NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1564222239|gb|RXM96848|]
View 

Exportin-2 [Acipenser ruthenus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN03076 super family cl33628
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional
66-1343 0e+00

ARF guanine nucleotide exchange factor (ARF-GEF); Provisional


The actual alignment was detected with superfamily member PLN03076:

Pssm-ID: 215560 [Multi-domain]  Cd Length: 1780  Bit Score: 736.25  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239   66 SFIEADKYFLPFELACQSKSPRMVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRILETICNCFQgpQTDEGVQLQII 145
Cdd:PLN03076    80 SLAESELILSPLINACGTGSAKIVDPALDCIQKLIAHGYLRGEADPSGGPEALLLAKLIESVCKCHD--LGDEGIELLVL 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  146 KALLTAVTSPHIEIHEGTILLTVRTCYNIYLASRNLINQTTAKATLTQMLNVIFARMESQAAllTAVTSPHI--EIHEgt 223
Cdd:PLN03076   158 KTLLSAVTSTSLRIHGDCLLQAVRTCYDIYLGSKNVVNQTTAKASLIQMLVIVFRRMEADSS--TVPIQPIVvaELME-- 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  224 illtvrtcyniylasrnLINQTTAKATLTQMLnvifarmesqaalearevekerlrqqQSPVMPSVSDSPRLTrtqppeQ 303
Cdd:PLN03076   234 -----------------PAEKSDSDTSMTQFV--------------------------QGFITKIMQDIDGVL------N 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  304 PGTPETSAEqedGEQEDGEQEDGEQEDGEQENGEQENGDSEpengavqnkanlgqeakLPDDQFLPFCSFPKASDlhfhs 383
Cdd:PLN03076   265 PATAGKSSG---SGAHDGAFETTATVETTNPADLLDSTDKD-----------------MLDAKYWEISMYKSALE----- 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  384 vflGSEEQSVEMEIEKtvpetenkdtapsagrteaiqangilDDRASVlstdildpdavhgpaaaRFSHILQKDAFLVFR 463
Cdd:PLN03076   320 ---GRKGELADGEVEK--------------------------DDDLEV-----------------QIGNKLRRDAFLVFR 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  464 SLCKLSMK-PLSDGPPDPKSheLRSKVVSLQLLLSVLQSAGPVFRTHEMFVNAIKQYLCVALSKNGVSSVPDVFELSLAI 542
Cdd:PLN03076   354 ALCKLSMKtPPKEALADPQL--MRGKILALELLKILLENAGAVFRTSDRFLGAIKQYLCLSLLKNSASSLMIIFQLSCSI 431
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  543 FLTLLSNFKIHLKMQIEVFFREIFLTILETTSS-SFEHKWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDL 621
Cdd:PLN03076   432 FISLVSRFRAGLKAEIGVFFPMIVLRVLENVAQpNFQQKMIVLRFLDKLCVDSQILVDIFINYDCDVNSSNIFERMVNGL 511
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  622 SKIAQG-RSGHELGMTPLQELSLRKKGLECLVSILKCMVEWSkdlyvnpNLQSNLGQEKPPEQESTESKILEVLARRDSA 700
Cdd:PLN03076   512 LKTAQGvPPGVETTLLPPQEAAMKLEAMKCLVAILRSMGDWM-------NKQLRLPDPASLKKLDAVENNLEPGSLPVAN 584
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  701 SSLDSTV--SSGIGSTSTQASLADDPEQYEVIKQQkeiIEHGIELFNKKPKRGVQYLQEQGMLGVTPEDIAQFL------ 772
Cdd:PLN03076   585 GNGDENGegSDSHSELSSETSDAATIEQRRAYKLE---LQEGISLFNRKPKKGIEFLINANKVGESPEEIAAFLkdasgl 661
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  773 ----------HQEE-------------------------------RL-----------------------------DT-- 780
Cdd:PLN03076   662 nktligdylgEREDlslkvmhayvdsfdfqgmefdeairaflqgfRLpgeaqkidrimekfaeryckcnpkafssaDTay 741
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  781 -----------------VKNKMTKEQYIKMNRGINDSKDLPEENLSAIYDEIAGKKIALKdskEHSITPKNsKQNVPTEK 843
Cdd:PLN03076   742 vlaysvimlntdahnpmVKNKMSADDFIRNNRGIDDGKDLPEEFMRSLYERISKNEIKMK---EDDLVPQQ-KQSANSNR 817
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  844 QRRLLYNLEMEQMAKTAKALMEA----VSHAQAPFT-----------SATHLEHVRPMFKLAWTPLLAAFSVGLQDCDDQ 908
Cdd:PLN03076   818 ILGLDSILNIVIRKRGEDSYMETsddlIKHMQEQFKekarksesvyyAATDVVILRFMVEVCWAPMLAAFSVPLDQSDDE 897
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  909 EVASLCLEGIRCAIRIACIFSMQLERDAYVQALARFTLLTASSSItemKQKNIDTIKTLITVAHTDGNYLGNSWHEILKC 988
Cdd:PLN03076   898 VVTFQCLEGFRHAIHVTAVMSMKTHRDAFVTSLAKFTSLHSPADI---KQKNIDAIKAIVSIADEDGNYLQEAWEHILTC 974
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  989 ISQLELAQLIGTG--------------------VKTRYISGVTRERQGSIR----GFPSGSEDFMPLGLGNLVGGGPDkk 1044
Cdd:PLN03076   975 VSRFEHLHLLGEGappdatffaapqnesdkskqAKSPILPVLKRKGPGKLQyaaaAVRRGSYDSAGVGGKASGVVTSE-- 1052
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1045 QMASIQESVGETSsQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSLQKIVEISYYNMNRIRLQW 1124
Cdd:PLN03076  1053 QMNNLVSNLNMLE-QVGSFEMNRIFTRSQKLNSEAIIDFVKALCKVSMEELRSPSDPRVFSLTKIVEIAHYNMNRIRLVW 1131
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1125 SRIWQVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFMRPFEHIMKKNKSPTIRDMVIRCIAQMV 1204
Cdd:PLN03076  1132 SSIWHVLSDFFVTIGCSENLSIAIFAMDSLRQLSMKFLEREELANYNFQNEFMKPFVIVMRKSNAVEIRELIIRCVSQMV 1211
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1205 NSQAVNIRSGWKNIFSVFHQAASDHDETIVELAFQTTGHIVVSTFQNHFAAAIDSFQDAVKCLSEFVCNAAFPDTSMEAI 1284
Cdd:PLN03076  1212 LSRVNNVKSGWKSMFMVFTTAAYDDHKNIVLLAFEIIEKIIREYFPYITETETTTFTDCVNCLIAFTNSRFNKDISLNAI 1291
                         1370      1380      1390      1400      1410      1420      1430
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564222239 1285 RLIRHCAKYVSERPQALREYTSDDMNVAPGDRVWVRG----------------WFPVLFELSCIINRCKLDIRTS 1343
Cdd:PLN03076  1292 AFLRFCATKLAEGDLGSSSRNKDKEAPPSSPQSGKDGkqesgeftdkddhlyfWFPLLAGLSELSFDPRPEIRKS 1366
CAS_CSE1 pfam03378
CAS/CSE protein, C-terminus; Mammalian cellular apoptosis susceptibility (CAS) proteins are ...
1921-2337 0e+00

CAS/CSE protein, C-terminus; Mammalian cellular apoptosis susceptibility (CAS) proteins are homologous to the yeast chromosome-segregation protein, CSE1. This family aligns the C-terminal halves (approximately). CAS is involved in both cellular apoptosis and proliferation. Apoptosis is inhibited in CAS-depleted cells, while the expression of CAS correlates to the degree of cellular proliferation. Like CSE1, it is essential for the mitotic checkpoint in the cell cycle (CAS depletion blocks the cell in the G2 phase), and has been shown to be associated with the microtubule network and the mitotic spindle, as is the protein MEK, which is thought to regulate the intracellular localization (predominantly nuclear vs. predominantly cytosolic) of CAS. In the nucleus, CAS acts as a nuclear transport factor in the importin pathway. The importin pathway mediates the nuclear transport of several proteins that are necessary for mitosis and further progression. CAS is therefore thought to affect the cell cycle through its effect on the nuclear transport of these proteins. Since apoptosis also requires the nuclear import of several proteins (such as P53 and transcription factors), it has been suggested that CAS also enables apoptosis by facilitating the nuclear import of at least a subset of these essential proteins.


:

Pssm-ID: 367469  Cd Length: 435  Bit Score: 640.89  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1921 ERLFTMRGPNNTTLITAAEMAPFTEQLLLHLFKALSMPGSSENEYIMKAIMRSFSLLQESIVPYIPTLISQLTQKLLLVS 2000
Cdd:pfam03378    1 ERLLTLRDEQGQPIFTSADIAPFAKDLLTHLFAAIEKPGSQENEYLMKCIMRVLIVIQEAVLPVADVVLQHLTNILQEVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2001 KNPSKPHFNHYLFESLCLSVRITCKANPATVSSFEEALFPVFTEILQNDVQEFVPYVFQVMSLLLEMH-TTSIPPSYMAL 2079
Cdd:pfam03378   81 KNPSNPRFNHYLFEAIGALIRFACKADPAAVSKFEEALFPPFQAILQEDVTEFMPYVFQLLAQLLEANpSGTLPDYYMAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2080 FPHLLQPVLWERTGNIPPLVRLLQAYLQKGGTTIatTAADKIPGLLGVFQKLIASKANDHQGFYLLNSIIEHMPPDSINQ 2159
Cdd:pfam03378  161 FPPLLSPALWERRGNVPALVRLLSAFIPKASQEI--VANNKLEPVLGIFQKLIASKANDHQGFYLLESVIENFPPEVLEP 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2160 YKKQVFILLFQRLQSSKTTKFIKSFLVFINLHTVKYGAIATQEIFDSIQPKMFGMVLEKIVIPEVQKVSGPVEKKICAVG 2239
Cdd:pfam03378  239 YFKTIFSLLFQRLQNSKTEKFVKRFVIFYHLYSAKHGADFLIQLIDAIQPGVFGMIYLNVILPETQKLAGPLDRKLAAVS 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2240 ITKILTECPSMMDTdYTKLWSPLLQALIGFFELPEDDSIPDDEHFIDIEDTP--GYQTAFSQLAFAGKKEHDPIGDsVSN 2317
Cdd:pfam03378  319 YTKLLCESPAFADR-YPKGWGFLLQSLLKLLELPPDPAAADEDDIIDEADVDdmGYGVGFTQLNTAGKKERDPFPD-IPD 396
                          410       420
                   ....*....|....*....|
gi 1564222239 2318 PKILLAQSLHKLSTACPGRL 2337
Cdd:pfam03378  397 VKQWVGQSLKEASQAHPGRI 416
Cse1 super family cl38282
Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the ...
1617-1920 1.14e-127

Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the nuclear export of importin alpha. This domain contains HEAT repeats.


