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Conserved domains on  [gi|1958659554|ref|XP_038942251|]
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NACHT, LRR and PYD domains-containing protein 1a allele 1 isoform X2 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
 838-1090 1.62e-142

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).


:

Pssm-ID: 463919  Cd Length: 252  Bit Score: 430.54  E-value: 1.62e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  838 VRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHsHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDS 917
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLPPQH-WMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  918 SLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRmIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTI 997
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLR-IHATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  998 RKAIDEEELK-FQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKK 1076
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                          250
                   ....*....|....
gi 1958659554 1077 YMNLIWEALLKPGD 1090
Cdd:pfam13553  239 SETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 157-326 1.73e-43

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


:

Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 155.54  E-value: 1.73e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  157 QLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDrFQHVFFFSCRELA-QCKQLSLAELIAQGQEVPTAPTRQ----ILSRP 231
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  232 EKLLFILDGIDEPAWVLEDQNPElcvhwsqaQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFS 311
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 1958659554  312 EFERKDYFYKYFAKE 326
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1110-1190 5.36e-40

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. In general, CARDs are death domains (DDs) 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.


:

Pssm-ID: 260039  Cd Length: 81  Bit Score: 142.36  E-value: 5.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554 1110 HFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDL 1189
Cdd:cd08330      1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                   .
gi 1958659554 1190 L 1190
Cdd:cd08330     81 E 81
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 452-563 8.61e-28

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.


:

Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 108.92  E-value: 8.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  452 HLCLQEFFAAMSYILEDSEE-------AHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFP 524
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEksnplkeFFGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958659554  525 WETKLKLLQSI---IGEPFCQPCHLGLFHCLYENQEEELLTE 563
Cdd:pfam17776   81 SEIKQELLQWIkslIQKELSSERFLNLFHCLYELQDESFVKE 122
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 646-767 8.70e-17

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 82.79  E-value: 8.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  646 LFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGD 725
Cdd:cd00116    100 VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGD 179

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958659554  726 NGVRQLCEGLRNpACNLSILRLDQASLSEQ-------VITELRALETKN 767
Cdd:cd00116    180 AGIRALAEGLKA-NCNLEVLDLNNNGLTDEgasalaeTLASLKSLEVLN 227
NOD2_WH super family cl39286
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 396-450 2.69e-03

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


The actual alignment was detected with superfamily member pfam17779:

Pssm-ID: 465501  Cd Length: 57  Bit Score: 37.16  E-value: 2.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659554  396 QLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLS-YSF 450
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKvYSF 57
 
Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
 838-1090 1.62e-142

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).


Pssm-ID: 463919  Cd Length: 252  Bit Score: 430.54  E-value: 1.62e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  838 VRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHsHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDS 917
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLPPQH-WMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  918 SLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRmIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTI 997
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLR-IHATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  998 RKAIDEEELK-FQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKK 1076
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                          250
                   ....*....|....
gi 1958659554 1077 YMNLIWEALLKPGD 1090
Cdd:pfam13553  239 SETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 157-326 1.73e-43

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 155.54  E-value: 1.73e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  157 QLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDrFQHVFFFSCRELA-QCKQLSLAELIAQGQEVPTAPTRQ----ILSRP 231
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  232 EKLLFILDGIDEPAWVLEDQNPElcvhwsqaQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFS 311
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 1958659554  312 EFERKDYFYKYFAKE 326
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1110-1190 5.36e-40

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. In general, CARDs are death domains (DDs) 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.


Pssm-ID: 260039  Cd Length: 81  Bit Score: 142.36  E-value: 5.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554 1110 HFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDL 1189
Cdd:cd08330      1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                   .
gi 1958659554 1190 L 1190
Cdd:cd08330     81 E 81
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 452-563 8.61e-28

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.


Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 108.92  E-value: 8.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  452 HLCLQEFFAAMSYILEDSEE-------AHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFP 524
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEksnplkeFFGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958659554  525 WETKLKLLQSI---IGEPFCQPCHLGLFHCLYENQEEELLTE 563
Cdd:pfam17776   81 SEIKQELLQWIkslIQKELSSERFLNLFHCLYELQDESFVKE 122
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
153-514 3.37e-21

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 100.26  E-value: 3.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  153 EKKPQLVIIEGAAGIGKSTLARQV-KRAWDEGQLYRDRFqhVFFFSCRELAqcKQLSLAELIAQGQEVPTAPTRQILS-- 229
Cdd:COG5635    177 EAKKKRLLILGEPGSGKTTLLRYLaLELAERYLDAEDPI--PILIELRDLA--EEASLEDLLAEALEKRGGEPEDALErl 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  230 -RPEKLLFILDGIDEpawVLEDQNPELCVHWsqaqpvhtlLGSLLGKsiLPEASLMLTARTTALQKlvPSLGQPHRVEVL 308
Cdd:COG5635    253 lRNGRLLLLLDGLDE---VPDEADRDEVLNQ---------LRRFLER--YPKARVIITSRPEGYDS--SELEGFEVLELA 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  309 GFSEFERKDYFYKYFAKERNTIIDF-NLIGSIPVLLTLCEVPWVCWLLCTclekQMQQGEVLSltsQTTTALCLKYLSL- 386
Cdd:COG5635    317 PLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLAL----LLRERGELP---DTRAELYEQFVELl 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  387 ---------TIPGQHLSTQ--LRTLCSLAAEGICQRRTLFSKSD--------LCKQGLAEDAIATFL-KIGVLQRQpSSL 446
Cdd:COG5635    390 lerwdeqrgLTIYRELSREelRELLSELALAMQENGRTEFAREEleeilreyLGRRKDAEALLDELLlRTGLLVER-GEG 468

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659554  447 SYSFAHLCLQEFFAAmSYILEDSEEahgdmgndRTVETLVERYGRQNLFEapTVRFLLGLLNTREMRE 514
Cdd:COG5635    469 RYSFAHRSFQEYLAA-RALVEELDE--------ELLELLAEHLEDPRWRE--VLLLLAGLLDDVKQIK 525
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 1109-1189 1.76e-20

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 86.84  E-value: 1.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554 1109 LHFVDQHREQLVARVTSVDPLLDKLHG-LVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIM 1187
Cdd:pfam00619    1 RKLLKKNRVALVERLGTLDGLLDYLLEkNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                   ..
gi 1958659554 1188 DL 1189
Cdd:pfam00619   81 DL 82
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 646-767 8.70e-17

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).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 82.79  E-value: 8.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  646 LFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGD 725
Cdd:cd00116    100 VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGD 179

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958659554  726 NGVRQLCEGLRNpACNLSILRLDQASLSEQ-------VITELRALETKN 767
Cdd:cd00116    180 AGIRALAEGLKA-NCNLEVLDLNNNGLTDEgasalaeTLASLKSLEVLN 227
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 638-764 2.38e-08

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 57.88  E-value: 2.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  638 ISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCrLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELD 717
Cdd:COG5238    276 IGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKT-LHTLNLAYNGIGAQGAIALAKALQENTTLHSLD 354

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958659554  718 LRLNDLGDNGVRQLCEGLRNpacNLSILRLDqasLSEQVITELRALE 764
Cdd:COG5238    355 LSDNQIGDEGAIALAKYLEG---NTTLRELN---LGKNNIGKQGAEA 395
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
710-736 8.80e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.77  E-value: 8.80e-04
                            10        20
                    ....*....|....*....|....*..
gi 1958659554   710 HSRLAELDLRLNDLGDNGVRQLCEGLR 736
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 396-450 2.69e-03

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


Pssm-ID: 465501  Cd Length: 57  Bit Score: 37.16  E-value: 2.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659554  396 QLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLS-YSF 450
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKvYSF 57
COG3899 COG3899
Predicted ATPase [General function prediction only];
156-296 5.61e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 41.00  E-value: 5.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  156 PQLVIIEGAAGIGKSTLARQVKRAWDEgqlyrdrfQHVFFFSCRelaqCKQLslaeliaqGQEVPTAPTRQILSRpekLL 235
Cdd:COG3899    311 GELVLVSGEAGIGKSRLVRELARRARA--------RGGRVLRGK----CDQL--------ERGVPYAPLAQALRA---LL 367

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659554  236 FILDGIDEPAW--VLEDQNPELcvhwsqAQPVHTLLGSLLGKSILPEASLMLTARTT--ALQKLV 296
Cdd:COG3899    368 GQLPEDELAAWraRLLAALGAN------GRLLADLLPELELQPAPPELDPEEARNRLfrALLRLL 426
 
Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
 838-1090 1.62e-142

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).


