through recruitment of the Fanconi anemia (FA) core complex to damaged DNA. It regulates FANCD2 monoubiquitination upon DNA damage and induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. FAAP24 may possess a high affinity toward single-stranded DNA (ssDNA). The nuclease domain of FAAP24 lacks the catalytic motif. The FANCM/FAAP24 complex is related to XPF/MUS81 endonucleases but lacks endonucleolytic activity. It binds branched DNA structures containing ssDNA regions, such as splayed-arm and 3'-flap DNA structures, and anchors the FA core complex to chromatin in repairing DNA interstrand crosslinks.


Pssm-ID: 410852  Cd Length: 123  Bit Score: 172.00  E-value: 2.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303  16 GHVLCSGKWKDSALVRALRGaGLKILFENELHVADFLLPNKSSILYVSESDIIAGSSYRRKLVRYRNAsNRFQELVLVER 95
Cdd:cd20076    1 GHILVNEKWRGSELVKSLQG-KVKVIFEDGLGVVDFYPSNDCAVIYISEADLVAGNGYKRKLVKLRKA-NYLRGIVIAEK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 432959303  96 TGLSEQYFGSLQRFVVLELGLPLLPVGGQTEASQLIAQMVQADGR 140
Cdd:cd20076   79 TPMSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVNEETK 123
PND pfam17949
FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the ...
 14-136 5.71e-52

FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the FANCM protein. This domain is part of the PD(D/E)XK superfamily but does not appear to have a full set of catalytic residues.


Pssm-ID: 375443  Cd Length: 125  Bit Score: 163.39  E-value: 5.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303   14 PYGHVLCSGKWKDSALVRALRGaGLKILFENELHVADFLLPNKSSILYVSESDIIAGSSYRRKLVRYRNASNrFQELVLV 93
Cdd:pfam17949   5 PLGHILCSEKWRNSSLVQILKD-KIKIIFEDRLGVVDFHPSNDTAIIYISEADIIAGNGYKRRLVKLRNANV-FQGIVLA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 432959303   94 ERTGLSEQYFGSLQRFVVLELGLPLLPVGGQTEASQLIAQMVQ 136
Cdd:pfam17949  83 EKTTLSEQYFSALQKFAVLELGLVLLPVLNQTEAADLIIQLVS 125
MUS81 COG1948
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
25-209 1.25e-10

ERCC4-type crossover junction endonuclease [Replication, recombination and repair];


Pssm-ID: 441551 [Multi-domain]  Cd Length: 214  Bit Score: 58.65  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303  25 KDSALVRALRGAGLKILFENeLHVADFLLPNKSSILYVSESDIIAGSSYRRKLVRYRNASNRFQE-LVLVERTGLSEQYF 103
Cdd:COG1948   11 KNSGVPRLLSRLGVEVRVKT-LEVGDYVVSDRVAVERKTVRDFVNSLIDGRLFEQASRLAEAYERpVLIIEGDLLYEERN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303 104 GSLQRF------VVLELGLPLLPVGGQTEASQLIAQMV---QADGRENIFRRS--SCRLLDPLVLALVQQIPGVGRVKAL 172
Cdd:COG1948   90 IHPNAIrgalasLALDFGIPVLPTRDAEDTAELLVTLArreQEEEKREVSLHGkkKPKTLREQQLYVVESLPGIGPKLAR 169

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 432959303 173 ALLQHFSSIQQLCSAAPEQLEPV--VGQAVAQQIHSFFH 209
Cdd:COG1948  170 RLLEHFGSVEAVFNASEEELMKVegIGEKTAERIREVLD 208
UvrC COG0322
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
162-209 1.74e-09

Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440091 [Multi-domain]  Cd Length: 603  Bit Score: 56.67  E-value: 1.74e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 432959303 162 QIPGVGRVKALALLQHFSSIQQLCSAAPEQLEPVVG--QAVAQQIHSFFH 209
Cdd:COG0322  552 EIPGIGPKRRKALLKHFGSLKAIKEASVEELAAVPGisKKLAEAIYEYLH 601
uvrC PRK00558
excinuclease ABC subunit UvrC;
162-209 6.48e-09

