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Conserved domains on  [gi|189181677|ref|NP_766344|]
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ankyrin repeat and LEM domain-containing protein 1 isoform 1 [Mus musculus]

Protein Classification

LEM and GIY-YIG_COG3680_Meta domain-containing protein( domain architecture ID 10250082)

LEM and GIY-YIG_COG3680_Meta domain-containing protein

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 ...
 372-484 1.73e-61

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: 197.52  E-value: 1.73e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677 372 SFTYLLLDPRLTKDLPARASSLTLAECLQCFVRAIFYVGKGTRARPDAHLWEAFGYHDQPR-KQVCPKVRRILDIWASGR 450
Cdd:cd10454    1 SFNYLLLDPRVTRNLPSRARGLTPIETFQTFVSSIFYVGKGKRSRPYAHFYEALKQHNDKDkKKGSRKLRRILDIWNSGL 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 189181677 451 GIISLHCFQHVVAMEAYTREACLLDALGLQTLTN 484
Cdd:cd10454   81 GVVSLHCFQNVIPVEAYTREAAMIEALGLSNLTN 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-130 1.05e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  26 LLRLGADPNLVLDDGAAavhlaarashprALH---------CLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLL 96
Cdd:COG0666  139 LLEAGADVNAQDNDGNT------------PLHlaaangnleIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110
                 ....*....|....*....|....*....|....
gi 189181677  97 SRGGDPTLRDQDGLRPLDWALQQRHHNCARVLQE 130
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
LEM super family cl02649
LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner ...
 285-322 1.32e-07

LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner nuclear membrane protein Man1 and similar proteins; The family corresponds to a group of inner nuclear membrane proteins containing LEM domain. Emerin occurs in four phosphorylated forms and plays a role in cell cycle-dependent events. It is absent from the inner nuclear membrane in most patients with X-linked muscular dystrophy. Emerin interacts with A-type and B-type lamins. Man1, also termed LEM domain-containing protein 3 (LEMD3) is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and post-mitotic reassembly. Some LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are non-membrane nuclear polypeptides. This family also contains LEM domain-containing protein LEMP-1 and LEM2. LEMP-1, also termed cancer/testis antigen 50 (CT50), is encoded by LEMD1, a novel testis-specific gene expressed in colorectal cancers. LEMP-1 may function as a cancer-testis antigen for immunotherapy of colorectal carcinoma (CRC). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization while its binding to lamin C plays an important role in the organization of lamin A/C complexes. Some uncharacterized LEM domain-containing proteins are also included in this family. Unlike other family members, these harbor an ankyrin repeat region that may mediate protein-protein interactions.


The actual alignment was detected with superfamily member cd12943:

Pssm-ID: 470643  Cd Length: 38  Bit Score: 47.91  E-value: 1.32e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 189181677 285 MSDLQLLQALRALGYSPGPVTPFTRGHYLRRLQEAQAS 322
Cdd:cd12943    1 LSDLDLLRGLRALGESPGPITPFTRRVYLRRLEELQRA 38
 
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 ...
 372-484 1.73e-61

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: 197.52  E-value: 1.73e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677 372 SFTYLLLDPRLTKDLPARASSLTLAECLQCFVRAIFYVGKGTRARPDAHLWEAFGYHDQPR-KQVCPKVRRILDIWASGR 450
Cdd:cd10454    1 SFNYLLLDPRVTRNLPSRARGLTPIETFQTFVSSIFYVGKGKRSRPYAHFYEALKQHNDKDkKKGSRKLRRILDIWNSGL 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 189181677 451 GIISLHCFQHVVAMEAYTREACLLDALGLQTLTN 484
Cdd:cd10454   81 GVVSLHCFQNVIPVEAYTREAAMIEALGLSNLTN 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-130 1.05e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  26 LLRLGADPNLVLDDGAAavhlaarashprALH---------CLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLL 96
Cdd:COG0666  139 LLEAGADVNAQDNDGNT------------PLHlaaangnleIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110
                 ....*....|....*....|....*....|....
gi 189181677  97 SRGGDPTLRDQDGLRPLDWALQQRHHNCARVLQE 130
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 60-155 3.21e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  60 RMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVLQELDTPTQPDE 139
Cdd:PTZ00322  99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178