The actual alignment was detected with superfamily member pfam08506:

Pssm-ID: 430038 [Multi-domain]  Cd Length: 370  Bit Score: 407.07  E-value: 1.14e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1617 LFKRYRHEFKSNELWTEIKLVLDTFAQPLTELFK---------------------------------------------- 1650
Cdd:pfam08506    1 IFKRWRPLFRSDELFLEIKLVLDKFAEPFLTLLQkvdelieanknnkaslkilfevllllcklfydlncqdipeffednm 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1651 ---------------------DEEEAGLLELLKSQICDNAALYAQKYDEEFQPYLPRFVTDIWNLLVTTGQEVKYDLLVS 1709
Cdd:pfam08506   81 kewmgifhkylsydnplletdDDEEATVLEKLKASICELVQLYTLRYEEEFGPMVNDFIQAVWNLLVSTSPQPKYDILVS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1710 NAIQFLASVCERPHYKHLFEDQNTLTSICEKVIVPNMEFRTADEEAFEDNSEEYIRRDLEGSDIDTRRRAACDLVRGLCK 1789
Cdd:pfam08506  161 KALSFLTSVARRPKYAELFNNESVLKQIIEKVVLPNVTLRESDEELFEDDPIEYIRRDLEGSDSDTRRRAATDFLKELKE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1790 FFEGPVTAIFSGYVNSMLTEYAKSPGTNWKHKDAAIYLVTSLASKAQTQKHGITQANELVNLTEFFVSHILPDLKsANVN 1869
Cdd:pfam08506  241 KFEALVTNVVLEYIQRLLEKYSANPSLNWKAKDTAIYLFTSIAAKGAVTKSGVTSTNPLVDVVDFFQQQIAPDLM-ANVN 319
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1564222239 1870 EFPVLKADAVKYVMIFRSQLPKEQLLVAIPLLIALLQAESIVAHTYAAHAL 1920
Cdd:pfam08506  320 QHPILKADAIKYIYTFRNQLTKEQLIEIFPLLINFLQSSSYVVYTYAAITI 370
DSRM_STAU1_rpt4 cd19885
fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen ...
2762-2847 1.45e-56

fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


:

Pssm-ID: 380714  Cd Length: 86  Bit Score: 191.07  E-value: 1.45e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2762 QTSPEYGQGMNPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLELMGFK 2841
Cdd:cd19885      1 QTSPEYGQGMNPISRLAQIQQAKKEKEPEYTLITERGLPRRREFVMQVKVGNQTAEGMGPNKKVAKRNAAEKMLELLGFK 80

                   ....*.
gi 1564222239 2842 VPQPQP 2847
Cdd:cd19885     81 VPQPQP 86
Staufen_C pfam16482
Staufen C-terminal domain; This is the C-terminal domain of Staufen proteins. It consists of ...
2934-3037 2.19e-47

Staufen C-terminal domain; This is the C-terminal domain of Staufen proteins. It consists of an N-terminal Staufen-swapping motif (SSM) comprising two alpha helices, connected by a linker region to a dsRNA-binding-like domain ('RBD'). The 'RBD' has the fold of a functional dsRNA-binding domain, but lacks the residues required to bind RNA. This domain is responsible for dimerization, the SSM from one molecule interacts with the 'RBD' of another.


:

Pssm-ID: 465131  Cd Length: 110  Bit Score: 165.85  E-value: 2.19e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2934 KATITAMMARELLYGGTSPTAETLLKSNNNLVHLPHGPlTRPSEQLDFLTKVQGLQVEYKDFPKNNKNEFVSLINCSSQP 3013
Cdd:pfam16482    2 KATVTAAIARELLYGGTSPTAEAILKNNGKTGAVPCGL-VQPSQQLEYLARVQGFQVEYSDFPRQNKNEFLSLLTLSSQP 80
                           90       100
                   ....*....|....*....|....
gi 1564222239 3014 PLISHGIGKDVESCHDMVRASLRK 3037
Cdd:pfam16482   81 VQMTHGIGSSLEASHDQAALSALK 104
DSRM_STAU1_rpt1 cd19879
first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2467-2525 3.93e-36

first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


:

Pssm-ID: 380708  Cd Length: 66  Bit Score: 132.12  E-value: 3.93e-36
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1564222239 2467 KEKTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQH 2525
Cdd:cd19879      1 KEKTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFTVQLTLGDQHWEAEGTSIKKAQH 59
BIG2_C pfam20252
BIG2 C-terminal domain; This presumed domain is found at the C-terminus of BIG2 the brefeldin ...
1370-1481 3.24e-33

BIG2 C-terminal domain; This presumed domain is found at the C-terminus of BIG2 the brefeldin A-inhibited guanine nucleotide-exchange protein. The function of this region is unknown.


:

Pssm-ID: 466403  Cd Length: 178  Bit Score: 127.74  E-value: 3.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1370 QGMYRYMSSPHLFKLLDSLLESHTFAKAFNSNSEQRTALWRAGFkGKSKPNLLKQETSSLACCLRILFRMYMDENLK-DS 1448
Cdd:pfam20252   15 DEHYESLPSDHLLRLLDCLEKSYTFARSFNSDLELRTALWRAGF-MKQLPNLLKQETSSLSTYLRILFRLYADDEPRtSQ 93
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1564222239 1449 WKDIQTRLLRCInmdlnaanLQTLTEYLRKTLD 1481
Cdd:pfam20252   94 REEVEERLIPLC--------EDILEYYLSLDEE 118
DSRM_SF super family cl00054
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
2669-2735 2.62e-28

double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 amino acid domain that adopts an alpha-beta-beta-beta-alpha fold. It is not sequence specific, but highly specific for double-stranded RNAs (dsRNAs) of various origin and structure. The DSRM domains are found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila Staufen protein, E. coli RNase III, RNase H1, and dsRNA dependent adenosine deaminases. They are involved in numerous cellular mechanisms ranging from localization and transport of messenger RNAs, through maturation and degradation of RNAs, to viral response and signal transduction. Some members harbor tandem DSRMs that act in small RNA biogenesis.


The actual alignment was detected with superfamily member cd19883:

Pssm-ID: 444671  Cd Length: 67  Bit Score: 109.72  E-value: 2.62e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2669 KSEISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGNFSGDGEGKSKKIAKKNAAAAVLEEL 2735
Cdd:cd19883      1 KSEISQVFEIALKRNMPVNFEVTKETGPPHMKSFVTKVSVGEFAGEGEGKSKKISKKNAAIAVLEEL 67
DSRM_SF super family cl00054
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
2566-2631 5.00e-27

double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 amino acid domain that adopts an alpha-beta-beta-beta-alpha fold. It is not sequence specific, but highly specific for double-stranded RNAs (dsRNAs) of various origin and structure. The DSRM domains are found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila Staufen protein, E. coli RNase III, RNase H1, and dsRNA dependent adenosine deaminases. They are involved in numerous cellular mechanisms ranging from localization and transport of messenger RNAs, through maturation and degradation of RNAs, to viral response and signal transduction. Some members harbor tandem DSRMs that act in small RNA biogenesis.


The actual alignment was detected with superfamily member cd19881:

Pssm-ID: 444671  Cd Length: 79  Bit Score: 106.50  E-value: 5.00e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2566 MKLGKKPTYRPIDSYHGMRPNFNYNVRAPGPYPRYY-YPFSPVGPVLYQMEVSIGEQLFHGKGRTRQ 2631
Cdd:cd19881      1 MKLGKKPIYKPIDPYTGMRSAYNYNMRGNGAYPPRYfYPFPPVGPVLYQVELSIGGQQFHGKGRTRQ 67
IBN_N smart00913
Importin-beta N-terminal domain; Members of the importin-beta (karyopherin-beta) family can ...
1490-1563 8.47e-15

Importin-beta N-terminal domain; Members of the importin-beta (karyopherin-beta) family can bind and transport cargo by themselves, or can form heterodimers with importin-alpha. As part of a heterodimer, importin-beta mediates interactions with the pore complex, while importin-alpha acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo through the classical NLS import of proteins. Importin-beta is a helicoidal molecule constructed from 19 HEAT repeats. Many nuclear pore proteins contain FG sequence repeats that can bind to HEAT repeats within importins.. which is important for importin-beta mediated transport.