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 54.74  E-value: 6.48e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 432959303 162 QIPGVGRVKALALLQHFSSIQQLCSAAPEQLE--PVVGQAVAQQIHSFFH 209
Cdd:PRK00558 547 DIPGIGPKRRKALLKHFGSLKAIKEASVEELAkvPGISKKLAEAIYEALH 596
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 163-209 7.51e-08

Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


Pssm-ID: 432812 [Multi-domain]  Cd Length: 64  Bit Score: 47.52  E-value: 7.51e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 432959303  163 IPGVGRVKALALLQHFSSIQQLCSAAPEQLEPV--VGQAVAQQIHSFFH 209
Cdd:pfam12826   8 IRHVGETTAKLLARRFGSLDALAEASLEELLEVddIGPEIAQSIVEFFA 56
PRK13766 PRK13766
Hef nuclease; Provisional
 26-204 1.66e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 38.70  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303  26 DSALVRALRGAGLKILFENeLHVADFLLPNKSSILYVSESD----IIAGSSYRRklvrYRNASNRFQELVLVERTGLSEQ 101
Cdd:PRK13766 573 RSNVARHLKRLGAEVELKT-LEVGDYVVSDRVAVERKTAEDfvdsIIDRRLFEQ----VKDLKRAYERPVLIIEGDLYTI 647

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303 102 YF-------GSLQRfVVLELGLPLLPVGGQTEASQLIAQMVQadgRENIFRRSSCRL--------LDPLVLALVQQIPGV 166
Cdd:PRK13766 648 RNihpnairGALAS-IAVDFGIPILFTRDEEETADLLKVIAK---REQEEEKREVSVhgekkamtLKEQQEYIVESLPDV 723

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 432959303 167 GRVKALALLQHFSSIQQLCSAAPEQLEPV--VGQAVAQQI 204
Cdd:PRK13766 724 GPVLARNLLEHFGSVEAVMTASEEELMEVegIGEKTAKRI 763
 
Name Accession Description Interval E-value
XPF_nuclease_FAAP24 cd20076
XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also ...
 16-140 2.41e-55

XPF-like nuclease domain of Fanconi anemia associated protein 24 kDa (FAAP24); FAAP24, also called Fanconi anemia core complex-associated protein 24, plays a role in DNA repair through recruitment of the Fanconi anemia (FA) core complex to damaged DNA. It regulates FANCD2 monoubiquitination upon DNA damage and induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. FAAP24 may possess a high affinity toward single-stranded DNA (ssDNA). The nuclease domain of FAAP24 lacks the catalytic motif. The FANCM/FAAP24 complex is related to XPF/MUS81 endonucleases but lacks endonucleolytic activity. It binds branched DNA structures containing ssDNA regions, such as splayed-arm and 3'-flap DNA structures, and anchors the FA core complex to chromatin in repairing DNA interstrand crosslinks.


Pssm-ID: 410852  Cd Length: 123  Bit Score: 172.00  E-value: 2.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303  16 GHVLCSGKWKDSALVRALRGaGLKILFENELHVADFLLPNKSSILYVSESDIIAGSSYRRKLVRYRNAsNRFQELVLVER 95
Cdd:cd20076    1 GHILVNEKWRGSELVKSLQG-KVKVIFEDGLGVVDFYPSNDCAVIYISEADLVAGNGYKRKLVKLRKA-NYLRGIVIAEK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 432959303  96 TGLSEQYFGSLQRFVVLELGLPLLPVGGQTEASQLIAQMVQADGR 140
Cdd:cd20076   79 TPMSEQYFPALQKFVVLELGLVLLPVTSQSEAAQLLIQMVNEETK 123
PND pfam17949
FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the ...
 14-136 5.71e-52

FANCM pseudonuclease domain; This entry represents the pseudonuclease domain (PND) from the FANCM protein. This domain is part of the PD(D/E)XK superfamily but does not appear to have a full set of catalytic residues.


