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Conserved domains on  [gi|71274172|ref|NP_001025041|]
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ankyrin repeat domain-containing protein SOWAHB [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
631-723 5.35e-14

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 5.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172 631 GYTALHWIAKHGDLRALQDLVS-GAkkagivlDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRLASrVNVRDSSGKKPWQ 709
Cdd:COG0666 153 GNTPLHLAAANGNLEIVKLLLEaGA-------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD-VNAKDNDGKTALD 224

                        90
                ....*....|....
gi 71274172 710 YLTSNTSGEIWQLL 723
Cdd:COG0666 225 LAAENGNLEIVKLL 238
CSB_WHD super family cl45559
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
 2-78 2.39e-05

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


The actual alignment was detected with superfamily member cd22254:

Pssm-ID: 439329  Cd Length: 72  Bit Score: 42.89  E-value: 2.39e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71274172   2 ARELSQEaLLDFLC-QAGGRVTNAALLSHFKsflrdPDASPSQhqhrRELFKGFVNSVAAVRQDPDGTKYVVLKRRYR 78
Cdd:cd22254   5 AEELLAD-IRDFLAfQAGGQATTDEIVDHFK-----DRLPPEQ----SALFKALLKQICTFERDPGGRGVWVLKPEFR 72
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
631-723 5.35e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 5.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172 631 GYTALHWIAKHGDLRALQDLVS-GAkkagivlDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRLASrVNVRDSSGKKPWQ 709
Cdd:COG0666 153 GNTPLHLAAANGNLEIVKLLLEaGA-------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD-VNAKDNDGKTALD 224

                        90
                ....*....|....
gi 71274172 710 YLTSNTSGEIWQLL 723
Cdd:COG0666 225 LAAENGNLEIVKLL 238
Ank_4 pfam13637
Ankyrin repeats (many copies);
631-690 3.84e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 3.84e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172   631 GYTALHWIAKHGDLRALQDLVsgAKKAgivlDVNVRSSCGYTPLHLAAIHGHQGVIKLLV 690
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLL--EKGA----DINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 631-713 6.38e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 6.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172  631 GYTALHWIAkHGDLRALQDLVSGAKKAGIvlDVNVRSSCGYTPLHLAAIHGHQ-GVIKLLVQRLAsRVNVRDSSGKKPWQ 709
Cdd:PHA03095  47 GKTPLHLYL-HYSSEKVKDIVRLLLEAGA--DVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGA-DVNAKDKVGRTPLH 122


                 ....*
gi 71274172  710 -YLTS 713
Cdd:PHA03095 123 vYLSG 127
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
 2-78 2.39e-05

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


Pssm-ID: 439329  Cd Length: 72  Bit Score: 42.89  E-value: 2.39e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71274172   2 ARELSQEaLLDFLC-QAGGRVTNAALLSHFKsflrdPDASPSQhqhrRELFKGFVNSVAAVRQDPDGTKYVVLKRRYR 78
Cdd:cd22254   5 AEELLAD-IRDFLAfQAGGQATTDEIVDHFK-----DRLPPEQ----SALFKALLKQICTFERDPGGRGVWVLKPEFR 72
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 670-695 3.39e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 3.39e-04
                           10        20
                   ....*....|....*....|....*.
gi 71274172    670 GYTPLHLAAIHGHQGVIKLLVQRLAS 695
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
631-723 5.35e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 5.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172 631 GYTALHWIAKHGDLRALQDLVS-GAkkagivlDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRLASrVNVRDSSGKKPWQ 709
Cdd:COG0666 153 GNTPLHLAAANGNLEIVKLLLEaGA-------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD-VNAKDNDGKTALD 224

                        90
                ....*....|....
gi 71274172 710 YLTSNTSGEIWQLL 723
Cdd:COG0666 225 LAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
631-725 4.29e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 4.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172 631 GYTALHWIAKHGDLRALQDLVsgakKAGIvlDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRLAsRVNVRDSSGKKPWQY 710
Cdd:COG0666 120 GETPLHLAAYNGNLEIVKLLL----EAGA--DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192

                        90
                ....*....|....*...
gi 71274172 711 LTSNTSGEIWQLL---GA 725
Cdd:COG0666 193 AAENGHLEIVKLLleaGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
622-710 1.45e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.13  E-value: 1.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172 622 LALHKDFLTGYTALHWIAKHGDLRALQDLVsgakKAGIvlDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRLASrVNVRD 701
Cdd:COG0666  78 ADINAKDDGGNTLLHAAARNGDLEIVKLLL----EAGA--DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD-VNAQD 150