:

Pssm-ID: 197981 [Multi-domain]  Cd Length: 67  Bit Score: 71.12  E-value: 8.47e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564222239  1490 AEKFLESVEGNQNYPILLLTLLEKSQDNVIRVCAAVMFKNYIKRNWRIVEDEpnkicdiDRTAIKANIVNLMLS 1563
Cdd:smart00913    1 AEKQLEQFQKSPGFWLLLLEILANSEDQYVRQLAAITLKNKITRRWSSLPEE-------EKEEIKNSLLELLLS 67
 
Name Accession Description Interval E-value
PLN03076 PLN03076
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional
66-1343 0e+00

ARF guanine nucleotide exchange factor (ARF-GEF); Provisional


Pssm-ID: 215560 [Multi-domain]  Cd Length: 1780  Bit Score: 736.25  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239   66 SFIEADKYFLPFELACQSKSPRMVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRILETICNCFQgpQTDEGVQLQII 145
Cdd:PLN03076    80 SLAESELILSPLINACGTGSAKIVDPALDCIQKLIAHGYLRGEADPSGGPEALLLAKLIESVCKCHD--LGDEGIELLVL 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  146 KALLTAVTSPHIEIHEGTILLTVRTCYNIYLASRNLINQTTAKATLTQMLNVIFARMESQAAllTAVTSPHI--EIHEgt 223
Cdd:PLN03076   158 KTLLSAVTSTSLRIHGDCLLQAVRTCYDIYLGSKNVVNQTTAKASLIQMLVIVFRRMEADSS--TVPIQPIVvaELME-- 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  224 illtvrtcyniylasrnLINQTTAKATLTQMLnvifarmesqaalearevekerlrqqQSPVMPSVSDSPRLTrtqppeQ 303
Cdd:PLN03076   234 -----------------PAEKSDSDTSMTQFV--------------------------QGFITKIMQDIDGVL------N 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  304 PGTPETSAEqedGEQEDGEQEDGEQEDGEQENGEQENGDSEpengavqnkanlgqeakLPDDQFLPFCSFPKASDlhfhs 383
Cdd:PLN03076   265 PATAGKSSG---SGAHDGAFETTATVETTNPADLLDSTDKD-----------------MLDAKYWEISMYKSALE----- 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  384 vflGSEEQSVEMEIEKtvpetenkdtapsagrteaiqangilDDRASVlstdildpdavhgpaaaRFSHILQKDAFLVFR 463
Cdd:PLN03076   320 ---GRKGELADGEVEK--------------------------DDDLEV-----------------QIGNKLRRDAFLVFR 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  464 SLCKLSMK-PLSDGPPDPKSheLRSKVVSLQLLLSVLQSAGPVFRTHEMFVNAIKQYLCVALSKNGVSSVPDVFELSLAI 542
Cdd:PLN03076   354 ALCKLSMKtPPKEALADPQL--MRGKILALELLKILLENAGAVFRTSDRFLGAIKQYLCLSLLKNSASSLMIIFQLSCSI 431
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  543 FLTLLSNFKIHLKMQIEVFFREIFLTILETTSS-SFEHKWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDL 621
Cdd:PLN03076   432 FISLVSRFRAGLKAEIGVFFPMIVLRVLENVAQpNFQQKMIVLRFLDKLCVDSQILVDIFINYDCDVNSSNIFERMVNGL 511
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  622 SKIAQG-RSGHELGMTPLQELSLRKKGLECLVSILKCMVEWSkdlyvnpNLQSNLGQEKPPEQESTESKILEVLARRDSA 700
Cdd:PLN03076   512 LKTAQGvPPGVETTLLPPQEAAMKLEAMKCLVAILRSMGDWM-------NKQLRLPDPASLKKLDAVENNLEPGSLPVAN 584
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  701 SSLDSTV--SSGIGSTSTQASLADDPEQYEVIKQQkeiIEHGIELFNKKPKRGVQYLQEQGMLGVTPEDIAQFL------ 772
Cdd:PLN03076   585 GNGDENGegSDSHSELSSETSDAATIEQRRAYKLE---LQEGISLFNRKPKKGIEFLINANKVGESPEEIAAFLkdasgl 661
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  773 ----------HQEE-------------------------------RL-----------------------------DT-- 780
Cdd:PLN03076   662 nktligdylgEREDlslkvmhayvdsfdfqgmefdeairaflqgfRLpgeaqkidrimekfaeryckcnpkafssaDTay 741
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  781 -----------------VKNKMTKEQYIKMNRGINDSKDLPEENLSAIYDEIAGKKIALKdskEHSITPKNsKQNVPTEK 843
Cdd:PLN03076   742 vlaysvimlntdahnpmVKNKMSADDFIRNNRGIDDGKDLPEEFMRSLYERISKNEIKMK---EDDLVPQQ-KQSANSNR 817
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  844 QRRLLYNLEMEQMAKTAKALMEA----VSHAQAPFT-----------SATHLEHVRPMFKLAWTPLLAAFSVGLQDCDDQ 908
Cdd:PLN03076   818 ILGLDSILNIVIRKRGEDSYMETsddlIKHMQEQFKekarksesvyyAATDVVILRFMVEVCWAPMLAAFSVPLDQSDDE 897
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  909 EVASLCLEGIRCAIRIACIFSMQLERDAYVQALARFTLLTASSSItemKQKNIDTIKTLITVAHTDGNYLGNSWHEILKC 988
Cdd:PLN03076   898 VVTFQCLEGFRHAIHVTAVMSMKTHRDAFVTSLAKFTSLHSPADI---KQKNIDAIKAIVSIADEDGNYLQEAWEHILTC 974
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  989 ISQLELAQLIGTG--------------------VKTRYISGVTRERQGSIR----GFPSGSEDFMPLGLGNLVGGGPDkk 1044
Cdd:PLN03076   975 VSRFEHLHLLGEGappdatffaapqnesdkskqAKSPILPVLKRKGPGKLQyaaaAVRRGSYDSAGVGGKASGVVTSE-- 1052
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1045 QMASIQESVGETSsQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSLQKIVEISYYNMNRIRLQW 1124
Cdd:PLN03076  1053 QMNNLVSNLNMLE-QVGSFEMNRIFTRSQKLNSEAIIDFVKALCKVSMEELRSPSDPRVFSLTKIVEIAHYNMNRIRLVW 1131
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1125 SRIWQVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFMRPFEHIMKKNKSPTIRDMVIRCIAQMV 1204
Cdd:PLN03076  1132 SSIWHVLSDFFVTIGCSENLSIAIFAMDSLRQLSMKFLEREELANYNFQNEFMKPFVIVMRKSNAVEIRELIIRCVSQMV 1211
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1205 NSQAVNIRSGWKNIFSVFHQAASDHDETIVELAFQTTGHIVVSTFQNHFAAAIDSFQDAVKCLSEFVCNAAFPDTSMEAI 1284
Cdd:PLN03076  1212 LSRVNNVKSGWKSMFMVFTTAAYDDHKNIVLLAFEIIEKIIREYFPYITETETTTFTDCVNCLIAFTNSRFNKDISLNAI 1291
                         1370      1380      1390      1400      1410      1420      1430
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564222239 1285 RLIRHCAKYVSERPQALREYTSDDMNVAPGDRVWVRG----------------WFPVLFELSCIINRCKLDIRTS 1343
Cdd:PLN03076  1292 AFLRFCATKLAEGDLGSSSRNKDKEAPPSSPQSGKDGkqesgeftdkddhlyfWFPLLAGLSELSFDPRPEIRKS 1366
CAS_CSE1 pfam03378
CAS/CSE protein, C-terminus; Mammalian cellular apoptosis susceptibility (CAS) proteins are ...
1921-2337 0e+00

CAS/CSE protein, C-terminus; Mammalian cellular apoptosis susceptibility (CAS) proteins are homologous to the yeast chromosome-segregation protein, CSE1. This family aligns the C-terminal halves (approximately). CAS is involved in both cellular apoptosis and proliferation. Apoptosis is inhibited in CAS-depleted cells, while the expression of CAS correlates to the degree of cellular proliferation. Like CSE1, it is essential for the mitotic checkpoint in the cell cycle (CAS depletion blocks the cell in the G2 phase), and has been shown to be associated with the microtubule network and the mitotic spindle, as is the protein MEK, which is thought to regulate the intracellular localization (predominantly nuclear vs. predominantly cytosolic) of CAS. In the nucleus, CAS acts as a nuclear transport factor in the importin pathway. The importin pathway mediates the nuclear transport of several proteins that are necessary for mitosis and further progression. CAS is therefore thought to affect the cell cycle through its effect on the nuclear transport of these proteins. Since apoptosis also requires the nuclear import of several proteins (such as P53 and transcription factors), it has been suggested that CAS also enables apoptosis by facilitating the nuclear import of at least a subset of these essential proteins.


Pssm-ID: 367469  Cd Length: 435  Bit Score: 640.89  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1921 ERLFTMRGPNNTTLITAAEMAPFTEQLLLHLFKALSMPGSSENEYIMKAIMRSFSLLQESIVPYIPTLISQLTQKLLLVS 2000
Cdd:pfam03378    1 ERLLTLRDEQGQPIFTSADIAPFAKDLLTHLFAAIEKPGSQENEYLMKCIMRVLIVIQEAVLPVADVVLQHLTNILQEVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2001 KNPSKPHFNHYLFESLCLSVRITCKANPATVSSFEEALFPVFTEILQNDVQEFVPYVFQVMSLLLEMH-TTSIPPSYMAL 2079
Cdd:pfam03378   81 KNPSNPRFNHYLFEAIGALIRFACKADPAAVSKFEEALFPPFQAILQEDVTEFMPYVFQLLAQLLEANpSGTLPDYYMAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2080 FPHLLQPVLWERTGNIPPLVRLLQAYLQKGGTTIatTAADKIPGLLGVFQKLIASKANDHQGFYLLNSIIEHMPPDSINQ 2159
Cdd:pfam03378  161 FPPLLSPALWERRGNVPALVRLLSAFIPKASQEI--VANNKLEPVLGIFQKLIASKANDHQGFYLLESVIENFPPEVLEP 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2160 YKKQVFILLFQRLQSSKTTKFIKSFLVFINLHTVKYGAIATQEIFDSIQPKMFGMVLEKIVIPEVQKVSGPVEKKICAVG 2239
Cdd:pfam03378  239 YFKTIFSLLFQRLQNSKTEKFVKRFVIFYHLYSAKHGADFLIQLIDAIQPGVFGMIYLNVILPETQKLAGPLDRKLAAVS 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2240 ITKILTECPSMMDTdYTKLWSPLLQALIGFFELPEDDSIPDDEHFIDIEDTP--GYQTAFSQLAFAGKKEHDPIGDsVSN 2317
Cdd:pfam03378  319 YTKLLCESPAFADR-YPKGWGFLLQSLLKLLELPPDPAAADEDDIIDEADVDdmGYGVGFTQLNTAGKKERDPFPD-IPD 396
                          410       420
                   ....*....|....*....|
gi 1564222239 2318 PKILLAQSLHKLSTACPGRL 2337
Cdd:pfam03378  397 VKQWVGQSLKEASQAHPGRI 416
Cse1 pfam08506
Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the ...
1617-1920 1.14e-127

Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the nuclear export of importin alpha. This domain contains HEAT repeats.