                         90
                 ....*....|....*.
gi 189181677 140 TREPTETFHVAQGSFE 155
Cdd:PTZ00322 179 ANAKPDSFTGKPPSLE 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-128 8.77e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.81  E-value: 8.77e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189181677   56 LHCLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRgGDPTLRDqDGLRPLDWALQQRHHNCARVL 128
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLL 80
LEM_ANKL1 cd12943
LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 1 ...
 285-322 1.32e-07

LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 1 (ANKL1); The family includes ANKL1, also termed ankyrin repeat domain-containing protein 41 (ANKRD41), or LEM-domain containing protein 3 (LEM3), and similar proteins. Although their biological roles remain unclear, the family members contain an N-terminal ankyrin repeat region, LEM domain and C-terminal GIY-YIG nuclease domain. The ankyrin repeats are unique motifs mediating protein-protein interactions. The LEM domain, mainly found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding.


Pssm-ID: 240590  Cd Length: 38  Bit Score: 47.91  E-value: 1.32e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 189181677 285 MSDLQLLQALRALGYSPGPVTPFTRGHYLRRLQEAQAS 322
Cdd:cd12943    1 LSDLDLLRGLRALGESPGPITPFTRRVYLRRLEELQRA 38
COG3680 COG3680
Uncharacterized protein, contains GIY-YIG domain [Function unknown];
375-490 2.00e-07

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


Pssm-ID: 442896  Cd Length: 253  Bit Score: 52.43  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677 375 YLLLDPRltkdlparassltlaeclqcfVRAIFYVGKGTRARPDAHLWEAFGYHDQPRkqvcPKVRRILDIWASGRGIIS 454
Cdd:COG3680   18 YALIDPR---------------------DNKPFYIGKGKGNRVFAHLREAIASNESES----AKLERIREIKKAGLDVEH 72

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 189181677 455 LHCFQHVVAMEAYTREACLLDALGL--QTLTNQKQGHY 490
Cdd:COG3680   73 YILRHGLDEKTAFEVEAALIDLLGIveAKLTNIVRGHG 110
 
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 ...
 372-484 1.73e-61

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: 197.52  E-value: 1.73e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677 372 SFTYLLLDPRLTKDLPARASSLTLAECLQCFVRAIFYVGKGTRARPDAHLWEAFGYHDQPR-KQVCPKVRRILDIWASGR 450
Cdd:cd10454    1 SFNYLLLDPRVTRNLPSRARGLTPIETFQTFVSSIFYVGKGKRSRPYAHFYEALKQHNDKDkKKGSRKLRRILDIWNSGL 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 189181677 451 GIISLHCFQHVVAMEAYTREACLLDALGLQTLTN 484
Cdd:cd10454   81 GVVSLHCFQNVIPVEAYTREAAMIEALGLSNLTN 114
GIY-YIG_COG3680 cd10440
GIY-YIG domain of uncharacterized proteins from bacteria and their eukaryotic homologs; This ...
 375-484 4.59e-22

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: 90.52  E-value: 4.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677 375 YLLLDPRltkdlparassltlaeclqcfVRAIFYVGKGTRARPDAHLWEAFGYHDQPRKQVCPKVRRILDIWASGRGIIS 454
Cdd:cd10440    4 YALIDPR---------------------TGEVFYVGKGKGNRVFSHVKEALGEYENIKEKLSAKLQRIREILSAGLEVEH 62