Pssm-ID: 375443  Cd Length: 125  Bit Score: 163.39  E-value: 5.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303   14 PYGHVLCSGKWKDSALVRALRGaGLKILFENELHVADFLLPNKSSILYVSESDIIAGSSYRRKLVRYRNASNrFQELVLV 93
Cdd:pfam17949   5 PLGHILCSEKWRNSSLVQILKD-KIKIIFEDRLGVVDFHPSNDTAIIYISEADIIAGNGYKRRLVKLRNANV-FQGIVLA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 432959303   94 ERTGLSEQYFGSLQRFVVLELGLPLLPVGGQTEASQLIAQMVQ 136
Cdd:pfam17949  83 EKTTLSEQYFSALQKFAVLELGLVLLPVLNQTEAADLIIQLVS 125
MUS81 COG1948
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
25-209 1.25e-10

ERCC4-type crossover junction endonuclease [Replication, recombination and repair];


Pssm-ID: 441551 [Multi-domain]  Cd Length: 214  Bit Score: 58.65  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303  25 KDSALVRALRGAGLKILFENeLHVADFLLPNKSSILYVSESDIIAGSSYRRKLVRYRNASNRFQE-LVLVERTGLSEQYF 103
Cdd:COG1948   11 KNSGVPRLLSRLGVEVRVKT-LEVGDYVVSDRVAVERKTVRDFVNSLIDGRLFEQASRLAEAYERpVLIIEGDLLYEERN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303 104 GSLQRF------VVLELGLPLLPVGGQTEASQLIAQMV---QADGRENIFRRS--SCRLLDPLVLALVQQIPGVGRVKAL 172
Cdd:COG1948   90 IHPNAIrgalasLALDFGIPVLPTRDAEDTAELLVTLArreQEEEKREVSLHGkkKPKTLREQQLYVVESLPGIGPKLAR 169

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 432959303 173 ALLQHFSSIQQLCSAAPEQLEPV--VGQAVAQQIHSFFH 209
Cdd:COG1948  170 RLLEHFGSVEAVFNASEEELMKVegIGEKTAERIREVLD 208
UvrC COG0322
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
162-209 1.74e-09

Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440091 [Multi-domain]  Cd Length: 603  Bit Score: 56.67  E-value: 1.74e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 432959303 162 QIPGVGRVKALALLQHFSSIQQLCSAAPEQLEPVVG--QAVAQQIHSFFH 209
Cdd:COG0322  552 EIPGIGPKRRKALLKHFGSLKAIKEASVEELAAVPGisKKLAEAIYEYLH 601
uvrC PRK00558
excinuclease ABC subunit UvrC;
162-209 6.48e-09

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 54.74  E-value: 6.48e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 432959303 162 QIPGVGRVKALALLQHFSSIQQLCSAAPEQLE--PVVGQAVAQQIHSFFH 209
Cdd:PRK00558 547 DIPGIGPKRRKALLKHFGSLKAIKEASVEELAkvPGISKKLAEAIYEALH 596
HHH_2 pfam12826
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ...
 163-209 7.51e-08

Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


Pssm-ID: 432812 [Multi-domain]  Cd Length: 64  Bit Score: 47.52  E-value: 7.51e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 432959303  163 IPGVGRVKALALLQHFSSIQQLCSAAPEQLEPV--VGQAVAQQIHSFFH 209
Cdd:pfam12826   8 IRHVGETTAKLLARRFGSLDALAEASLEELLEVddIGPEIAQSIVEFFA 56
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
163-209 6.43e-07

NAD-dependent DNA ligase [Replication, recombination and repair];


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 48.87  E-value: 6.43e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 432959303 163 IPGVGRVKALALLQHFSSIQQLCSAAPEQLEPV--VGQAVAQQIHSFFH 209
Cdd:COG0272  517 IRHVGETTAKLLARHFGSLDALMAASEEELAAVdgIGPVVAESIVEFFA 565
XPF_nuclease-like cd19940
nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap ...
 17-136 1.43e-06

nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap endonuclease that act upon 3'-flap structures and involved in DNA repair pathways that are necessary for the removal of UV-light-induced DNA lesions and cross-links between DNA strands. Family members exist either as heterodimers or as homodimers in their functionally competent states which consist of a catalytic and a noncatalytic subunit. The catalytic subunits have a DX(n)RKX(3)D motif. This motif is required for metal-dependent endonuclease activity but not for DNA junction binding. The equivalent regions of the noncatalytic subunits (ERCC1, EME1, and FAAP24) have diverged. The noncatalytic subunits have roles such as binding ssDNA or an ability to target the endonuclease to defined DNA structures or sites of DNA damage.