Pssm-ID: 430038 [Multi-domain]  Cd Length: 370  Bit Score: 407.07  E-value: 1.14e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1617 LFKRYRHEFKSNELWTEIKLVLDTFAQPLTELFK---------------------------------------------- 1650
Cdd:pfam08506    1 IFKRWRPLFRSDELFLEIKLVLDKFAEPFLTLLQkvdelieanknnkaslkilfevllllcklfydlncqdipeffednm 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1651 ---------------------DEEEAGLLELLKSQICDNAALYAQKYDEEFQPYLPRFVTDIWNLLVTTGQEVKYDLLVS 1709
Cdd:pfam08506   81 kewmgifhkylsydnplletdDDEEATVLEKLKASICELVQLYTLRYEEEFGPMVNDFIQAVWNLLVSTSPQPKYDILVS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1710 NAIQFLASVCERPHYKHLFEDQNTLTSICEKVIVPNMEFRTADEEAFEDNSEEYIRRDLEGSDIDTRRRAACDLVRGLCK 1789
Cdd:pfam08506  161 KALSFLTSVARRPKYAELFNNESVLKQIIEKVVLPNVTLRESDEELFEDDPIEYIRRDLEGSDSDTRRRAATDFLKELKE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1790 FFEGPVTAIFSGYVNSMLTEYAKSPGTNWKHKDAAIYLVTSLASKAQTQKHGITQANELVNLTEFFVSHILPDLKsANVN 1869
Cdd:pfam08506  241 KFEALVTNVVLEYIQRLLEKYSANPSLNWKAKDTAIYLFTSIAAKGAVTKSGVTSTNPLVDVVDFFQQQIAPDLM-ANVN 319
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1564222239 1870 EFPVLKADAVKYVMIFRSQLPKEQLLVAIPLLIALLQAESIVAHTYAAHAL 1920
Cdd:pfam08506  320 QHPILKADAIKYIYTFRNQLTKEQLIEIFPLLINFLQSSSYVVYTYAAITI 370
CSE1 COG5657
CAS/CSE protein involved in chromosome segregation [Cell division and chromosome partitioning]; ...
1482-2329 7.08e-106

CAS/CSE protein involved in chromosome segregation [Cell division and chromosome partitioning];


Pssm-ID: 227944 [Multi-domain]  Cd Length: 947  Bit Score: 364.52  E-value: 7.08e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1482 PDPAVRRPAEKFLESVEGNQNYPILLLTL-LEKSQDNVIRVCAAVMFKNYIKRNWRivEDEPNKICDIDRTAIKANIVNL 1560
Cdd:COG5657     16 PDPPSVKCAEERLRQWEKQHGFALKLLSInLSAFNSMSLRWAALIQFKNYIDKHWR--EENGNSILPDENVLIRDELFSL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1561 MLSSPEQIQKQLSDAISIIGREDFPQKWPDLLTEMVNRFQSGDFHIINGVLRTAHSLFKRYRHEFKSNELWTEIKLVLDT 1640
Cdd:COG5657     94 IISSSNQLQIQNALAVSRIARLDFPDEWPTLVPDLLSLLSEKDMVTNENSLRVLHHIFKRLRRLFRSDALFLEIAPVLLS 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1641 FAQP---------------------------------------------------------------LTELFKDEEEAGL 1657
Cdd:COG5657    174 ILCPflfssayfwsmsenldesllslfqvclklirryydlgfqdipeffednldkfmehfckllsysNPVLQKDCLEDCV 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1658 LELLKSQICDNAALYAQKYDEEFQPYLPRFVTDIWNLLVTTGQEVKYDLLVSNAIQFLASVCERPHYKH----LFEDQNT 1733
Cdd:COG5657    254 YFKLKGSICEIFNLYTTKYPEVITYLIYDFVEIVWNLLTTITRPYIRDYLVSKSLTVLINVIKYPIRKTaevlSNVSENL 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1734 LTSICEKVIVPNMEFRTADEEAFEDNSEEYIRrdlEGSDIDTRRRAACDLVRGLCKFFEGpVTAIFSGYVNSMLTEYAKS 1813
Cdd:COG5657    334 INNLVDLLILPNLILREEDLEEWEDDPLEYIR---EQSKTDYEVNVRPCIENELKDLFDV-FGRIAVGHELTVIESEATT 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1814 PgtnwKHKDAAIYLVTSLASKAQtqkhGITQANELVNLTEFFVSHILPDLKSANVNEFPVLKADAVKYVMIFRSQLPKEQ 1893
Cdd:COG5657    410 P----NILDEARQLFAAYASFGL----GVEAVNRMVDFVKFLGSIIYPDLLSPNEIIHLRILRSRIAYILTFRNQLDSSE 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1894 LLVAiplliALLQAESIVAHTYAAHALERLFTMRGPNNTTL----ITAAEMAPFTEQLLLHLFKALSMPGS-SENEYIMK 1968
Cdd:COG5657    482 LSES-----KFLASQFFVNYTTACIDAVVLLTTREAYSTIFddwnFSVCSKIGLLENLILLVLSLMASPSSlEEREFLLQ 556
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1969 AIMRSFSLLQESIVPYIPTLISQLTQKLLLVSKNPSKPHFNHYLFESLCLSVRITCKANPATVSSFEEALFPVFTEILQN 2048
Cdd:COG5657    557 LISRIIIIDPELIAPLGSEILQLLDNLVEINAKNPSNPQFAHYTFEDIGALVFLKSGMCEITIPTLVLALVPEFPVLLSE 636
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2049 DVQEFVPYVFQVMSLLLEMHTT-SIPPSYMALFPHLLQPVLWERTGNIPPLVRLLQAYLQKGGTTIATTAADKIpglLGV 2127
Cdd:COG5657    637 DATELWSYVLQLLSILPEHFSGdVLPSVVKILRQPSLATELLPTKLEILKSYRLLDNPILTTGYIFKSSGFQPV---LGI 713
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2128 FQKLIASKANDHQGFyLLNSIIEHMPPDSINQ-YKKQVFILLFQRLQSSKTTKFIKSFLVFINLHTVKYGAIATQEIF-- 2204
Cdd:COG5657    714 LQYLLGSEPHDALCF-LNLTVVETLYLENIYEpYVNLIFVLLLSRLKNSKTERFVIKIIHVFSLVSFKDSLTVGCDNLis 792
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2205 --DSIQPKMFGMVLEKIVIPEVQkVSGPVEKKICAVGITKIL-TECPSMM-DTDYTKLWSPLLQALIGFFELP----EDD 2276
Cdd:COG5657    793 kiNQTKNILIVQLYGNWILGFDE-IHDSKDRKIHLIGLSNLLrTLHPEVLsYVSVTNLIISLLSEIFETASGDaiiyELN 871
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1564222239 2277 SIPDDEHFIDIEDtpgyQTAFSQLAFAGKKeHDPIgDSVSNPKILLAQSLHKL 2329
Cdd:COG5657    872 DDYADDWFDGEIS----AEEFSRLAQLEFK-VDPV-HDIDNTKYFISFFMEAM 918
DSRM_STAU1_rpt4 cd19885
fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen ...
2762-2847 1.45e-56

fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380714  Cd Length: 86  Bit Score: 191.07  E-value: 1.45e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2762 QTSPEYGQGMNPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLELMGFK 2841
Cdd:cd19885      1 QTSPEYGQGMNPISRLAQIQQAKKEKEPEYTLITERGLPRRREFVMQVKVGNQTAEGMGPNKKVAKRNAAEKMLELLGFK 80

                   ....*.
gi 1564222239 2842 VPQPQP 2847
Cdd:cd19885     81 VPQPQP 86
Sec7_N pfam12783
Guanine nucleotide exchange factor in Golgi transport N-terminal; The full-length Sec7 ...
454-609 3.90e-50

Guanine nucleotide exchange factor in Golgi transport N-terminal; The full-length Sec7 functions proximally in the secretory pathway as a protein binding scaffold for the coat protein complexes COPII-COPI. The COPII-COPI-protein switch is necessary for maturation of the vesicular-tubular cluster, VTC, intermediate compartments for Golgi compartment biogenesis. This N-terminal domain however does not appear to be binding either of the COP or the ARF.


