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Conserved domains on  [gi|2462490192|ref|XP_054184868|]
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lamin tail domain-containing protein 2 isoform X10 [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 ...
 393-485 2.21e-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: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192 393 KFVRIFNPSqESTADLSGMVLKQLVRGfperLYRFPPGTLLAPRHHVTVWgeaTRSAKKPLRASSSREPVPLLSIRGCAT 472
Cdd:pfam00932  22 EFIELYNTG-SKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVW---TGSGTNSATAGYWGPSNAVWNNGGDAV 93

                          90
                  ....*....|...
gi 2462490192 473 LLLSPKGEVLSEH 485
Cdd:pfam00932  94 ALYDANGELVDSV 106
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
69-182 1.00e-03

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: 42.45  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  69 RLALESLDPRTLRLLWRQRELEIQALRWAIQNGEDARLCHILEEvaglppkrssHSQEKLLQNQVQKLIQELKEQKERAQ 148
Cdd:COG4717   350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ----------AEEYQELKEELEELEEQLEELLGELE 419

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462490192 149 WALSEQEKEHLEERLLQTTRTLQEMEAELQNLQK 182
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 ...
 393-485 2.21e-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: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192 393 KFVRIFNPSqESTADLSGMVLKQLVRGfperLYRFPPGTLLAPRHHVTVWgeaTRSAKKPLRASSSREPVPLLSIRGCAT 472
Cdd:pfam00932  22 EFIELYNTG-SKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVW---TGSGTNSATAGYWGPSNAVWNNGGDAV 93

                          90
                  ....*....|...
gi 2462490192 473 LLLSPKGEVLSEH 485
Cdd:pfam00932  94 ALYDANGELVDSV 106
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
69-182 1.00e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  69 RLALESLDPRTLRLLWRQRELEIQALRWAIQNGEDARLCHILEEvaglppkrssHSQEKLLQNQVQKLIQELKEQKERAQ 148
Cdd:COG4717   350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ----------AEEYQELKEELEELEEQLEELLGELE 419

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462490192 149 WALSEQEKEHLEERLLQTTRTLQEMEAELQNLQK 182
Cdd:COG4717   420 ELLEALDEEELEEELEELEEELEELEEELEELRE 453
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 80-184 1.98e-03

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: 41.26  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  80 LRLLWRQRELEIQALRwaiQNGEDARLCHILEEVAGLPPKRSSHSQEKL--LQNQVQKLIQELKEQKERAQWALSEQ--E 155
Cdd:pfam05557  57 IRLLEKREAEAEEALR---EQAELNRLKKKYLEALNKKLNEKESQLADAreVISCLKNELSELRRQIQRAELELQSTnsE 133

                          90       100
                  ....*....|....*....|....*....
gi 2462490192 156 KEHLEERLLQTTRTLQEMEAELQNLQKSC 184
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQLRQNLEKQQ 162
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-181 2.16e-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: 41.20  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  104 ARLCHILEEVAGlppkrsshsQEKLLQNQVQKLI--QELKEQKERAQWALSEQEKEHLEERLLQTTRTLQEMEAELQNLQ 181
Cdd:TIGR02168  189 DRLEDILNELER---------QLKSLERQAEKAEryKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELT 259
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
86-182 5.58e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  86 QRELEIQALrwaIQNGEDaRLCHILEEVAGLPPKRSSHSQEklLQNqVQKLIQELKEQKE-----RAQWALSEQEKEHLE 160
Cdd:PRK03918  186 KRTENIEEL---IKEKEK-ELEEVLREINEISSELPELREE--LEK-LEKEVKELEELKEeieelEKELESLEGSKRKLE 258

                          90       100
                  ....*....|....*....|..
gi 2462490192 161 ERLLQTTRTLQEMEAELQNLQK 182
Cdd:PRK03918  259 EKIRELEERIEELKKEIEELEE 280
 
Name Accession Description Interval E-value
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 393-485 2.21e-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: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192 393 KFVRIFNPSqESTADLSGMVLKQLVRGfperLYRFPPGTLLAPRHHVTVWgeaTRSAKKPLRASSSREPVPLLSIRGCAT 472
Cdd:pfam00932  22 EFIELYNTG-SKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVW---TGSGTNSATAGYWGPSNAVWNNGGDAV 93

                          90
                  ....*....|...
gi 2462490192 473 LLLSPKGEVLSEH 485
Cdd:pfam00932  94 ALYDANGELVDSV 106
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
69-182 1.00e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  69 RLALESLDPRTLRLLWRQRELEIQALRWAIQNGEDARLCHILEEvaglppkrssHSQEKLLQNQVQKLIQELKEQKERAQ 148
Cdd:COG4717   350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ----------AEEYQELKEELEELEEQLEELLGELE 419