                         90       100       110
                 ....*....|....*....|....*....|..
gi 189181677 455 LHCFQHVVAMEAYTREACLLDALG--LQTLTN 484
Cdd:cd10440   63 YILRHGLDEVEAFEVEAALIDALGltLPGLTN 94
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-130 1.05e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  26 LLRLGADPNLVLDDGAAavhlaarashprALH---------CLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLL 96
Cdd:COG0666  139 LLEAGADVNAQDNDGNT------------PLHlaaangnleIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         90       100       110
                 ....*....|....*....|....*....|....
gi 189181677  97 SRGGDPTLRDQDGLRPLDWALQQRHHNCARVLQE 130
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-128 2.46e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.75  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  26 LLRLGADPNLVLDDGAAAVHLAARASHPRALhclRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLR 105
Cdd:COG0666   73 LLAAGADINAKDDGGNTLLHAAARNGDLEIV---KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149

                         90       100
                 ....*....|....*....|...
gi 189181677 106 DQDGLRPLDWALQQRHHNCARVL 128
Cdd:COG0666  150 DNDGNTPLHLAAANGNLEIVKLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-131 3.10e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  26 LLRLGADPNLVLDDGAaavhlaarashpRALHC---------LRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLL 96
Cdd:COG0666  172 LLEAGADVNARDNDGE------------TPLHLaaenghleiVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 189181677  97 SRGGDPTLRDQDGLRPLDWALQQRHHNCARVLQEL 131
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 60-155 3.21e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  60 RMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVLQELDTPTQPDE 139
Cdd:PTZ00322  99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178

                         90
                 ....*....|....*.
gi 189181677 140 TREPTETFHVAQGSFE 155
Cdd:PTZ00322 179 ANAKPDSFTGKPPSLE 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-128 8.77e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.81  E-value: 8.77e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189181677   56 LHCLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRgGDPTLRDqDGLRPLDWALQQRHHNCARVL 128
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLL 80
LEM_ANKL1 cd12943
LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 1 ...
 285-322 1.32e-07

LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 1 (ANKL1); The family includes ANKL1, also termed ankyrin repeat domain-containing protein 41 (ANKRD41), or LEM-domain containing protein 3 (LEM3), and similar proteins. Although their biological roles remain unclear, the family members contain an N-terminal ankyrin repeat region, LEM domain and C-terminal GIY-YIG nuclease domain. The ankyrin repeats are unique motifs mediating protein-protein interactions. The LEM domain, mainly found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding.


Pssm-ID: 240590  Cd Length: 38  Bit Score: 47.91  E-value: 1.32e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 189181677 285 MSDLQLLQALRALGYSPGPVTPFTRGHYLRRLQEAQAS 322
Cdd:cd12943    1 LSDLDLLRGLRALGESPGPITPFTRRVYLRRLEELQRA 38
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-128 1.91e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.65  E-value: 1.91e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  59 LRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVL 128
Cdd:COG0666   70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
COG3680 COG3680
Uncharacterized protein, contains GIY-YIG domain [Function unknown];
375-490 2.00e-07

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


Pssm-ID: 442896  Cd Length: 253  Bit Score: 52.43  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677 375 YLLLDPRltkdlparassltlaeclqcfVRAIFYVGKGTRARPDAHLWEAFGYHDQPRkqvcPKVRRILDIWASGRGIIS 454
Cdd:COG3680   18 YALIDPR---------------------DNKPFYIGKGKGNRVFAHLREAIASNESES----AKLERIREIKKAGLDVEH 72

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 189181677 455 LHCFQHVVAMEAYTREACLLDALGL--QTLTNQKQGHY 490
Cdd:COG3680   73 YILRHGLDEKTAFEVEAALIDLLGIveAKLTNIVRGHG 110
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-128 3.20e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  26 LLRLGADPNLVLDDGAAAVHLAARASHPRALHcLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLR 105
Cdd:PHA03095 208 LIRAGCDPAATDMLGNTPLHSMATGSSCKRSL-VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286