Pssm-ID: 463919  Cd Length: 252  Bit Score: 430.54  E-value: 1.62e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  838 VRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHsHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDS 917
Cdd:pfam13553    1 VHLPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFLDLLPPQH-WMVAGPLFDIKAEPGAVTAIHLPHFICLQAGHVDT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  918 SLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRmIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTI 997
Cdd:pfam13553   80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLR-IHATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  998 RKAIDEEELK-FQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKK 1076
Cdd:pfam13553  159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238

                          250
                   ....*....|....
gi 1958659554 1077 YMNLIWEALLKPGD 1090
Cdd:pfam13553  239 SETLVWEALVRPGD 252
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 157-326 1.73e-43

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 155.54  E-value: 1.73e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  157 QLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDrFQHVFFFSCRELA-QCKQLSLAELIAQGQEVPTAPTRQ----ILSRP 231
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  232 EKLLFILDGIDEPAWVLEDQNPElcvhwsqaQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFS 311
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 1958659554  312 EFERKDYFYKYFAKE 326
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 1110-1190 5.36e-40

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. In general, CARDs are death domains (DDs) 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.


Pssm-ID: 260039  Cd Length: 81  Bit Score: 142.36  E-value: 5.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554 1110 HFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDL 1189
Cdd:cd08330      1 HFVDRHREALIQRVTNVDPILDELRGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLVEDL 80


                   .
gi 1958659554 1190 L 1190
Cdd:cd08330     81 E 81
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 452-563 8.61e-28

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.


Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 108.92  E-value: 8.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  452 HLCLQEFFAAMSYILEDSEE-------AHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFP 524
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEksnplkeFFGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958659554  525 WETKLKLLQSI---IGEPFCQPCHLGLFHCLYENQEEELLTE 563
Cdd:pfam17776   81 SEIKQELLQWIkslIQKELSSERFLNLFHCLYELQDESFVKE 122
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
153-514 3.37e-21

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 100.26  E-value: 3.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  153 EKKPQLVIIEGAAGIGKSTLARQV-KRAWDEGQLYRDRFqhVFFFSCRELAqcKQLSLAELIAQGQEVPTAPTRQILS-- 229
Cdd:COG5635    177 EAKKKRLLILGEPGSGKTTLLRYLaLELAERYLDAEDPI--PILIELRDLA--EEASLEDLLAEALEKRGGEPEDALErl 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  230 -RPEKLLFILDGIDEpawVLEDQNPELCVHWsqaqpvhtlLGSLLGKsiLPEASLMLTARTTALQKlvPSLGQPHRVEVL 308
Cdd:COG5635    253 lRNGRLLLLLDGLDE---VPDEADRDEVLNQ---------LRRFLER--YPKARVIITSRPEGYDS--SELEGFEVLELA 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  309 GFSEFERKDYFYKYFAKERNTIIDF-NLIGSIPVLLTLCEVPWVCWLLCTclekQMQQGEVLSltsQTTTALCLKYLSL- 386
Cdd:COG5635    317 PLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLAL----LLRERGELP---DTRAELYEQFVELl 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  387 ---------TIPGQHLSTQ--LRTLCSLAAEGICQRRTLFSKSD--------LCKQGLAEDAIATFL-KIGVLQRQpSSL 446
Cdd:COG5635    390 lerwdeqrgLTIYRELSREelRELLSELALAMQENGRTEFAREEleeilreyLGRRKDAEALLDELLlRTGLLVER-GEG 468

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958659554  447 SYSFAHLCLQEFFAAmSYILEDSEEahgdmgndRTVETLVERYGRQNLFEapTVRFLLGLLNTREMRE 514
Cdd:COG5635    469 RYSFAHRSFQEYLAA-RALVEELDE--------ELLELLAEHLEDPRWRE--VLLLLAGLLDDVKQIK 525
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 1109-1189 1.76e-20