Pssm-ID: 463703  Cd Length: 154  Bit Score: 175.38  E-value: 3.90e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  454 LQKDAFLVFRSLCKLS-MKPLSDgpPDPKSHELRSKVVSLQLLLSVLQSAGPVFRTHEMFVNAIKQYLCVALSKNGVSSV 532
Cdd:pfam12783    1 AAKDAFLVFRDLCKLSnGKPLSK--SDPKSHAERSKLFSLELIESILENHGDVFLKHPELLQLLKQYLCPSLLRNLSSSS 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239  533 PDVFELSLAIFLTLLSNFKIHLKMQIEVFFREIFLTILETTsSSFEHKWMVIQTLTRICADAQCVVDIYVNYDCDLN 609
Cdd:pfam12783   79 FPVFVRSLRIFLLLLRRFRSHLKLEIEVFLSLLILPLLESD-SSLWQKALVLEVLRRLCSDPQLLVEIYLNYDCDLG 154
Staufen_C pfam16482
Staufen C-terminal domain; This is the C-terminal domain of Staufen proteins. It consists of ...
2934-3037 2.19e-47

Staufen C-terminal domain; This is the C-terminal domain of Staufen proteins. It consists of an N-terminal Staufen-swapping motif (SSM) comprising two alpha helices, connected by a linker region to a dsRNA-binding-like domain ('RBD'). The 'RBD' has the fold of a functional dsRNA-binding domain, but lacks the residues required to bind RNA. This domain is responsible for dimerization, the SSM from one molecule interacts with the 'RBD' of another.


Pssm-ID: 465131  Cd Length: 110  Bit Score: 165.85  E-value: 2.19e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2934 KATITAMMARELLYGGTSPTAETLLKSNNNLVHLPHGPlTRPSEQLDFLTKVQGLQVEYKDFPKNNKNEFVSLINCSSQP 3013
Cdd:pfam16482    2 KATVTAAIARELLYGGTSPTAEAILKNNGKTGAVPCGL-VQPSQQLEYLARVQGFQVEYSDFPRQNKNEFLSLLTLSSQP 80
                           90       100
                   ....*....|....*....|....
gi 1564222239 3014 PLISHGIGKDVESCHDMVRASLRK 3037
Cdd:pfam16482   81 VQMTHGIGSSLEASHDQAALSALK 104
DSRM_STAU1_rpt1 cd19879
first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2467-2525 3.93e-36

first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380708  Cd Length: 66  Bit Score: 132.12  E-value: 3.93e-36
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1564222239 2467 KEKTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQH 2525
Cdd:cd19879      1 KEKTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFTVQLTLGDQHWEAEGTSIKKAQH 59
BIG2_C pfam20252
BIG2 C-terminal domain; This presumed domain is found at the C-terminus of BIG2 the brefeldin ...
1370-1481 3.24e-33

BIG2 C-terminal domain; This presumed domain is found at the C-terminus of BIG2 the brefeldin A-inhibited guanine nucleotide-exchange protein. The function of this region is unknown.


Pssm-ID: 466403  Cd Length: 178  Bit Score: 127.74  E-value: 3.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1370 QGMYRYMSSPHLFKLLDSLLESHTFAKAFNSNSEQRTALWRAGFkGKSKPNLLKQETSSLACCLRILFRMYMDENLK-DS 1448
Cdd:pfam20252   15 DEHYESLPSDHLLRLLDCLEKSYTFARSFNSDLELRTALWRAGF-MKQLPNLLKQETSSLSTYLRILFRLYADDEPRtSQ 93
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1564222239 1449 WKDIQTRLLRCInmdlnaanLQTLTEYLRKTLD 1481
Cdd:pfam20252   94 REEVEERLIPLC--------EDILEYYLSLDEE 118
DSRM_STAU1_rpt5 cd19887
fifth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2974-3037 3.48e-31

fifth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fifth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380716  Cd Length: 70  Bit Score: 118.23  E-value: 3.48e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564222239 2974 RPSEQLDFLTKVQGLQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMVRASLRK 3037
Cdd:cd19887      1 RPSEQLDYLSRVQGLQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMAALNILK 64
DSRM_STAU1_rpt3 cd19883
third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2669-2735 2.62e-28

third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380712  Cd Length: 67  Bit Score: 109.72  E-value: 2.62e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2669 KSEISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGNFSGDGEGKSKKIAKKNAAAAVLEEL 2735
Cdd:cd19883      1 KSEISQVFEIALKRNMPVNFEVTKETGPPHMKSFVTKVSVGEFAGEGEGKSKKISKKNAAIAVLEEL 67
DSRM_STAU1_rpt2 cd19881
second double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen ...
2566-2631 5.00e-27

second double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380710  Cd Length: 79  Bit Score: 106.50  E-value: 5.00e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2566 MKLGKKPTYRPIDSYHGMRPNFNYNVRAPGPYPRYY-YPFSPVGPVLYQMEVSIGEQLFHGKGRTRQ 2631
Cdd:cd19881      1 MKLGKKPIYKPIDPYTGMRSAYNYNMRGNGAYPPRYfYPFPPVGPVLYQVELSIGGQQFHGKGRTRQ 67
DSRM smart00358
Double-stranded RNA binding motif;
2773-2839 9.68e-16

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 73.84  E-value: 9.68e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1564222239  2773 PISRLAQIQQAKKeKEPEYSLVTERGLPRRREFIMQVQICDQI-AEGMGPNKKVAKRNAAEKMLELMG 2839
Cdd:smart00358    1 PKSLLQELAQKRK-LPPEYELVKEEGPDHAPRFTVTVKVGGKRtGEGEGSSKKEAKQRAAEAALRSLK 67
Sec7 cd00171
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ...
733-820 1.13e-15

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity.


Pssm-ID: 238100  Cd Length: 185  Bit Score: 77.65  E-value: 1.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  733 QKEIIEHGIELFNKKPKRGVQYLQEQGMLGV-TPEDIAQFLHQEERLD-------------------------------- 779
Cdd:cd00171      1 RKTLLSEGRQLFNRKPKKGISFLIEKGFLEDdSPKEIAKFLYETEGLNkkaigeylgennefnslvlhefvdlfdfsglr 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  780 ----------------------------------------------------------------TVKNKMTKEQYIKMNR 795
Cdd:cd00171     81 ldealrkflqsfrlpgeaqkidrllekfserycecnpgifsssadaaytlaysiimlntdlhnpNVKKKMTLEDFIKNLR 160
                          170       180
                   ....*....|....*....|....*
gi 1564222239  796 GINDSKDLPEENLSAIYDEIAGKKI 820
Cdd:cd00171    161 GINDGEDFPREFLKELYDSIKNNEI 185
IBN_N smart00913
Importin-beta N-terminal domain; Members of the importin-beta (karyopherin-beta) family can ...
1490-1563 8.47e-15

Importin-beta N-terminal domain; Members of the importin-beta (karyopherin-beta) family can bind and transport cargo by themselves, or can form heterodimers with importin-alpha. As part of a heterodimer, importin-beta mediates interactions with the pore complex, while importin-alpha acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo through the classical NLS import of proteins. Importin-beta is a helicoidal molecule constructed from 19 HEAT repeats. Many nuclear pore proteins contain FG sequence repeats that can bind to HEAT repeats within importins.. which is important for importin-beta mediated transport.


Pssm-ID: 197981 [Multi-domain]  Cd Length: 67  Bit Score: 71.12  E-value: 8.47e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564222239  1490 AEKFLESVEGNQNYPILLLTLLEKSQDNVIRVCAAVMFKNYIKRNWRIVEDEpnkicdiDRTAIKANIVNLMLS 1563
Cdd:smart00913    1 AEKQLEQFQKSPGFWLLLLEILANSEDQYVRQLAAITLKNKITRRWSSLPEE-------EKEEIKNSLLELLLS 67
Sec7 smart00222
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for ...
731-820 2.72e-12

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for proper protein transport through the Golgi. The domain facilitates guanine nucleotide exchange on the small GTPases, ARFs (ADP ribosylation factors).


Pssm-ID: 214569 [Multi-domain]  Cd Length: 189  Bit Score: 68.09  E-value: 2.72e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239   731 KQQKEIIEHGIELFNKKPKRGVQYLQEQGMLG-VTPEDIAQFLHQEERLD------------------------------ 779
Cdd:smart00222    2 KGRKKLLSEGIVKFNDKPKKGIQSLQEKGFLAnEDPQDVADFLSKNEGLNkkaigdylgehdefnrlvlhafvdlfdfsa 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239   780 -------------------------------------------------------------------TVKNKMTKEQYIK 792
Cdd:smart00222   82 kdldqalreflesfrlpgeaqkidrlleafssrycecnpgvfskanadaaytlayslimlntdlhnpNVKKKMTLEDFIK 161
                           170       180
                    ....*....|....*....|....*...
gi 1564222239   793 MNRGINDSKDLPEENLSAIYDEIAGKKI 820
Cdd:smart00222  162 NVRGSNDGEDLPREFLEELYDSIKNNEI 189
DSRM smart00358
Double-stranded RNA binding motif;
2471-2525 4.85e-12

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 63.44  E-value: 4.85e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564222239  2471 PMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYW-EAEGTSIKKSQH 2525
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTgEGEGSSKKEAKQ 56
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
2760-2839 1.48e-11

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 66.66  E-value: 1.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2760 KLQTSPEYGQGMNPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQ-IAEGMGPNKKVAKRNAAEKMLELM 2838
Cdd:COG0571    146 RLEEIAPGGAGKDYKTALQEWLQARGLPLPEYEVVEEEGPDHAKTFTVEVLVGGKvLGEGTGRSKKEAEQAAAKAALEKL 225

                   .
gi 1564222239 2839 G 2839
Cdd:COG0571    226 G 226
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
2773-2838 2.43e-10

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 58.40  E-value: 2.43e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2773 PISRLAQIQQaKKEKEPEYSLVTERGLPRRREFIMQVQICDQ-IAEGMGPNKKVAKRNAAEKMLELM 2838
Cdd:pfam00035    1 PKSLLQEYAQ-KNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKlYGSGTGSSKKEAEQLAAEKALEKL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
2471-2525 2.85e-08

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 52.62  E-value: 2.85e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564222239 2471 PMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEH-YWEAEGTSIKKSQH 2525
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKlYGSGTGSSKKEAEQ 56
DSRM smart00358
Double-stranded RNA binding motif;
2672-2715 5.51e-08

