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Conserved domains on  [gi|1034572853|ref|XP_011518267|]
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lamin tail domain-containing protein 2 isoform X1 [Homo sapiens]

Protein Classification

lamin tail domain-containing protein( domain architecture ID 10469225)

lamin tail domain (LTD)-containing protein similar to Homo sapiens lamin tail domain-containing protein 1 (LMNTD1)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 445-537 2.40e-09

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


:

Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 55.12  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 445 KFVRIFNPSqESTADLSGMVLKQLVRGfperLYRFPPGTLLAPRHHVTVWgeaTRSAKKPLRASSSREPVPLLSIRGCAT 524
Cdd:pfam00932  22 EFIELYNTG-SKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVW---TGSGTNSATAGYWGPSNAVWNNGGDAV 93

                          90
                  ....*....|...
gi 1034572853 525 LLLSPKGEVLSEH 537
Cdd:pfam00932  94 ALYDANGELVDSV 106
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
121-234 2.35e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 121 QLALESLDPRTLRLLWRQRELEIQALRWAIQNGEDARLCHILEEvaglppkrssHSQEKLLQNQVQKLIQELKEQKERAQ 200
Cdd:COG4717   350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ----------AEEYQELKEELEELEEQLEELLGELE 419

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034572853 201 WALSEQEKEHLEERLLQTTRTLQEMEAELQNLQK 234
Cdd:COG4717   420 ELLEALDEEELEEELEELEEELEELEEELEELRE 453
 
Name Accession Description Interval E-value
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 445-537 2.40e-09

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 55.12  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 445 KFVRIFNPSqESTADLSGMVLKQLVRGfperLYRFPPGTLLAPRHHVTVWgeaTRSAKKPLRASSSREPVPLLSIRGCAT 524
Cdd:pfam00932  22 EFIELYNTG-SKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVW---TGSGTNSATAGYWGPSNAVWNNGGDAV 93

                          90
                  ....*....|...
gi 1034572853 525 LLLSPKGEVLSEH 537
Cdd:pfam00932  94 ALYDANGELVDSV 106
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
121-234 2.35e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 121 QLALESLDPRTLRLLWRQRELEIQALRWAIQNGEDARLCHILEEvaglppkrssHSQEKLLQNQVQKLIQELKEQKERAQ 200
Cdd:COG4717   350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ----------AEEYQELKEELEELEEQLEELLGELE 419

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034572853 201 WALSEQEKEHLEERLLQTTRTLQEMEAELQNLQK 234
Cdd:COG4717   420 ELLEALDEEELEEELEELEEELEELEEELEELRE 453
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 176-245 5.26e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 40.70  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 176 SQEKLLQNQVQKLIQELKEQKERAQWALSEQEKE---H---------LEERLLQTTRTLQEMEAELQNLQKSclLQLARS 243
Cdd:pfam07926  15 EEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvlHaedikalqaLREELNELKAEIAELKAEAESAKAE--LEESEE 92


                  ..
gi 1034572853 244 SW 245
Cdd:pfam07926  93 SW 94
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-233 9.41e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 9.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853  156 ARLCHILEEVaglppKRsshsQEKLLQNQVQKLI--QELKEQKERAQWALSEQEKEHLEERLLQTTRTLQEMEAELQNLQ 233
Cdd:TIGR02168  189 DRLEDILNEL-----ER----QLKSLERQAEKAEryKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELT 259
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
138-234 1.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 138 QRELEIQALrwaIQNGEDaRLCHILEEVAGLPPKRSSHSQEklLQNqVQKLIQELKEQKE-----RAQWALSEQEKEHLE 212
Cdd:PRK03918  186 KRTENIEEL---IKEKEK-ELEEVLREINEISSELPELREE--LEK-LEKEVKELEELKEeieelEKELESLEGSKRKLE 258