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 86.84  E-value: 1.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554 1109 LHFVDQHREQLVARVTSVDPLLDKLHG-LVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIM 1187
Cdd:pfam00619    1 RKLLKKNRVALVERLGTLDGLLDYLLEkNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                   ..
gi 1958659554 1188 DL 1189
Cdd:pfam00619   81 DL 82
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 646-767 8.70e-17

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).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 82.79  E-value: 8.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  646 LFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGD 725
Cdd:cd00116    100 VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGD 179

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958659554  726 NGVRQLCEGLRNpACNLSILRLDQASLSEQ-------VITELRALETKN 767
Cdd:cd00116    180 AGIRALAEGLKA-NCNLEVLDLNNNGLTDEgasalaeTLASLKSLEVLN 227
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 611-747 4.86e-15

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).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 77.78  E-value: 4.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  611 RSLRLKGKGQQEYKLTAPAMVLYRWTpISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQpGCRLKTLWL 690
Cdd:cd00116    123 RGLRLLAKGLKDLPPALEKLVLGRNR-LEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDL 200

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659554  691 VDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRL 747
Cdd:cd00116    201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 650-748 5.54e-14

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).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 74.31  E-value: 5.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  650 LKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVR 729
Cdd:cd00116    217 LASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQ 296

                           90
                   ....*....|....*....
gi 1958659554  730 QLCEGLRNPACNLSILRLD 748
Cdd:cd00116    297 LLAESLLEPGNELESLWVK 315
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 612-770 8.33e-11

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).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 64.68  E-value: 8.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  612 SLRLKGK-------GQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPL--SYSAVRSLCTALrQPG 682
Cdd:cd00116      2 QLSLKGEllkteraTELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETgrIPRGLQSLLQGL-TKG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  683 CRLKTLWLVDCGLTSRCCSFLASMLSAHSrLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRA 762
Cdd:cd00116     81 CGLQELDLSDNALGPDGCGVLESLLRSSS-LQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAK 159


                   ....*...
gi 1958659554  763 LETKNPKL 770
Cdd:cd00116    160 ALRANRDL 167
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 1114-1190 1.58e-09

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.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 55.60  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554 1114 QHREQLVARVtSVDPLLDKLHGL-VLSEEDYETVRAEATNQDKMRKLF-----RGSRSwswdcKDHFYQALKETH-PHLI 1186
Cdd:cd01671      3 KNRVELVEDL-DVEDILDHLIQKgVLTEEDKEEILSEKTRQDKARKLLdilprRGPKA-----FEVFCEALRETGqPHLA 76


                   ....
gi 1958659554 1187 mDLL 1190
Cdd:cd01671     77 -ELL 79
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 638-764 2.38e-08

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 57.88  E-value: 2.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  638 ISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCrLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELD 717
Cdd:COG5238    276 IGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKT-LHTLNLAYNGIGAQGAIALAKALQENTTLHSLD 354

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958659554  718 LRLNDLGDNGVRQLCEGLRNpacNLSILRLDqasLSEQVITELRALE 764
Cdd:COG5238    355 LSDNQIGDEGAIALAKYLEG---NTTLRELN---LGKNNIGKQGAEA 395
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 636-770 4.51e-07

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 53.64  E-value: 4.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  636 TPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALrQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAE 715
Cdd:COG5238    218 NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEAL-KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTS 296

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659554  716 LDLRLNDLGDNGVRQLCEGLRNPAcNLSILRLDQASLSEQ-VITELRALEtKNPKL 770
Cdd:COG5238    297 LDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQgAIALAKALQ-ENTTL 350
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 655-748 5.41e-07

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 53.64  E-value: 5.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  655 NLEELDLSGNPLSYSAVRSLCTALRQpGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEG 734
Cdd:COG5238    181 SVETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEA 259

                           90
                   ....*....|....
gi 1958659554  735 LRNpacNLSILRLD 748
Cdd:COG5238    260 LKN---NTTVETLY 270
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 637-735 3.33e-06

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 50.94  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  637 PISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALrQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAEL 716
Cdd:COG5238    303 RIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLREL 381

                           90
                   ....*....|....*....
gi 1958659554  717 DLRLNDLGDNGVRQLCEGL 735
Cdd:COG5238    382 NLGKNNIGKQGAEALIDAL 400
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 638-735 5.55e-06

