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Conserved domains on  [gi|1511289864|ref|NP_001265374|]
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ankyrin repeat and LEM domain-containing protein 1 isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

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 ...
410-525 1.81e-67

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: 214.09  E-value: 1.81e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864 410 SFTYLLLDPRETQDLPARAFSLTPAERLQTFIRAIFYVGKGTRARPYVHLWEALGHHGrsRKQPHQACPKVRQILDIWAS 489
Cdd:cd10454     1 SFNYLLLDPRVTRNLPSRARGLTPIETFQTFVSSIFYVGKGKRSRPYAHFYEALKQHN--DKDKKKGSRKLRRILDIWNS 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1511289864 490 GCGVVSLHCFQHVVAVEAYTREACIVEALGIQTLTN 525
Cdd:cd10454    79 GLGVVSLHCFQNVIPVEAYTREAAMIEALGLSNLTN 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-114 2.28e-19

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 2.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864   2 RCGRRSRVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELL 81
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK---LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1511289864  82 LSQGADPALRDQDGLRPLDLALQQGHLECARVL 114
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLL 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 ...
410-525 1.81e-67

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: 214.09  E-value: 1.81e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864 410 SFTYLLLDPRETQDLPARAFSLTPAERLQTFIRAIFYVGKGTRARPYVHLWEALGHHGrsRKQPHQACPKVRQILDIWAS 489
Cdd:cd10454     1 SFNYLLLDPRVTRNLPSRARGLTPIETFQTFVSSIFYVGKGKRSRPYAHFYEALKQHN--DKDKKKGSRKLRRILDIWNS 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1511289864 490 GCGVVSLHCFQHVVAVEAYTREACIVEALGIQTLTN 525
Cdd:cd10454    79 GLGVVSLHCFQNVIPVEAYTREAAMIEALGLSNLTN 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-114 2.28e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 2.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864   2 RCGRRSRVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELL 81
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK---LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1511289864  82 LSQGADPALRDQDGLRPLDLALQQGHLECARVL 114
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-114 2.28e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 2.28e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1511289864  42 LRCLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQgADPALRDqDGLRPLDLALQQGHLECARVL 114
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
48-114 2.82e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 2.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1511289864  48 LLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 114
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
COG3680 COG3680
Uncharacterized protein, contains GIY-YIG domain [Function unknown];
413-530 6.07e-06

Uncharacterized protein, contains GIY-YIG domain [Function unknown];


Pssm-ID: 442896  Cd Length: 253  Bit Score: 47.81  E-value: 6.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864 413 YLLLDPREtqdlparafsltpaerlqtfiRAIFYVGKGTRARPYVHLWEALghhgrsrKQPHQACPKVRQILDIWASGCG 492
Cdd:COG3680    18 YALIDPRD---------------------NKPFYIGKGKGNRVFAHLREAI-------ASNESESAKLERIREIKKAGLD 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1511289864 493 VVSLHCFQHVVAVEAYTREACIVEALGI--QTLTNQKQGH 530
Cdd:COG3680    70 VEHYILRHGLDEKTAFEVEAALIDLLGIveAKLTNIVRGH 109
 
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 ...
410-525 1.81e-67

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: 214.09  E-value: 1.81e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864 410 SFTYLLLDPRETQDLPARAFSLTPAERLQTFIRAIFYVGKGTRARPYVHLWEALGHHGrsRKQPHQACPKVRQILDIWAS 489
Cdd:cd10454     1 SFNYLLLDPRVTRNLPSRARGLTPIETFQTFVSSIFYVGKGKRSRPYAHFYEALKQHN--DKDKKKGSRKLRRILDIWNS 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1511289864 490 GCGVVSLHCFQHVVAVEAYTREACIVEALGIQTLTN 525
Cdd:cd10454    79 GLGVVSLHCFQNVIPVEAYTREAAMIEALGLSNLTN 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-114 2.28e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 2.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864   2 RCGRRSRVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELL 81
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK---LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1511289864  82 LSQGADPALRDQDGLRPLDLALQQGHLECARVL 114
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
GIY-YIG_COG3680 cd10440
GIY-YIG domain of uncharacterized proteins from bacteria and their eukaryotic homologs; This ...
413-525 1.29e-18