Pssm-ID: 410849 [Multi-domain]  Cd Length: 126  Bit Score: 45.84  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303  17 HVLCSGKWKDSALVRALRGAGLKILFEnELHVADFLLPNKSSILYVSESDIIAG---SSYRRKLVRYRNASNRFQELVLV 93
Cdd:cd19940    1 SIVVDPRERRSELLSELQRLGVQVEFE-DLAVGDYVLSNRTCVERKSLSDLVSSinkGRLREQLQRLTRKFERRVLLVEK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 432959303  94 ERT-----GLSEQYFGSLQRFVVLeLGLPLLPVGGQTEASQLIAQMVQ 136
Cdd:cd19940   80 DRSkfrsmVSSVQALSALTKLQLL-TGIRLLIVASPKETADLLEELTQ 126
uvrC PRK14666
excinuclease ABC subunit C; Provisional
 160-205 8.34e-05

excinuclease ABC subunit C; Provisional


Pssm-ID: 237782 [Multi-domain]  Cd Length: 694  Bit Score: 42.57  E-value: 8.34e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 432959303 160 VQQIPGVGRVKALALLQHFSSIQQLCSAAPEQLE--PVVGQAVAQQIH 205
Cdd:PRK14666 639 LQRVEGIGPATARLLWERFGSLQAMAAAGEEGLAavPGIGPARAAALH 686
HHH_5 pfam14520
Helix-hairpin-helix domain;
159-204 2.28e-04

Helix-hairpin-helix domain;


Pssm-ID: 434010 [Multi-domain]  Cd Length: 57  Bit Score: 37.85  E-value: 2.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 432959303  159 LVQQIPGVGRVKALALLQH-FSSIQQLCSAAPEQLE--PVVGQAVAQQI 204
Cdd:pfam14520   3 ELLSISGIGPKTALALLSAgIGTVEDLAEADVDELAeiPGIGEKTAQRI 51
Smf COG0758
Predicted Rossmann fold nucleotide-binding protein DprA/Smf involved in DNA uptake ...
 157-209 3.51e-04

Predicted Rossmann fold nucleotide-binding protein DprA/Smf involved in DNA uptake [Replication, recombination and repair];


Pssm-ID: 440521 [Multi-domain]  Cd Length: 360  Bit Score: 40.45  E-value: 3.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 432959303 157 LALvQQIPGVGRVKALALLQHFSSIQQLCSAAPEQLEPVV-GQAVAQQIHSFFH 209
Cdd:COG0758    8 LAL-SRVPGVGPVTLRRLLAHFGSAEAALEALPSELARLGlGEKAAEAIRARPD 60
PRK13766 PRK13766
Hef nuclease; Provisional
 26-204 1.66e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 38.70  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303  26 DSALVRALRGAGLKILFENeLHVADFLLPNKSSILYVSESD----IIAGSSYRRklvrYRNASNRFQELVLVERTGLSEQ 101
Cdd:PRK13766 573 RSNVARHLKRLGAEVELKT-LEVGDYVVSDRVAVERKTAEDfvdsIIDRRLFEQ----VKDLKRAYERPVLIIEGDLYTI 647

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432959303 102 YF-------GSLQRfVVLELGLPLLPVGGQTEASQLIAQMVQadgRENIFRRSSCRL--------LDPLVLALVQQIPGV 166
Cdd:PRK13766 648 RNihpnairGALAS-IAVDFGIPILFTRDEEETADLLKVIAK---REQEEEKREVSVhgekkamtLKEQQEYIVESLPDV 723

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 432959303 167 GRVKALALLQHFSSIQQLCSAAPEQLEPV--VGQAVAQQI 204
Cdd:PRK13766 724 GPVLARNLLEHFGSVEAVMTASEEELMEVegIGEKTAKRI 763
 
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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