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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283046799  372 KFVRIFNPSqESTADLSGMVLKQLVRGfperLYRFPPGTLLAPRHHVTVWgeaTRSAKKPLRASSSREPVPLLSIRGCAT 451
Cdd:pfam00932  22 EFIELYNTG-SKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVW---TGSGTNSATAGYWGPSNAVWNNGGDAV 93

                          90
                  ....*....|...
gi 283046799  452 LLLSPKGEVLSEH 464
Cdd:pfam00932  94 ALYDANGELVDSV 106

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283046799  372 KFVRIFNPSqESTADLSGMVLKQLVRGfperLYRFPPGTLLAPRHHVTVWgeaTRSAKKPLRASSSREPVPLLSIRGCAT 451
Cdd:pfam00932  22 EFIELYNTG-SKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVW---TGSGTNSATAGYWGPSNAVWNNGGDAV 93

                          90
                  ....*....|...
gi 283046799  452 LLLSPKGEVLSEH 464
Cdd:pfam00932  94 ALYDANGELVDSV 106

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 283046799 109 QEKLLQNQVQKLIQELKEQKERAQWEKEH-LEERLLQTTRTLQE--------MEAELQNLQ 160
Cdd:cd16269  231 QERSYEEHLRQLKEKMEEERENLLKEQERaLESKLKEQEALLEEgfkeqaelLQEEIRSLK 291

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283046799  108 SQEKLLQNQVQKLIQELKEQKERAQ-----WEKEH------------LEERLLQTTRTLQEMEAELQNLQKSclLQLARS 170
Cdd:pfam07926  15 EEAADAEAQLQKLQEDLEKQAEIAReaqqnYERELvlhaedikalqaLREELNELKAEIAELKAEAESAKAE--LEESEE 92

                  ..
gi 283046799  171 SW 172
Cdd:pfam07926  93 SW 94

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283046799  372 KFVRIFNPSqESTADLSGMVLKQLVRGfperLYRFPPGTLLAPRHHVTVWgeaTRSAKKPLRASSSREPVPLLSIRGCAT 451
Cdd:pfam00932  22 EFIELYNTG-SKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVW---TGSGTNSATAGYWGPSNAVWNNGGDAV 93

                          90
                  ....*....|...
gi 283046799  452 LLLSPKGEVLSEH 464
Cdd:pfam00932  94 ALYDANGELVDSV 106

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 283046799 109 QEKLLQNQVQKLIQE---LKEQKERAQWEKEHLEERLLQTTRTLQEMEAELQNLQK 161
Cdd:COG4372  109 EAEELQEELEELQKErqdLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 283046799 109 QEKLLQNQVQKLIQELKEQKERAQWEKEH-LEERLLQTTRTLQE--------MEAELQNLQ 160
Cdd:cd16269  231 QERSYEEHLRQLKEKMEEERENLLKEQERaLESKLKEQEALLEEgfkeqaelLQEEIRSLK 291

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283046799  108 SQEKLLQNQVQKLIQELKEQKERAQ-----WEKEH------------LEERLLQTTRTLQEMEAELQNLQKSclLQLARS 170
Cdd:pfam07926  15 EEAADAEAQLQKLQEDLEKQAEIAReaqqnYERELvlhaedikalqaLREELNELKAEIAELKAEAESAKAE--LEESEE 92

                  ..
gi 283046799  171 SW 172
Cdd:pfam07926  93 SW 94

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283046799  62 RTLRLLWRQRELEIQALRWAIQ-NGEDARLchILEEVAGLppkRSSHSQEKLLQNQVQKLIQELKEQKERAQWEKEHLEE 140
Cdd:COG1196  263 AELEAELEELRLELEELELELEeAQAEEYE--LLAELARL---EQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                         90       100
                 ....*....|....*....|..
gi 283046799 141 RLLQTTRTLQEMEAELQNLQKS 162
Cdd:COG1196  338 ELEELEEELEEAEEELEEAEAE 359