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 51.88  E-value: 5.51e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1564222239  2672 ISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGN---FSGDG 2715
Cdd:smart00358    2 KSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGkrtGEGEG 48
IBN_N pfam03810
Importin-beta N-terminal domain;
1490-1563 7.19e-07

Importin-beta N-terminal domain;


Pssm-ID: 397745 [Multi-domain]  Cd Length: 72  Bit Score: 48.77  E-value: 7.19e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564222239 1490 AEKFLESVEGNQNYPILLLTLLEKSQ-DNVIRVCAAVMFKNYIKRNWRiveDEPNKICDIDRTAIKANIVNLMLS 1563
Cdd:pfam03810    1 AEKQLEQFEKSPGFWSKLLQILSNSEnPLEVRQLAALYLKNLITRHWE---EEKNSLPPEEKEQIKNNLLNLLGS 72
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
2478-2524 4.23e-06

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 50.48  E-value: 4.23e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1564222239 2478 LARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYW-EAEGTSIKKSQ 2524
Cdd:COG0571    167 LQARGLPLPEYEVVEEEGPDHAKTFTVEVLVGGKVLgEGTGRSKKEAE 214
RNaseIII TIGR02191
ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. ...
2478-2524 8.52e-05

ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. This enzyme cleaves double-stranded rRNA. It is involved in processing ribosomal RNA precursors. It is found even in minimal genones such as Mycoplasma genitalium and Buchnera aphidicola, and in some cases has been shown to be an essential gene. These bacterial proteins contain a double-stranded RNA binding motif (pfam00035) and a ribonuclease III domain (pfam00636). Eukaryotic homologs tend to be much longer proteins with additional domains, localized to the nucleus, and not included in this family. [Transcription, RNA processing]


Pssm-ID: 274024 [Multi-domain]  Cd Length: 220  Bit Score: 46.43  E-value: 8.52e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1564222239 2478 LARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYW-EAEGTSIKKSQ 2524
Cdd:TIGR02191  162 AQARGKPLPEYRLIKEEGPDHDKEFTVEVSVNGEPYgEGKGKSKKEAE 209
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
2672-2715 1.36e-04

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 42.22  E-value: 1.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1564222239 2672 ISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGNF---SGDG 2715
Cdd:pfam00035    2 KSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKlygSGTG 48
 
Name Accession Description Interval E-value
PLN03076 PLN03076
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional
66-1343 0e+00

ARF guanine nucleotide exchange factor (ARF-GEF); Provisional


Pssm-ID: 215560 [Multi-domain]  Cd Length: 1780  Bit Score: 736.25  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239   66 SFIEADKYFLPFELACQSKSPRMVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRILETICNCFQgpQTDEGVQLQII 145
Cdd:PLN03076    80 SLAESELILSPLINACGTGSAKIVDPALDCIQKLIAHGYLRGEADPSGGPEALLLAKLIESVCKCHD--LGDEGIELLVL 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  146 KALLTAVTSPHIEIHEGTILLTVRTCYNIYLASRNLINQTTAKATLTQMLNVIFARMESQAAllTAVTSPHI--EIHEgt 223
Cdd:PLN03076   158 KTLLSAVTSTSLRIHGDCLLQAVRTCYDIYLGSKNVVNQTTAKASLIQMLVIVFRRMEADSS--TVPIQPIVvaELME-- 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  224 illtvrtcyniylasrnLINQTTAKATLTQMLnvifarmesqaalearevekerlrqqQSPVMPSVSDSPRLTrtqppeQ 303
Cdd:PLN03076   234 -----------------PAEKSDSDTSMTQFV--------------------------QGFITKIMQDIDGVL------N 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  304 PGTPETSAEqedGEQEDGEQEDGEQEDGEQENGEQENGDSEpengavqnkanlgqeakLPDDQFLPFCSFPKASDlhfhs 383
Cdd:PLN03076   265 PATAGKSSG---SGAHDGAFETTATVETTNPADLLDSTDKD-----------------MLDAKYWEISMYKSALE----- 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  384 vflGSEEQSVEMEIEKtvpetenkdtapsagrteaiqangilDDRASVlstdildpdavhgpaaaRFSHILQKDAFLVFR 463
Cdd:PLN03076   320 ---GRKGELADGEVEK--------------------------DDDLEV-----------------QIGNKLRRDAFLVFR 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  464 SLCKLSMK-PLSDGPPDPKSheLRSKVVSLQLLLSVLQSAGPVFRTHEMFVNAIKQYLCVALSKNGVSSVPDVFELSLAI 542
Cdd:PLN03076   354 ALCKLSMKtPPKEALADPQL--MRGKILALELLKILLENAGAVFRTSDRFLGAIKQYLCLSLLKNSASSLMIIFQLSCSI 431
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  543 FLTLLSNFKIHLKMQIEVFFREIFLTILETTSS-SFEHKWMVIQTLTRICADAQCVVDIYVNYDCDLNAANIFERLVNDL 621
Cdd:PLN03076   432 FISLVSRFRAGLKAEIGVFFPMIVLRVLENVAQpNFQQKMIVLRFLDKLCVDSQILVDIFINYDCDVNSSNIFERMVNGL 511
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  622 SKIAQG-RSGHELGMTPLQELSLRKKGLECLVSILKCMVEWSkdlyvnpNLQSNLGQEKPPEQESTESKILEVLARRDSA 700
Cdd:PLN03076   512 LKTAQGvPPGVETTLLPPQEAAMKLEAMKCLVAILRSMGDWM-------NKQLRLPDPASLKKLDAVENNLEPGSLPVAN 584
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  701 SSLDSTV--SSGIGSTSTQASLADDPEQYEVIKQQkeiIEHGIELFNKKPKRGVQYLQEQGMLGVTPEDIAQFL------ 772
Cdd:PLN03076   585 GNGDENGegSDSHSELSSETSDAATIEQRRAYKLE---LQEGISLFNRKPKKGIEFLINANKVGESPEEIAAFLkdasgl 661
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  773 ----------HQEE-------------------------------RL-----------------------------DT-- 780
Cdd:PLN03076   662 nktligdylgEREDlslkvmhayvdsfdfqgmefdeairaflqgfRLpgeaqkidrimekfaeryckcnpkafssaDTay 741
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  781 -----------------VKNKMTKEQYIKMNRGINDSKDLPEENLSAIYDEIAGKKIALKdskEHSITPKNsKQNVPTEK 843
Cdd:PLN03076   742 vlaysvimlntdahnpmVKNKMSADDFIRNNRGIDDGKDLPEEFMRSLYERISKNEIKMK---EDDLVPQQ-KQSANSNR 817
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  844 QRRLLYNLEMEQMAKTAKALMEA----VSHAQAPFT-----------SATHLEHVRPMFKLAWTPLLAAFSVGLQDCDDQ 908
Cdd:PLN03076   818 ILGLDSILNIVIRKRGEDSYMETsddlIKHMQEQFKekarksesvyyAATDVVILRFMVEVCWAPMLAAFSVPLDQSDDE 897
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  909 EVASLCLEGIRCAIRIACIFSMQLERDAYVQALARFTLLTASSSItemKQKNIDTIKTLITVAHTDGNYLGNSWHEILKC 988
Cdd:PLN03076   898 VVTFQCLEGFRHAIHVTAVMSMKTHRDAFVTSLAKFTSLHSPADI---KQKNIDAIKAIVSIADEDGNYLQEAWEHILTC 974
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  989 ISQLELAQLIGTG--------------------VKTRYISGVTRERQGSIR----GFPSGSEDFMPLGLGNLVGGGPDkk 1044
Cdd:PLN03076   975 VSRFEHLHLLGEGappdatffaapqnesdkskqAKSPILPVLKRKGPGKLQyaaaAVRRGSYDSAGVGGKASGVVTSE-- 1052
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1045 QMASIQESVGETSsQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELASPHHPRMFSLQKIVEISYYNMNRIRLQW 1124
Cdd:PLN03076  1053 QMNNLVSNLNMLE-QVGSFEMNRIFTRSQKLNSEAIIDFVKALCKVSMEELRSPSDPRVFSLTKIVEIAHYNMNRIRLVW 1131
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1125 SRIWQVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFMRPFEHIMKKNKSPTIRDMVIRCIAQMV 1204
Cdd:PLN03076  1132 SSIWHVLSDFFVTIGCSENLSIAIFAMDSLRQLSMKFLEREELANYNFQNEFMKPFVIVMRKSNAVEIRELIIRCVSQMV 1211
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1205 NSQAVNIRSGWKNIFSVFHQAASDHDETIVELAFQTTGHIVVSTFQNHFAAAIDSFQDAVKCLSEFVCNAAFPDTSMEAI 1284
Cdd:PLN03076  1212 LSRVNNVKSGWKSMFMVFTTAAYDDHKNIVLLAFEIIEKIIREYFPYITETETTTFTDCVNCLIAFTNSRFNKDISLNAI 1291
                         1370      1380      1390      1400      1410      1420      1430
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564222239 1285 RLIRHCAKYVSERPQALREYTSDDMNVAPGDRVWVRG----------------WFPVLFELSCIINRCKLDIRTS 1343
Cdd:PLN03076  1292 AFLRFCATKLAEGDLGSSSRNKDKEAPPSSPQSGKDGkqesgeftdkddhlyfWFPLLAGLSELSFDPRPEIRKS 1366
CAS_CSE1 pfam03378
CAS/CSE protein, C-terminus; Mammalian cellular apoptosis susceptibility (CAS) proteins are ...
1921-2337 0e+00

CAS/CSE protein, C-terminus; Mammalian cellular apoptosis susceptibility (CAS) proteins are homologous to the yeast chromosome-segregation protein, CSE1. This family aligns the C-terminal halves (approximately). CAS is involved in both cellular apoptosis and proliferation. Apoptosis is inhibited in CAS-depleted cells, while the expression of CAS correlates to the degree of cellular proliferation. Like CSE1, it is essential for the mitotic checkpoint in the cell cycle (CAS depletion blocks the cell in the G2 phase), and has been shown to be associated with the microtubule network and the mitotic spindle, as is the protein MEK, which is thought to regulate the intracellular localization (predominantly nuclear vs. predominantly cytosolic) of CAS. In the nucleus, CAS acts as a nuclear transport factor in the importin pathway. The importin pathway mediates the nuclear transport of several proteins that are necessary for mitosis and further progression. CAS is therefore thought to affect the cell cycle through its effect on the nuclear transport of these proteins. Since apoptosis also requires the nuclear import of several proteins (such as P53 and transcription factors), it has been suggested that CAS also enables apoptosis by facilitating the nuclear import of at least a subset of these essential proteins.