                          90       100
                  ....*....|....*....|..
gi 1034572853 213 ERLLQTTRTLQEMEAELQNLQK 234
Cdd:PRK03918  259 EKIRELEERIEELKKEIEELEE 280
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 177-233 6.83e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.10  E-value: 6.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034572853 177 QEKLLQNQVQKLIQELKEQKERAqwaLSEQEKEhLEERLLQTTRTLQE--------MEAELQNLQ 233
Cdd:cd16269   231 QERSYEEHLRQLKEKMEEERENL---LKEQERA-LESKLKEQEALLEEgfkeqaelLQEEIRSLK 291
 
Name Accession Description Interval E-value
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 445-537 2.40e-09

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 55.12  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 445 KFVRIFNPSqESTADLSGMVLKQLVRGfperLYRFPPGTLLAPRHHVTVWgeaTRSAKKPLRASSSREPVPLLSIRGCAT 524
Cdd:pfam00932  22 EFIELYNTG-SKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVW---TGSGTNSATAGYWGPSNAVWNNGGDAV 93

                          90
                  ....*....|...
gi 1034572853 525 LLLSPKGEVLSEH 537
Cdd:pfam00932  94 ALYDANGELVDSV 106
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
121-234 2.35e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 121 QLALESLDPRTLRLLWRQRELEIQALRWAIQNGEDARLCHILEEvaglppkrssHSQEKLLQNQVQKLIQELKEQKERAQ 200
Cdd:COG4717   350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ----------AEEYQELKEELEELEEQLEELLGELE 419

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034572853 201 WALSEQEKEHLEERLLQTTRTLQEMEAELQNLQK 234
Cdd:COG4717   420 ELLEALDEEELEEELEELEEELEELEEELEELRE 453
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 132-242 4.56e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 132 LRLL-WRQRELEIQALRWAIQNGED------ARLCHILEEVAGLppkRSSHSQEKLLQNQVQKLIQELKEQKERAqwals 204
Cdd:COG1196   229 LLLLkLRELEAELEELEAELEELEAeleeleAELAELEAELEEL---RLELEELELELEEAQAEEYELLAELARL----- 300

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034572853 205 EQEKEHLEERLLQTTRTLQEMEAELQNLQKSCLLQLAR 242
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 176-245 5.26e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 40.70  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 176 SQEKLLQNQVQKLIQELKEQKERAQWALSEQEKE---H---------LEERLLQTTRTLQEMEAELQNLQKSclLQLARS 243
Cdd:pfam07926  15 EEAADAEAQLQKLQEDLEKQAEIAREAQQNYERElvlHaedikalqaLREELNELKAEIAELKAEAESAKAE--LEESEE 92


                  ..
gi 1034572853 244 SW 245
Cdd:pfam07926  93 SW 94
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 132-236 5.26e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.19  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 132 LRLLWRQRELEIQALRwaiQNGEDARLCHILEEVAGLPPKRSSHSQEKL--LQNQVQKLIQELKEQKERAQWALSEQ--E 207
Cdd:pfam05557  57 IRLLEKREAEAEEALR---EQAELNRLKKKYLEALNKKLNEKESQLADAreVISCLKNELSELRRQIQRAELELQSTnsE 133

                          90       100
                  ....*....|....*....|....*....
gi 1034572853 208 KEHLEERLLQTTRTLQEMEAELQNLQKSC 236
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQLRQNLEKQQ 162
FlxA pfam14282
FlxA-like protein; This family includes FlxA from E. coli. The expression of FlxA is regulated ...
 173-242 6.20e-04

FlxA-like protein; This family includes FlxA from E. coli. The expression of FlxA is regulated by the FliA sigma factor, a transcription factor specific for class 3 flagellar operons. However FlxA is not required for flagellar function or formation.


Pssm-ID: 433836 [Multi-domain]  Cd Length: 101  Bit Score: 39.70  E-value: 6.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 173 SSHSQEKLLQNQVQKLIQELKEqkeraqwaLSEQEKEHLEERLLQTtrtlQEMEAELQNLQksclLQLAR 242
Cdd:pfam14282  14 GSASQIASLQKQIKNLTKQLKE--------LSNSDEMTKEEKKQQQ----QLIQAQIQQLQ----AQIAQ 67
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-233 9.41e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 9.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853  156 ARLCHILEEVaglppKRsshsQEKLLQNQVQKLI--QELKEQKERAQWALSEQEKEHLEERLLQTTRTLQEMEAELQNLQ 233
Cdd:TIGR02168  189 DRLEDILNEL-----ER----QLKSLERQAEKAEryKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELT 259
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 137-235 1.11e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853  137 RQRELEIQALRWAIQNGEDARLCHILEEVAGLPPKRSSHSQEKLLQ-NQVQKLIQELKEQKERAQWALS---------EQ 206
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKlEELRLEVSELEEEIEELQKELYalaneisrlEQ 302