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462490192 149 WALSEQEKEHLEERLLQTTRTLQEMEAELQNLQK 182
Cdd:COG4717   420 ELLEALDEEELEEELEELEEELEELEEELEELRE 453
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 80-190 1.26e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  80 LRLL-WRQRELEIQALRWAIQNGED------ARLCHILEEVAGLppkRSSHSQEKLLQNQVQKLIQELKEQKERAqwals 152
Cdd:COG1196   229 LLLLkLRELEAELEELEAELEELEAeleeleAELAELEAELEEL---RLELEELELELEEAQAEEYELLAELARL----- 300

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462490192 153 EQEKEHLEERLLQTTRTLQEMEAELQNLQKSCLLQLAR 190
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 80-184 1.98e-03

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: 41.26  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  80 LRLLWRQRELEIQALRwaiQNGEDARLCHILEEVAGLPPKRSSHSQEKL--LQNQVQKLIQELKEQKERAQWALSEQ--E 155
Cdd:pfam05557  57 IRLLEKREAEAEEALR---EQAELNRLKKKYLEALNKKLNEKESQLADAreVISCLKNELSELRRQIQRAELELQSTnsE 133

                          90       100
                  ....*....|....*....|....*....
gi 2462490192 156 KEHLEERLLQTTRTLQEMEAELQNLQKSC 184
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQLRQNLEKQQ 162
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-181 2.16e-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: 41.20  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  104 ARLCHILEEVAGlppkrsshsQEKLLQNQVQKLI--QELKEQKERAQWALSEQEKEHLEERLLQTTRTLQEMEAELQNLQ 181
Cdd:TIGR02168  189 DRLEDILNELER---------QLKSLERQAEKAEryKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELT 259
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-183 2.37e-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: 41.20  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192   85 RQRELEIQALRWAIQNGEDARLCHILEEVAGLPPKRSSHSQEKLLQ-NQVQKLIQELKEQKERAQWALS---------EQ 154
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKlEELRLEVSELEEEIEELQKELYalaneisrlEQ 302

                           90       100
                   ....*....|....*....|....*....
gi 2462490192  155 EKEHLEERLLQTTRTLQEMEAELQNLQKS 183
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESK 331
FlxA pfam14282
FlxA-like protein; This family includes FlxA from E. coli. The expression of FlxA is regulated ...
 121-190 2.79e-03

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: 37.78  E-value: 2.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192 121 SSHSQEKLLQNQVQKLIQELKEqkeraqwaLSEQEKEHLEERLLQTtrtlQEMEAELQNLQksclLQLAR 190
Cdd:pfam14282  14 GSASQIASLQKQIKNLTKQLKE--------LSNSDEMTKEEKKQQQ----QLIQAQIQQLQ----AQIAQ 67
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 124-193 2.80e-03

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: 38.39  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192 124 SQEKLLQNQVQKLIQELKEQKERAQWALSEQEKEH------------LEERLLQTTRTLQEMEAELQNLQKSclLQLARS 191
Cdd:pfam07926  15 EEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELvlhaedikalqaLREELNELKAEIAELKAEAESAKAE--LEESEE 92


                  ..
gi 2462490192 192 SW 193
Cdd:pfam07926  93 SW 94
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
86-182 5.58e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  86 QRELEIQALrwaIQNGEDaRLCHILEEVAGLPPKRSSHSQEklLQNqVQKLIQELKEQKE-----RAQWALSEQEKEHLE 160
Cdd:PRK03918  186 KRTENIEEL---IKEKEK-ELEEVLREINEISSELPELREE--LEK-LEKEVKELEELKEeieelEKELESLEGSKRKLE 258

                          90       100
                  ....*....|....*....|..
gi 2462490192 161 ERLLQTTRTLQEMEAELQNLQK 182
Cdd:PRK03918  259 EKIRELEERIEELKKEIEELEE 280
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
69-183 8.33e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 8.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490192  69 RLALESLDPRTLRLLWRQREleiqALRWAIQNGEDAR--LCHILEEVAGLPpKRSSHSQEKL--LQNQVQKLIQELKE-- 142
Cdd:COG4372    12 RLSLFGLRPKTGILIAALSE----QLRKALFELDKLQeeLEQLREELEQAR-EELEQLEEELeqARSELEQLEEELEEln 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462490192 143 ---QKERAQWALSEQEKEHLEERLLQTTRTLQEMEAELQNLQKS 183
Cdd:COG4372    87 eqlQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
 
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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