                ....*....
gi 71274172 702 SSGKKPWQY 710
Cdd:COG0666 151 NDGNTPLHL 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
631-690 3.84e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 3.84e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172   631 GYTALHWIAKHGDLRALQDLVsgAKKAgivlDVNVRSSCGYTPLHLAAIHGHQGVIKLLV 690
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLL--EKGA----DINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
631-701 5.39e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 5.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71274172   631 GYTALHWIAKHGDLRALQDLVSGAkkagivlDVNVRSScGYTPLHLAAIHGHQGVIKLLVQRLASrVNVRD 701
Cdd:pfam12796  30 GRTALHLAAKNGHLEIVKLLLEHA-------DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGAD-INVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
635-698 7.51e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 7.51e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71274172   635 LHWIAKHGDLRALQDLVSGAKkagivlDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRLASRVN 698
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA------DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK 58
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
631-725 9.42e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 9.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172 631 GYTALHWIAKHGDLRALQDLVS-GAkkagivlDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRLASRVNVRDSSGKKPWQ 709
Cdd:COG0666 186 GETPLHLAAENGHLEIVKLLLEaGA-------DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                        90
                ....*....|....*.
gi 71274172 710 YLTSNTSGEIWQLLGA 725
Cdd:COG0666 259 AAAAGAALIVKLLLLA 274
Ank_5 pfam13857
Ankyrin repeats (many copies);
661-710 2.06e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 2.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 71274172   661 LDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRLASrVNVRDSSGKKPWQY 710
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD-LNLKDEEGLTALDL 55
PHA03095 PHA03095
ankyrin-like protein; Provisional
 631-713 6.38e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 6.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172  631 GYTALHWIAkHGDLRALQDLVSGAKKAGIvlDVNVRSSCGYTPLHLAAIHGHQ-GVIKLLVQRLAsRVNVRDSSGKKPWQ 709
Cdd:PHA03095  47 GKTPLHLYL-HYSSEKVKDIVRLLLEAGA--DVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGA-DVNAKDKVGRTPLH 122


                 ....*
gi 71274172  710 -YLTS 713
Cdd:PHA03095 123 vYLSG 127
PHA03095 PHA03095
ankyrin-like protein; Provisional
 631-707 1.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71274172  631 GYTALHWIAKHGDLRA--LQDLVSgakkAGIvlDVNVRSSCGYTPLHLAAIHGHQGVIKLLVqRLASRVNVRDSSGKKP 707
Cdd:PHA03095 222 GNTPLHSMATGSSCKRslVLPLLI----AGI--SINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTP 293
CSB_WHD cd22254
winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, ...
 2-78 2.39e-05

winged-helix domain (WHD) found in cockayne syndrome group B (CSB) and similar proteins; CSB, also called cockayne syndrome protein CSB, DNA excision repair protein ERCC-6, ERCC Excision Repair 6, or ATP-dependent helicase ERCC6, is involved in many DNA repair processes and is essential for transcription-coupled repair (TCR). It regulates DNA double-strand break (DSB) repair and checkpoint activation. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for TCR complex formation. CSB also regulates transcription and chromatin remodeling activities that are essential for neuronal differentiation and neuritogenesis. This model corresponds to the winged-helix domain (WHD) of CSB, which is involved in the recruitment of CSB to DSBs. The CSB WHD folds as a single globular domain, defining a class of ubiquitin-binding domains (UBDs) different from other UBD classes.


Pssm-ID: 439329  Cd Length: 72  Bit Score: 42.89  E-value: 2.39e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71274172   2 ARELSQEaLLDFLC-QAGGRVTNAALLSHFKsflrdPDASPSQhqhrRELFKGFVNSVAAVRQDPDGTKYVVLKRRYR 78
Cdd:cd22254   5 AEELLAD-IRDFLAfQAGGQATTDEIVDHFK-----DRLPPEQ----SALFKALLKQICTFERDPGGRGVWVLKPEFR 72
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 670-701 8.85e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 8.85e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 71274172   670 GYTPLHLAAIH-GHQGVIKLLVQRLASrVNVRD 701
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGAD-VNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 638-723 2.23e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172  638 IAKHGDLRALQDLVSGAKkagivlDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQrLASRVNVRDSSGKKPWQYLTSNTSG 717
Cdd:PTZ00322  89 LAASGDAVGARILLTGGA------DPNCRDYDGRTPLHIACANGHVQVVRVLLE-FGADPTLLDKDGKTPLELAEENGFR 161