                         90       100
                 ....*....|....*....|...
gi 189181677 106 DQDGLRPLDWALqqrHHNCARVL 128
Cdd:PHA03095 287 SSDGNTPLSLMV---RNNNGRAV 306
Ank_2 pfam12796
Ankyrin repeats (3 copies);
26-106 5.78e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 5.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677   26 LLRLGADPNLVLDDGAAavhlaarashprALH---------CLRMLLRwGADPNARSaEGLTPVHVAAAWGCCGALELLL 96
Cdd:pfam12796  16 LLENGADANLQDKNGRT------------ALHlaaknghleIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 189181677   97 SRGGDPTLRD 106
Cdd:pfam12796  82 EKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
81-128 2.90e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 2.90e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 189181677   81 HVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVL 128
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-121 3.34e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 3.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189181677  61 MLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRH 121
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
76-128 1.85e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 1.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 189181677   76 GLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVL 128
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-116 2.91e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 189181677   67 ADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWA 116
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 56-138 3.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  56 LHCLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVLqeLDTPT 135
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML--LDSGA 192


                 ...
gi 189181677 136 QPD 138
Cdd:PHA02875 193 NID 195
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-124 3.26e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189181677  26 LLRLGADPNLVLDDGAAavhlaarashprALHC----------LRMLLRWGADPNARSAEGLTPVHVaaawgCC------ 89
Cdd:PHA03095  69 LLEAGADVNAPERCGFT------------PLHLylynattldvIKLLIKAGADVNAKDKVGRTPLHV-----YLsgfnin 131

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 189181677  90 -GALELLLSRGGDPTLRDQDGLRPLDWALqqRHHNC 124
Cdd:PHA03095 132 pKVIRLLLRKGADVNALDLYGMTPLAVLL--KSRNA 165
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 59-137 1.24e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 1.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189181677  59 LRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVLQELDTPTQP 137
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP 619
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 59-128 1.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 1.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189181677  59 LRMLLRWGADPNARSA-EGLTPVHVAAAwgCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRH-HNCARVL 128
Cdd:PHA02878 251 LKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRIL 320
Ank_4 pfam13637
Ankyrin repeats (many copies);
56-96 1.83e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 189181677   56 LHCLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLL 96
Cdd:pfam13637  14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-131 3.76e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 3.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189181677  59 LRMLLRWGADPNARSAEGLTPVHV----AAAwgCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNcARVLQEL 131
Cdd:PHA03095 135 IRLLLRKGADVNALDLYGMTPLAVllksRNA--NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPR-ARIVREL 208
LEM cd12934
LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner ...
 298-319 4.86e-03

LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner nuclear membrane protein Man1 and similar proteins; The family corresponds to a group of inner nuclear membrane proteins containing LEM domain. Emerin occurs in four phosphorylated forms and plays a role in cell cycle-dependent events. It is absent from the inner nuclear membrane in most patients with X-linked muscular dystrophy. Emerin interacts with A-type and B-type lamins. Man1, also termed LEM domain-containing protein 3 (LEMD3) is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and post-mitotic reassembly. Some LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are non-membrane nuclear polypeptides. This family also contains LEM domain-containing protein LEMP-1 and LEM2. LEMP-1, also termed cancer/testis antigen 50 (CT50), is encoded by LEMD1, a novel testis-specific gene expressed in colorectal cancers. LEMP-1 may function as a cancer-testis antigen for immunotherapy of colorectal carcinoma (CRC). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization while its binding to lamin C plays an important role in the organization of lamin A/C complexes. Some uncharacterized LEM domain-containing proteins are also included in this family. Unlike other family members, these harbor an ankyrin repeat region that may mediate protein-protein interactions.


Pssm-ID: 240585  Cd Length: 37  Bit Score: 34.69  E-value: 4.86e-03
                         10        20
                 ....*....|....*....|..
gi 189181677 298 GYSPGPVTPFTRGHYLRRLQEA 319
Cdd:cd12934   14 GEPPGPITDTTRKVYLKKLAKL 35
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 56-128 5.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 5.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189181677  56 LHCLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVL 128
Cdd:PHA02874 137 LESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209
 
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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