                           90       100
                   ....*....|....*....|....*....
gi 1034572853  207 EKEHLEERLLQTTRTLQEMEAELQNLQKS 235
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESK 331
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
138-234 1.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 138 QRELEIQALrwaIQNGEDaRLCHILEEVAGLPPKRSSHSQEklLQNqVQKLIQELKEQKE-----RAQWALSEQEKEHLE 212
Cdd:PRK03918  186 KRTENIEEL---IKEKEK-ELEEVLREINEISSELPELREE--LEK-LEKEVKELEELKEeieelEKELESLEGSKRKLE 258

                          90       100
                  ....*....|....*....|..
gi 1034572853 213 ERLLQTTRTLQEMEAELQNLQK 234
Cdd:PRK03918  259 EKIRELEERIEELKKEIEELEE 280
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
121-235 2.03e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 121 QLALESLDPRTLRLLWRQREleiqALRWAIQNGEDAR--LCHILEEVAGLPpKRSSHSQEKL--LQNQVQKLIQELKE-- 194
Cdd:COG4372    12 RLSLFGLRPKTGILIAALSE----QLRKALFELDKLQeeLEQLREELEQAR-EELEQLEEELeqARSELEQLEEELEEln 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034572853 195 ---QKERAQWALSEQEKEHLEERLLQTTRTLQEMEAELQNLQKS 235
Cdd:COG4372    87 eqlQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 137-230 4.70e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.02  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 137 RQRELEIQALRWAIQNGE-DARLCHILEEVAGLppkRSSHSQEKLLQNQVQKLIQE--LKEQkERAQWALSEQEKEHLEE 213
Cdd:pfam15558  74 LGREERRRADRREKQVIEkESRWREQAEDQENQ---RQEKLERARQEAEQRKQCQEqrLKEK-EEELQALREQNSLQLQE 149

                          90
                  ....*....|....*..
gi 1034572853 214 RLLQTTRTLQEMEAELQ 230
Cdd:pfam15558 150 RLEEACHKRQLKEREEQ 166
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
140-234 5.30e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 140 ELEIQALRWAIQNGEDARLcHILEEVAGLPPKRSShsqeklLQNQVQKLIQELKEQKERAQwALSEQEKEHLEER--LLQ 217
Cdd:COG1340    14 EEKIEELREEIEELKEKRD-ELNEELKELAEKRDE------LNAQVKELREEAQELREKRD-ELNEKVKELKEERdeLNE 85

                          90
                  ....*....|....*..
gi 1034572853 218 TTRTLQEMEAELQNLQK 234
Cdd:COG1340    86 KLNELREELDELRKELA 102
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 177-233 6.83e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.10  E-value: 6.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034572853 177 QEKLLQNQVQKLIQELKEQKERAqwaLSEQEKEhLEERLLQTTRTLQE--------MEAELQNLQ 233
Cdd:cd16269   231 QERSYEEHLRQLKEKMEEERENL---LKEQERA-LESKLKEQEALLEEgfkeqaelLQEEIRSLK 291
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 130-234 9.08e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034572853 130 RTLRLLWRQRELEIQALRWAIQ-NGEDARLchILEEVAGLPpKRSSHSQEKL--LQNQVQKLIQELKEQKERAqwALSEQ 206
Cdd:COG1196   263 AELEAELEELRLELEELELELEeAQAEEYE--LLAELARLE-QDIARLEERRreLEERLEELEEELAELEEEL--EELEE 337

                          90       100
                  ....*....|....*....|....*...
gi 1034572853 207 EKEHLEERLLQTTRTLQEMEAELQNLQK 234
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEE 365
 
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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