Pssm-ID: 367469  Cd Length: 435  Bit Score: 640.89  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1921 ERLFTMRGPNNTTLITAAEMAPFTEQLLLHLFKALSMPGSSENEYIMKAIMRSFSLLQESIVPYIPTLISQLTQKLLLVS 2000
Cdd:pfam03378    1 ERLLTLRDEQGQPIFTSADIAPFAKDLLTHLFAAIEKPGSQENEYLMKCIMRVLIVIQEAVLPVADVVLQHLTNILQEVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2001 KNPSKPHFNHYLFESLCLSVRITCKANPATVSSFEEALFPVFTEILQNDVQEFVPYVFQVMSLLLEMH-TTSIPPSYMAL 2079
Cdd:pfam03378   81 KNPSNPRFNHYLFEAIGALIRFACKADPAAVSKFEEALFPPFQAILQEDVTEFMPYVFQLLAQLLEANpSGTLPDYYMAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2080 FPHLLQPVLWERTGNIPPLVRLLQAYLQKGGTTIatTAADKIPGLLGVFQKLIASKANDHQGFYLLNSIIEHMPPDSINQ 2159
Cdd:pfam03378  161 FPPLLSPALWERRGNVPALVRLLSAFIPKASQEI--VANNKLEPVLGIFQKLIASKANDHQGFYLLESVIENFPPEVLEP 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2160 YKKQVFILLFQRLQSSKTTKFIKSFLVFINLHTVKYGAIATQEIFDSIQPKMFGMVLEKIVIPEVQKVSGPVEKKICAVG 2239
Cdd:pfam03378  239 YFKTIFSLLFQRLQNSKTEKFVKRFVIFYHLYSAKHGADFLIQLIDAIQPGVFGMIYLNVILPETQKLAGPLDRKLAAVS 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2240 ITKILTECPSMMDTdYTKLWSPLLQALIGFFELPEDDSIPDDEHFIDIEDTP--GYQTAFSQLAFAGKKEHDPIGDsVSN 2317
Cdd:pfam03378  319 YTKLLCESPAFADR-YPKGWGFLLQSLLKLLELPPDPAAADEDDIIDEADVDdmGYGVGFTQLNTAGKKERDPFPD-IPD 396
                          410       420
                   ....*....|....*....|
gi 1564222239 2318 PKILLAQSLHKLSTACPGRL 2337
Cdd:pfam03378  397 VKQWVGQSLKEASQAHPGRI 416
Cse1 pfam08506
Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the ...
1617-1920 1.14e-127

Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the nuclear export of importin alpha. This domain contains HEAT repeats.


Pssm-ID: 430038 [Multi-domain]  Cd Length: 370  Bit Score: 407.07  E-value: 1.14e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1617 LFKRYRHEFKSNELWTEIKLVLDTFAQPLTELFK---------------------------------------------- 1650
Cdd:pfam08506    1 IFKRWRPLFRSDELFLEIKLVLDKFAEPFLTLLQkvdelieanknnkaslkilfevllllcklfydlncqdipeffednm 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1651 ---------------------DEEEAGLLELLKSQICDNAALYAQKYDEEFQPYLPRFVTDIWNLLVTTGQEVKYDLLVS 1709
Cdd:pfam08506   81 kewmgifhkylsydnplletdDDEEATVLEKLKASICELVQLYTLRYEEEFGPMVNDFIQAVWNLLVSTSPQPKYDILVS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1710 NAIQFLASVCERPHYKHLFEDQNTLTSICEKVIVPNMEFRTADEEAFEDNSEEYIRRDLEGSDIDTRRRAACDLVRGLCK 1789
Cdd:pfam08506  161 KALSFLTSVARRPKYAELFNNESVLKQIIEKVVLPNVTLRESDEELFEDDPIEYIRRDLEGSDSDTRRRAATDFLKELKE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1790 FFEGPVTAIFSGYVNSMLTEYAKSPGTNWKHKDAAIYLVTSLASKAQTQKHGITQANELVNLTEFFVSHILPDLKsANVN 1869
Cdd:pfam08506  241 KFEALVTNVVLEYIQRLLEKYSANPSLNWKAKDTAIYLFTSIAAKGAVTKSGVTSTNPLVDVVDFFQQQIAPDLM-ANVN 319
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1564222239 1870 EFPVLKADAVKYVMIFRSQLPKEQLLVAIPLLIALLQAESIVAHTYAAHAL 1920
Cdd:pfam08506  320 QHPILKADAIKYIYTFRNQLTKEQLIEIFPLLINFLQSSSYVVYTYAAITI 370
CSE1 COG5657
CAS/CSE protein involved in chromosome segregation [Cell division and chromosome partitioning]; ...
1482-2329 7.08e-106

CAS/CSE protein involved in chromosome segregation [Cell division and chromosome partitioning];


Pssm-ID: 227944 [Multi-domain]  Cd Length: 947  Bit Score: 364.52  E-value: 7.08e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1482 PDPAVRRPAEKFLESVEGNQNYPILLLTL-LEKSQDNVIRVCAAVMFKNYIKRNWRivEDEPNKICDIDRTAIKANIVNL 1560
Cdd:COG5657     16 PDPPSVKCAEERLRQWEKQHGFALKLLSInLSAFNSMSLRWAALIQFKNYIDKHWR--EENGNSILPDENVLIRDELFSL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1561 MLSSPEQIQKQLSDAISIIGREDFPQKWPDLLTEMVNRFQSGDFHIINGVLRTAHSLFKRYRHEFKSNELWTEIKLVLDT 1640
Cdd:COG5657     94 IISSSNQLQIQNALAVSRIARLDFPDEWPTLVPDLLSLLSEKDMVTNENSLRVLHHIFKRLRRLFRSDALFLEIAPVLLS 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1641 FAQP---------------------------------------------------------------LTELFKDEEEAGL 1657
Cdd:COG5657    174 ILCPflfssayfwsmsenldesllslfqvclklirryydlgfqdipeffednldkfmehfckllsysNPVLQKDCLEDCV 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1658 LELLKSQICDNAALYAQKYDEEFQPYLPRFVTDIWNLLVTTGQEVKYDLLVSNAIQFLASVCERPHYKH----LFEDQNT 1733
Cdd:COG5657    254 YFKLKGSICEIFNLYTTKYPEVITYLIYDFVEIVWNLLTTITRPYIRDYLVSKSLTVLINVIKYPIRKTaevlSNVSENL 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1734 LTSICEKVIVPNMEFRTADEEAFEDNSEEYIRrdlEGSDIDTRRRAACDLVRGLCKFFEGpVTAIFSGYVNSMLTEYAKS 1813
Cdd:COG5657    334 INNLVDLLILPNLILREEDLEEWEDDPLEYIR---EQSKTDYEVNVRPCIENELKDLFDV-FGRIAVGHELTVIESEATT 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1814 PgtnwKHKDAAIYLVTSLASKAQtqkhGITQANELVNLTEFFVSHILPDLKSANVNEFPVLKADAVKYVMIFRSQLPKEQ 1893
Cdd:COG5657    410 P----NILDEARQLFAAYASFGL----GVEAVNRMVDFVKFLGSIIYPDLLSPNEIIHLRILRSRIAYILTFRNQLDSSE 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1894 LLVAiplliALLQAESIVAHTYAAHALERLFTMRGPNNTTL----ITAAEMAPFTEQLLLHLFKALSMPGS-SENEYIMK 1968
Cdd:COG5657    482 LSES-----KFLASQFFVNYTTACIDAVVLLTTREAYSTIFddwnFSVCSKIGLLENLILLVLSLMASPSSlEEREFLLQ 556
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1969 AIMRSFSLLQESIVPYIPTLISQLTQKLLLVSKNPSKPHFNHYLFESLCLSVRITCKANPATVSSFEEALFPVFTEILQN 2048
Cdd:COG5657    557 LISRIIIIDPELIAPLGSEILQLLDNLVEINAKNPSNPQFAHYTFEDIGALVFLKSGMCEITIPTLVLALVPEFPVLLSE 636
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2049 DVQEFVPYVFQVMSLLLEMHTT-SIPPSYMALFPHLLQPVLWERTGNIPPLVRLLQAYLQKGGTTIATTAADKIpglLGV 2127
Cdd:COG5657    637 DATELWSYVLQLLSILPEHFSGdVLPSVVKILRQPSLATELLPTKLEILKSYRLLDNPILTTGYIFKSSGFQPV---LGI 713
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2128 FQKLIASKANDHQGFyLLNSIIEHMPPDSINQ-YKKQVFILLFQRLQSSKTTKFIKSFLVFINLHTVKYGAIATQEIF-- 2204
Cdd:COG5657    714 LQYLLGSEPHDALCF-LNLTVVETLYLENIYEpYVNLIFVLLLSRLKNSKTERFVIKIIHVFSLVSFKDSLTVGCDNLis 792
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2205 --DSIQPKMFGMVLEKIVIPEVQkVSGPVEKKICAVGITKIL-TECPSMM-DTDYTKLWSPLLQALIGFFELP----EDD 2276
Cdd:COG5657    793 kiNQTKNILIVQLYGNWILGFDE-IHDSKDRKIHLIGLSNLLrTLHPEVLsYVSVTNLIISLLSEIFETASGDaiiyELN 871
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1564222239 2277 SIPDDEHFIDIEDtpgyQTAFSQLAFAGKKeHDPIgDSVSNPKILLAQSLHKL 2329
Cdd:COG5657    872 DDYADDWFDGEIS----AEEFSRLAQLEFK-VDPV-HDIDNTKYFISFFMEAM 918
DSRM_STAU1_rpt4 cd19885
fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen ...
2762-2847 1.45e-56

fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380714  Cd Length: 86  Bit Score: 191.07  E-value: 1.45e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2762 QTSPEYGQGMNPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLELMGFK 2841
Cdd:cd19885      1 QTSPEYGQGMNPISRLAQIQQAKKEKEPEYTLITERGLPRRREFVMQVKVGNQTAEGMGPNKKVAKRNAAEKMLELLGFK 80

