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Conserved domains on  [gi|1511289913|ref|NP_001265373|]
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ankyrin repeat and LEM domain-containing protein 1 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GIY-YIG_SF super family cl15257
GIY-YIG nuclease domain superfamily; The GIY-YIG nuclease domain superfamily includes a large ...
 424-507 5.08e-31

GIY-YIG nuclease domain superfamily; The GIY-YIG nuclease domain superfamily includes a large and diverse group of proteins involved in many cellular processes, such as class I homing GIY-YIG family endonucleases, prokaryotic nucleotide excision repair proteins UvrC and Cho, type II restriction enzymes, the endonuclease/reverse transcriptase of eukaryotic retrotransposable elements, and a family of eukaryotic enzymes that repair stalled replication forks. All of these members contain a conserved GIY-YIG nuclease domain that may serve as a scaffold for the coordination of a divalent metal ion required for catalysis of the phosphodiester bond cleavage. By combining with different specificity, targeting, or other domains, the GIY-YIG nucleases may perform different functions.


The actual alignment was detected with superfamily member cd10454:

Pssm-ID: 472790  Cd Length: 114  Bit Score: 116.63  E-value: 5.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913 424 SFTYLLLDPRETQDLPARAFSLTPAERLQTFIRAIFYVGKGTRARPYVHLWEALGHHGRSRKQgsrrSPTRSKGTAMEWW 503
Cdd:cd10454     1 SFNYLLLDPRVTRNLPSRARGLTPIETFQTFVSSIFYVGKGKRSRPYAHFYEALKQHNDKDKK----KGSRKLRRILDIW 76


                  ....
gi 1511289913 504 QAGH 507
Cdd:cd10454    77 NSGL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-128 4.18e-19

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913  22 AVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGAD 101
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK---LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178

                          90       100
                  ....*....|....*....|....*..
gi 1511289913 102 PALRDQDGLRPLDLALQQGHLECARVL 128
Cdd:COG0666   179 VNARDNDGETPLHLAAENGHLEIVKLL 205
 
Name Accession Description Interval E-value
GIY-YIG_COG3680_Meta cd10454
GIY-YIG domain of hypothetical proteins from Metazoa; Members of this family are functionally ...
 424-507 5.08e-31

GIY-YIG domain of hypothetical proteins from Metazoa; Members of this family are functionally uncharacterized hypothetical proteins from Metazoa. They have bacterial homologs that display sequence homology with the catalytic GIY-YIG domain of bacterial UvrC DNA repair proteins. However, unlike their bacterial relatives, these Metazoan proteins contain an N-terminal extension that includes the region of approximately 3-4 ankyrin repeats, unique motifs mediating protein-protein interactions. Some of them do have an additional LEM domain located between ankyrin repeats region and GIY-YIG domain. The LEM domain, found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding. The different domains composition suggests members in this subfamily might participate in interactions with multiple partners and imply some important cellular functions.


Pssm-ID: 198401  Cd Length: 114  Bit Score: 116.63  E-value: 5.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913 424 SFTYLLLDPRETQDLPARAFSLTPAERLQTFIRAIFYVGKGTRARPYVHLWEALGHHGRSRKQgsrrSPTRSKGTAMEWW 503
Cdd:cd10454     1 SFNYLLLDPRVTRNLPSRARGLTPIETFQTFVSSIFYVGKGKRSRPYAHFYEALKQHNDKDKK----KGSRKLRRILDIW 76


                  ....
gi 1511289913 504 QAGH 507
Cdd:cd10454    77 NSGL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-128 4.18e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913  22 AVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGAD 101
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK---LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178

                          90       100
                  ....*....|....*....|....*..
gi 1511289913 102 PALRDQDGLRPLDLALQQGHLECARVL 128
Cdd:COG0666   179 VNARDNDGETPLHLAAENGHLEIVKLL 205
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 62-128 2.23e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 2.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1511289913  62 LLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 128
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-128 2.38e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 2.38e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1511289913  56 LRCLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQgADPALRDqDGLRPLDLALQQGHLECARVL 128
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLL 80
 
Name Accession Description Interval E-value
GIY-YIG_COG3680_Meta cd10454
GIY-YIG domain of hypothetical proteins from Metazoa; Members of this family are functionally ...
 424-507 5.08e-31

GIY-YIG domain of hypothetical proteins from Metazoa; Members of this family are functionally uncharacterized hypothetical proteins from Metazoa. They have bacterial homologs that display sequence homology with the catalytic GIY-YIG domain of bacterial UvrC DNA repair proteins. However, unlike their bacterial relatives, these Metazoan proteins contain an N-terminal extension that includes the region of approximately 3-4 ankyrin repeats, unique motifs mediating protein-protein interactions. Some of them do have an additional LEM domain located between ankyrin repeats region and GIY-YIG domain. The LEM domain, found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding. The different domains composition suggests members in this subfamily might participate in interactions with multiple partners and imply some important cellular functions.