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: 80.89  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864 413 YLLLDPRETQdlparafsltpaerlqtfiraIFYVGKGTRARPYVHLWEALGHHGRSRKQPhqaCPKVRQILDIWASGCG 492
Cdd:cd10440     4 YALIDPRTGE---------------------VFYVGKGKGNRVFSHVKEALGEYENIKEKL---SAKLQRIREILSAGLE 59
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1511289864 493 VVSLHCFQHVVAVEAYTREACIVEALG--IQTLTN 525
Cdd:cd10440    60 VEHYILRHGLDEVEAFEVEAALIDALGltLPGLTN 94
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-116 2.78e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.61  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864   4 GRRSRVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLS 83
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK---LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1511289864  84 QGADPALRDQDGLRPLDLALQQGHLECARVLQD 116
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-131 3.21e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864   9 VEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADP 88
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK---LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1511289864  89 ALRDQDGLRPLDLALQQGHLECARVLQDLDTRTRTRTRIGAET 131
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-114 2.01e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 2.01e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1511289864  47 ALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 114
Cdd:COG0666    72 LLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-114 2.28e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 2.28e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1511289864  42 LRCLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQgADPALRDqDGLRPLDLALQQGHLECARVL 114
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
48-114 2.82e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 2.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1511289864  48 LLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 114
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
63-114 1.42e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.42e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1511289864  63 LTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 114
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-114 9.06e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 9.06e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1511289864  66 LHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 114
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA02876 PHA02876
ankyrin repeat protein; Provisional
42-116 2.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 2.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1511289864  42 LRCLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVLQD 116
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232
COG3680 COG3680
Uncharacterized protein, contains GIY-YIG domain [Function unknown];
413-530 6.07e-06

Uncharacterized protein, contains GIY-YIG domain [Function unknown];


Pssm-ID: 442896  Cd Length: 253  Bit Score: 47.81  E-value: 6.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864 413 YLLLDPREtqdlparafsltpaerlqtfiRAIFYVGKGTRARPYVHLWEALghhgrsrKQPHQACPKVRQILDIWASGCG 492
Cdd:COG3680    18 YALIDPRD---------------------NKPFYIGKGKGNRVFAHLREAI-------ASNESESAKLERIREIKKAGLD 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1511289864 493 VVSLHCFQHVVAVEAYTREACIVEALGI--QTLTNQKQGH 530
Cdd:COG3680    70 VEHYILRHGLDEKTAFEVEAALIDLLGIveAKLTNIVRGH 109
PHA03095 PHA03095
ankyrin-like protein; Provisional
5-107 6.44e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 6.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864   5 RRSRVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRcLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQ 84
Cdd:PHA03095  201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSL-VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL 279
                          90       100
                  ....*....|....*....|...
gi 1511289864  85 GADPALRDQDGLRPLDLALQQGH 107
Cdd:PHA03095  280 GADINAVSSDGNTPLSLMVRNNN 302
PHA02875 PHA02875
ankyrin repeat protein; Provisional
4-116 9.56e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 9.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864   4 GRRSRVEELLRCGADPNLVL-EDGAAAVHLAAGARHprgLRCLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLL 82
Cdd:PHA02875   79 GDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKK---LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1511289864  83 SQGADPALRDQDGLRPLDLALQQGHLECARVLQD 116
Cdd:PHA02875  156 DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
Ank_5 pfam13857
Ankyrin repeats (many copies);
48-102 3.75e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1511289864  48 LLRQGG-DPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLA 102
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
9-92 7.93e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 7.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511289864   9 VEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRclgaLLRQGGDPNARSvEALTPLHVAAAWGCRRGLELLLSQGADP 88
Cdd:pfam12796  13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK----LLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87

                  ....
gi 1511289864  89 ALRD 92
Cdd:pfam12796  88 NVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
70-114 2.50e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 2.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1511289864  70 AAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVL 114
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVL 134
PHA02878 PHA02878
ankyrin repeat protein; Provisional
45-114 4.02e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 4.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511289864  45 LGALLRQGGDPNARS-VEALTPLHVAAAwgCRRGLELLLSQGADPALRDQDGLRPLDLALQQGH-LECARVL 114
Cdd:PHA02878  251 LKLLLEHGVDVNAKSyILGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRIL 320
PHA02884 PHA02884
ankyrin repeat protein; Provisional
48-104 5.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.20  E-value: 5.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1511289864  48 LLRQGGDPNARSVEA-LTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQ 104
Cdd:PHA02884   89 LIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
64-92 5.82e-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: 34.57  E-value: 5.82e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1511289864  64 TPLHVAAA-WGCRRGLELLLSQGADPALRD 92
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
 
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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