Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745  85 NGQSGLTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKKMCLFHLTHLSDIGEGMDYIVKSLSSEPcDLEEIQLVS 164
Cdd:COG5238  279 EGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENT-TLHSLDLSD 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745 165 CCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEAlheLIDRMNVlEQLTALMLPW---GCDVQGSLSSLLKHLEEV 241
Cdd:COG5238  358 NQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEA---LIDALQT-NRLHTLILDGnliGAEAQQRLEQLLERIKSV 433

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 699114745   4 IKDNSRALIQRMgmtVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYP 79
Cdd:cd01671    1 LRKNRVELVEDL---DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQP 73

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745  71 KSLKEWNYPLFQDLNGQSGLTDSLGNLKNLTKLI-MDniKMNEEDAIKLAEGLKNLKKMCLFHLTHLSDIGEG---MDYI 146
Cdd:cd00116   51 PSLKELCLSLNETGRIPRGLQSLLQGLTKGCGLQeLD--LSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGdrgLRLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745 147 VKSLSSEPCDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEALHELIDRMNVLEQLTALMLPWGCD 226
Cdd:cd00116  129 AKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDE 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745 227 VQGSLSSLLKHLeevPQLVKLGLKNWRLTDTEIRILGAFFgKNPLKNFQQLNLAGNRVSSDGWLAFMGVFENLKQLVFFD 306
Cdd:cd00116  209 GASALAETLASL---KSLEVLNLGDNNLTDAGAAALASAL-LSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELD 284

                 ....*..
gi 699114745 307 FSTKEFL 313
Cdd:cd00116  285 LRGNKFG 291

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 699114745   4 IKDNSRALIQRMgmtVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYP 79
Cdd:cd01671    1 LRKNRVELVEDL---DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQP 73

Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase activation and recruitment domain (CARD) similar to those found in Caspase-1 (CASP1, ICE) and related proteins, including CARD-only proteins such as ICEBERG or CARD18, INCA (CARD17), CARD16 (COP1, PSEUDO-ICE), CARD8 (DACAR, NDPP1, TUCAN), and CARD12 (NLRC4), as well as ICE-like caspases such as CASP12, CASP5 (ICH-3) and CASP4 (TX, ICH-2). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. CASP1 plays a central role in the cellular response to a wide variety of microbial and non-microbial stimuli, being activated by the inflammasome or the pyroptosome. CARD8 binds itself and the initiator caspase-9, interfering with the binding of APAF-1 and suppressing caspase-9 activation. CARD12 is a Nod-like receptor (NLR) that plays an important role in the innate immune response to Gram-negative bacteria. Caspase-4 (CASP4), -5 (CASP5), and -12 (CASP12) are inflammatory caspases implicated in inflammation and endoplasmic reticulum stress-induced apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699114745   5 KDNSRALIQRMGMTVIKQITDDLFVWNVLNREEVNIICCEKVE-QDAARGIIHMILKKGSESCNLFLKSLKE 75
Cdd:cd08325    3 KEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTiVDKARVLIDSVTEKGQMAGQIFIQHLCN 74

Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745   3 FIKDNSRALIQRMgmTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPLFQ 82
Cdd:cd08329   10 LIRKNRMALFQHL--TCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKEIDVVLYR 87

                 ....*.
gi 699114745  83 DLNGQS 88
Cdd:cd08329   88 DLFVQK 93

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745 141 EGMDYIVKSLSSEPcDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLekdGNEALHELIDRMNVLEQLTALM 220
Cdd:COG5238  195 EGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI---GDEGVIALAEALKNNTTVETLY 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745 221 LpwGC---DVQGsLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNplKNFQQLNLAGNRVSSDGWLAFMGVFE 297
Cdd:COG5238  271 L--SGnqiGAEG-AIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGN--KTLHTLNLAYNGIGAQGAIALAKALQ 345

                        170
                 ....*....|.
gi 699114745 298 NLKQLVFFDFS 308
Cdd:COG5238  346 ENTTLHSLDLS 356

Leucine-rich repeat (LRR) protein [Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745  53 GIIHMILKKGSESCNLFLKSLKEWNYPLFQDLNGQSGLTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKKMCLFH 132
Cdd:COG4886   29 LLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745 133 LTHLSDIgegmdyivKSLSsepcdleeiqlvsccLSANAVKILAQNLHNLVKLSILDLSENYLekdgnEALHELIDRMNV 212
Cdd:COG4886  109 LSNLTNL--------ESLD---------------LSGNQLTDLPEELANLTNLKELDLSNNQL-----TDLPEPLGNLTN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699114745 213 LEQLtalmlpwgcDVQG-SLSSLLKHLEEVPQLVKLGlknwrLTDTEIRILGAFFGKnpLKNFQQLNLAGNRVSSdgwla 291
Cdd:COG4886  161 LKSL---------DLSNnQLTDLPEELGNLTNLKELD-----LSNNQITDLPEPLGN--LTNLEELDLSGNQLTD----- 219

                        250
                 ....*....|....*..
gi 699114745 292 FMGVFENLKQLVFFDFS 308
Cdd:COG4886  220 LPEPLANLTNLETLDLS 236