Pssm-ID: 198401  Cd Length: 114  Bit Score: 116.63  E-value: 5.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913 424 SFTYLLLDPRETQDLPARAFSLTPAERLQTFIRAIFYVGKGTRARPYVHLWEALGHHGRSRKQgsrrSPTRSKGTAMEWW 503
Cdd:cd10454     1 SFNYLLLDPRVTRNLPSRARGLTPIETFQTFVSSIFYVGKGKRSRPYAHFYEALKQHNDKDKK----KGSRKLRRILDIW 76


                  ....
gi 1511289913 504 QAGH 507
Cdd:cd10454    77 NSGL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-128 4.18e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913  22 AVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGAD 101
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK---LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178

                          90       100
                  ....*....|....*....|....*..
gi 1511289913 102 PALRDQDGLRPLDLALQQGHLECARVL 128
Cdd:COG0666   179 VNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-130 2.25e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.00  E-value: 2.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913  22 AVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGAD 101
Cdd:COG0666   135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK---LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                          90       100
                  ....*....|....*....|....*....
gi 1511289913 102 PALRDQDGLRPLDLALQQGHLECARVLQD 130
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-145 2.77e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913  22 AVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGAD 101
Cdd:COG0666   168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK---LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1511289913 102 PALRDQDGLRPLDLALQQGHLECARVLQDLDTRTRTRTRIGAET 145
Cdd:COG0666   245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-128 2.12e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 2.12e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1511289913  61 ALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 128
Cdd:COG0666    72 LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 62-128 2.23e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 2.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1511289913  62 LLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 128
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-128 2.38e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 2.38e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1511289913  56 LRCLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQgADPALRDqDGLRPLDLALQQGHLECARVL 128
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLL 80
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-128 7.37e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 7.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1511289913  77 LTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 128
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 11-130 7.67e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 7.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913  11 LRDALREEEPWAVEELLRCGADPNLVL-EDGAAAVHLAAGARHprgLRCLGALLRQGGDPNARSVEALTPLHVAAAWGCR 89
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKK---LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1511289913  90 RGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVLQD 130
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
80-128 9.43e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 9.43e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1511289913  80 LHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 128
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-130 2.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 2.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1511289913  56 LRCLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVLQD 130
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 23-121 8.98e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 8.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913  23 VEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRcLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADP 102
Cdd:PHA03095  205 VRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSL-VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI 283

                          90
                  ....*....|....*....
gi 1511289913 103 ALRDQDGLRPLDLALQQGH 121
Cdd:PHA03095  284 NAVSSDGNTPLSLMVRNNN 302
GIY-YIG_COG3680 cd10440
GIY-YIG domain of uncharacterized proteins from bacteria and their eukaryotic homologs; This ...
 427-491 1.57e-05

GIY-YIG domain of uncharacterized proteins from bacteria and their eukaryotic homologs; This family includes a group of functionally uncharacterized proteins from bacteria and their eukaryotic homologs which are present only in metazoa. These proteins might have nuclease activities and possibly be engaged in DNA repair or recombination, since they share sequence homology with the catalytic GIY-YIG domain of bacterial UvrC DNA repair proteins. Distinct from their prokaryotic relatives, the eukaryotic homologs contain an N-terminal extension that includes the region of approximately 3-4 ankyrin repeats, unique motifs mediating protein-protein interactions. Some of eukaryotic homologs do have an additional LEM domain located between ankyrin repeats region and GIY-YIG domain. The LEM domain, found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding. The different domain composition of the eukaryotic homologs suggests that they might participate in interactions with multiple partners and implies important cellular function.


Pssm-ID: 198387 [Multi-domain]  Cd Length: 94  Bit Score: 43.91  E-value: 1.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1511289913 427 YLLLDPRETQdlparafsltpaerlqtfiraIFYVGKGTRARPYVHLWEALGHHGRSRKQGSRRS 491
Cdd:cd10440     4 YALIDPRTGE---------------------VFYVGKGKGNRVFSHVKEALGEYENIKEKLSAKL 47
Ank_5 pfam13857
Ankyrin repeats (many copies);
62-116 1.94e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 1.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1511289913  62 LLRQGG-DPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLA 116
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
11-106 2.39e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289913  11 LRDALREEEPWAVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgaLLRQGGDPNARSvEALTPLHVAAAWGCRR 90
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK----LLLEHADVNLKD-NGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 1511289913  91 GLELLLSQGADPALRD 106
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 84-128 2.18e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 2.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1511289913  84 AAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 128
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVL 134
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-106 3.18e-03

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: 35.34  E-value: 3.18e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1511289913  78 TPLHVAAA-WGCRRGLELLLSQGADPALRD 106
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 59-128 4.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 4.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511289913  59 LGALLRQGGDPNARS-VEALTPLHVAAAwgCRRGLELLLSQGADPALRDQDGLRPLDLALQQGH-LECARVL 128
Cdd:PHA02878  251 LKLLLEHGVDVNAKSyILGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRIL 320
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 62-118 5.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.20  E-value: 5.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511289913  62 LLRQGGDPNARSVEA-LTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQ 118
Cdd:PHA02884   89 LIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
 
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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