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 50.17  E-value: 5.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  638 ISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGcRLKTLWLVDCGLTSRCCSFLASMLSaHSRLAELD 717
Cdd:COG5238    332 IGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNLGKNNIGKQGAEALIDALQ-TNRLHTLI 409

                           90
                   ....*....|....*...
gi 1958659554  718 LRLNDLGDNGVRQLCEGL 735
Cdd:COG5238    410 LDGNLIGAEAQQRLEQLL 427
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
710-736 8.80e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.77  E-value: 8.80e-04
                            10        20
                    ....*....|....*....|....*..
gi 1958659554   710 HSRLAELDLRLNDLGDNGVRQLCEGLR 736
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 396-450 2.69e-03

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


Pssm-ID: 465501  Cd Length: 57  Bit Score: 37.16  E-value: 2.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958659554  396 QLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLS-YSF 450
Cdd:pfam17779    2 LLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKvYSF 57
CARD_NOD1_CARD4 cd08324
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ...
 1115-1180 3.80e-03

Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation and recruitment domain (CARD) found in human NOD1 (CARD4) and similar proteins. NOD1 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD1, as well as NOD2, the N-terminal effector domain is a CARD. Nod1-CARD has been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. 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.


Pssm-ID: 260035  Cd Length: 85  Bit Score: 37.45  E-value: 3.80e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958659554 1115 HREQLVARVTSVDPLLDKL-HGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKE 1180
Cdd:cd08324      6 HRELLVSHIRNTQCLLDNLlKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYILQK 72
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
647-775 4.74e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 4.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  647 FSNLKctrNLEELDLSGNPLSysavrSLCTALRQpgC-RLKTLWLVDCGLTSrccsfLASMLSAHSRLAELDLRLNDLGD 725
Cdd:COG4886    132 LANLT---NLKELDLSNNQLT-----DLPEPLGN--LtNLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQITD 196

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958659554  726 ngvrqLCEGLRNPAcNLSILRLDQASLSE--QVITELRALETknpkLFISST 775
Cdd:COG4886    197 -----LPEPLGNLT-NLEELDLSGNQLTDlpEPLANLTNLET----LDLSNN 238
COG3899 COG3899
Predicted ATPase [General function prediction only];
156-296 5.61e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 41.00  E-value: 5.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  156 PQLVIIEGAAGIGKSTLARQVKRAWDEgqlyrdrfQHVFFFSCRelaqCKQLslaeliaqGQEVPTAPTRQILSRpekLL 235
Cdd:COG3899    311 GELVLVSGEAGIGKSRLVRELARRARA--------RGGRVLRGK----CDQL--------ERGVPYAPLAQALRA---LL 367

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958659554  236 FILDGIDEPAW--VLEDQNPELcvhwsqAQPVHTLLGSLLGKSILPEASLMLTARTT--ALQKLV 296
Cdd:COG3899    368 GQLPEDELAAWraRLLAALGAN------GRLLADLLPELELQPAPPELDPEEARNRLfrALLRLL 426
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 640-759 6.60e-03

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 40.54  E-value: 6.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  640 EASWKVLFSNlkctRNLEELDLSGNPLSYSAVRSLCTALrQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLR 719
Cdd:COG5238    198 EELAEALTQN----TTVTTLWLKRNPIGDEGAEILAEAL-KGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLS 272

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958659554  720 LNDLGDNGVRQLCEGLRNpacNLSILRLDqasLSEQVITE 759
Cdd:COG5238    273 GNQIGAEGAIALAKALQG---NTTLTSLD---LSVNRIGD 306
Dynamin_N pfam00350
Dynamin family;
267-347 6.66e-03

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 38.75  E-value: 6.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659554  267 TLLGSLLGKSILPEASLMLTARTTALQkLVPSLGQPHRVEVLGFSEFERKDY----FYKYFAKERNTIIDFNL-IGSIPV 341
Cdd:pfam00350   13 SVLNALLGRDILPRGPGPTTRRPTVLR-LGESPGASEGAVKVEYKDGEKKFEdfseLREEIEKETEKIAGTGKgISSEPI 91


                   ....*.
gi 1958659554  342 LLTLCE 347
Cdd:pfam00350   92 VLEILS 97
 
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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