                 ....*.
gi 71274172  718 EIWQLL 723
Cdd:PTZ00322 162 EVVQLL 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 670-695 3.39e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 3.39e-04
                           10        20
                   ....*....|....*....|....*.
gi 71274172    670 GYTPLHLAAIHGHQGVIKLLVQRLAS 695
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 633-710 4.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 4.65e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71274172  633 TALHWIAKHGDLRALQDLVS-GAkkagivlDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRlASRVNVRDSSGKKPWQY 710
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEyGA-------DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GAYANVKDNNGESPLHN 196
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 626-713 5.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172  626 KDFLTGYTALHWIAKHGDLRALQDLVS-GAKkagivldVNVRSSCGYTPLHLAAIHGHQGVIKLLVQRLASrVNVRDSSG 704
Cdd:PHA02878 163 KDRHKGNTALHYATENKDQRLTELLLSyGAN-------VNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS-TDARDKCG 234


                 ....*....
gi 71274172  705 KKPWQYLTS 713
Cdd:PHA02878 235 NTPLHISVG 243
Nucleoporin_N pfam08801
Nup133 N terminal like; Nup133 is a nucleoporin that is crucial for nuclear pore complex (NPC) ...
 564-741 1.23e-03

Nup133 N terminal like; Nup133 is a nucleoporin that is crucial for nuclear pore complex (NPC) biogenesis. The N terminal forms a seven-bladed beta propeller structure. This family now contains other sized nucleoporins, including Nup155, Nup8, Nuo132, Nup15 and Nup170.


Pssm-ID: 400932  Cd Length: 426  Bit Score: 41.99  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172   564 RHSLWVPSGEG--SAALAPHRTSEHKSSLVPLDAREHEWIVKLASGSWIQVWTLFWEDpqlalHKDFLTGYTALHWIAKH 641
Cdd:pfam08801 179 RSPSGGFSSLSiiPSVFGGGSEREEIVSLRVDPSRGERLLYTLTSKGVIQVWDLSSSG-----GSDLKSDADIRQIILEA 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172   642 GDLRALQDLVSGAKKagiVLDVNVRSSCGYTPLHLAAI---------------HGHQGVIKLLVQRLASRVNvrdssgkk 706
Cdd:pfam08801 254 ISLISTAPLASKSLK---ILDISPIDSDESSLLHLVAItsngvrlyyllstilLDSPSVLSLSSVRFPPRLN-------- 322

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 71274172   707 pwQYLTSNTSGEIWQLLGAPRGKPIFPVYPLVGSS 741
Cdd:pfam08801 323 --TYSSKLLEGKKKPRLLIPSYSPGTFLFVVFDSS 355
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 630-723 3.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172  630 TGYTALHWIAK--HGDLRALQDLVSgaKKAGI------------VLDVNVRSSCGYTPLHLAAIHGHQGVIKLLVQrLAS 695
Cdd:PHA03100 140 DGENLLHLYLEsnKIDLKILKLLID--KGVDInaknrvnyllsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD-LGA 216

                         90       100
                 ....*....|....*....|....*...
gi 71274172  696 RVNVRDSSGKKPWQYLTSNTSGEIWQLL 723
Cdd:PHA03100 217 NPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 631-710 3.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274172  631 GYTALHWIAKHGDLRALQDLVSGAKkagivlDVNVRSSCGYTPLHLAAIHgHQGVIKLLVQRlaSRVNVRDSSGKKPWQY 710
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGN------HIMNKCKNGFTPLHNAIIH-NRSAIELLINN--ASINDQDIDGSTPLHH 260
Ank_4 pfam13637
Ankyrin repeats (many copies);
670-723 6.28e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 6.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 71274172   670 GYTPLHLAAIHGHQGVIKLLVQRLASrVNVRDSSGKKPWQYLTSNTSGEIWQLL 723
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 631-682 8.28e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 8.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 71274172  631 GYTALHWIAKHGDLRALQDLVsgakKAGIvlDVNVRSSCGYTPLHLAAIHGH 682
Cdd:PHA03095 257 GQTPLHYAAVFNNPRACRRLI----ALGA--DINAVSSDGNTPLSLMVRNNN 302
 
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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