                   ....*.
gi 1564222239 2842 VPQPQP 2847
Cdd:cd19885     81 VPQPQP 86
Sec7_N pfam12783
Guanine nucleotide exchange factor in Golgi transport N-terminal; The full-length Sec7 ...
454-609 3.90e-50

Guanine nucleotide exchange factor in Golgi transport N-terminal; The full-length Sec7 functions proximally in the secretory pathway as a protein binding scaffold for the coat protein complexes COPII-COPI. The COPII-COPI-protein switch is necessary for maturation of the vesicular-tubular cluster, VTC, intermediate compartments for Golgi compartment biogenesis. This N-terminal domain however does not appear to be binding either of the COP or the ARF.


Pssm-ID: 463703  Cd Length: 154  Bit Score: 175.38  E-value: 3.90e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  454 LQKDAFLVFRSLCKLS-MKPLSDgpPDPKSHELRSKVVSLQLLLSVLQSAGPVFRTHEMFVNAIKQYLCVALSKNGVSSV 532
Cdd:pfam12783    1 AAKDAFLVFRDLCKLSnGKPLSK--SDPKSHAERSKLFSLELIESILENHGDVFLKHPELLQLLKQYLCPSLLRNLSSSS 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239  533 PDVFELSLAIFLTLLSNFKIHLKMQIEVFFREIFLTILETTsSSFEHKWMVIQTLTRICADAQCVVDIYVNYDCDLN 609
Cdd:pfam12783   79 FPVFVRSLRIFLLLLRRFRSHLKLEIEVFLSLLILPLLESD-SSLWQKALVLEVLRRLCSDPQLLVEIYLNYDCDLG 154
Staufen_C pfam16482
Staufen C-terminal domain; This is the C-terminal domain of Staufen proteins. It consists of ...
2934-3037 2.19e-47

Staufen C-terminal domain; This is the C-terminal domain of Staufen proteins. It consists of an N-terminal Staufen-swapping motif (SSM) comprising two alpha helices, connected by a linker region to a dsRNA-binding-like domain ('RBD'). The 'RBD' has the fold of a functional dsRNA-binding domain, but lacks the residues required to bind RNA. This domain is responsible for dimerization, the SSM from one molecule interacts with the 'RBD' of another.


Pssm-ID: 465131  Cd Length: 110  Bit Score: 165.85  E-value: 2.19e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2934 KATITAMMARELLYGGTSPTAETLLKSNNNLVHLPHGPlTRPSEQLDFLTKVQGLQVEYKDFPKNNKNEFVSLINCSSQP 3013
Cdd:pfam16482    2 KATVTAAIARELLYGGTSPTAEAILKNNGKTGAVPCGL-VQPSQQLEYLARVQGFQVEYSDFPRQNKNEFLSLLTLSSQP 80
                           90       100
                   ....*....|....*....|....
gi 1564222239 3014 PLISHGIGKDVESCHDMVRASLRK 3037
Cdd:pfam16482   81 VQMTHGIGSSLEASHDQAALSALK 104
DSRM_STAU2_rpt4 cd19886
fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen ...
2769-2850 4.39e-39

fourth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins; Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380715  Cd Length: 86  Bit Score: 141.25  E-value: 4.39e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2769 QGMNPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLELMGFKVPQPQPT 2848
Cdd:cd19886      1 QGMNPISRLAQIQQAKKEKEPEYVLLSERGMPRRREFVMQVKVGNEVATGTGPNKKIAKRNAAEAMLLQLGYKASTPLQD 80

                   ..
gi 1564222239 2849 KP 2850
Cdd:cd19886     81 QT 82
DUF1981 pfam09324
Domain of unknown function (DUF1981); Members of this family of functionally uncharacterized ...
1160-1241 1.33e-38

Domain of unknown function (DUF1981); Members of this family of functionally uncharacterized domains are found in various plant and yeast protein transport proteins.


Pssm-ID: 462756  Cd Length: 84  Bit Score: 139.55  E-value: 1.33e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1160 KFLEKGELANFRFQKDFMRPFEHIMKKNKSPTIRDMVIRCIAQMVNSQAVNIRSGWKNIFSVFHQAASDHDETIVELAFQ 1239
Cdd:pfam09324    1 KFLEKEELSNFKFQKDFLKPFEYIMSNNSSVDVKELVLECILQMIQSKGDNIKSGWKTIFGVLTAAAKDSNESLVRLAFQ 80

                   ..
gi 1564222239 1240 TT 1241
Cdd:pfam09324   81 IL 82
DSRM_STAU_rpt4 cd19860
fourth double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
2772-2839 7.41e-38

fourth double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the fourth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380689  Cd Length: 68  Bit Score: 137.08  E-value: 7.41e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1564222239 2772 NPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLELMG 2839
Cdd:cd19860      1 NPISRLIQIQQARKEKEPVYSLVAERGTPRRREFVMQVTVGDKTATGTGPNKKLAKRNAAEAMLELLG 68
DCB pfam16213
dimerization and cyclophilin-binding domain of Mon2; DCB is the N-terminal domain of Mon2- and ...
15-202 2.21e-36

dimerization and cyclophilin-binding domain of Mon2; DCB is the N-terminal domain of Mon2- and GIG1-like proteins from metazoa. Mon2 and BIG1 like proteins play an important role in the cytoplasm-to-vacuole transport pathway and are required for Golgi homeostasis.


Pssm-ID: 465072 [Multi-domain]  Cd Length: 172  Bit Score: 136.62  E-value: 2.21e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239   15 LSRALE---KILSdKEVKRaQHSQLRKTCqvalgkEHVCVLLILLDGSVVVPKASFIEADKYFLPFELACQSKSPRMVST 91
Cdd:pfam16213    5 LLEALQsdlRTLS-SEAKR-KYPPVKEAS------EKGILRLRTVHSSSPLMQNLLSASEDILKPFVLACETKNPKLVQI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239   92 SLDCLQKLIAYGHITGNApdsgapgkrlIDRILETICNCFQGPQTdegVQLQIIKALLTAVTSPHIeIHEGTILLTVRTC 171
Cdd:pfam16213   77 ALGCLQKLISHDAISQSA----------APYILDTLWMLMELGSE---IELKVLQTVLLLITTNSV-IHGDTLAKALVLC 142
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1564222239  172 YNIYLASRNlINQTTAKATLTQMLNVIFARM 202
Cdd:pfam16213  143 FRLHFSKDP-TVQNTASATLRQLVSVVFERV 172
DSRM_STAU1_rpt1 cd19879
first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2467-2525 3.93e-36

first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380708  Cd Length: 66  Bit Score: 132.12  E-value: 3.93e-36
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1564222239 2467 KEKTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQH 2525
Cdd:cd19879      1 KEKTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFTVQLTLGDQHWEAEGTSIKKAQH 59
DSRM_STAU2_rpt1 cd19880
first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2465-2525 2.20e-33

first double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins; Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380709  Cd Length: 68  Bit Score: 124.44  E-value: 2.20e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564222239 2465 NPKEKTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQH 2525
Cdd:cd19880      1 NPKEKTPMCLVNELARFNRIQPQYKLLNERGPAHAKIFTVQLTLGEQTWEAEGSSIKKAQH 61
BIG2_C pfam20252
BIG2 C-terminal domain; This presumed domain is found at the C-terminus of BIG2 the brefeldin ...
1370-1481 3.24e-33

BIG2 C-terminal domain; This presumed domain is found at the C-terminus of BIG2 the brefeldin A-inhibited guanine nucleotide-exchange protein. The function of this region is unknown.


Pssm-ID: 466403  Cd Length: 178  Bit Score: 127.74  E-value: 3.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1370 QGMYRYMSSPHLFKLLDSLLESHTFAKAFNSNSEQRTALWRAGFkGKSKPNLLKQETSSLACCLRILFRMYMDENLK-DS 1448
Cdd:pfam20252   15 DEHYESLPSDHLLRLLDCLEKSYTFARSFNSDLELRTALWRAGF-MKQLPNLLKQETSSLSTYLRILFRLYADDEPRtSQ 93
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1564222239 1449 WKDIQTRLLRCInmdlnaanLQTLTEYLRKTLD 1481
Cdd:pfam20252   94 REEVEERLIPLC--------EDILEYYLSLDEE 118
DSRM_STAU1_rpt5 cd19887
fifth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2974-3037 3.48e-31

fifth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fifth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380716  Cd Length: 70  Bit Score: 118.23  E-value: 3.48e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564222239 2974 RPSEQLDFLTKVQGLQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMVRASLRK 3037
Cdd:cd19887      1 RPSEQLDYLSRVQGLQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMAALNILK 64
DSRM_STAU1_rpt3 cd19883
third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2669-2735 2.62e-28

third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380712  Cd Length: 67  Bit Score: 109.72  E-value: 2.62e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2669 KSEISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGNFSGDGEGKSKKIAKKNAAAAVLEEL 2735
Cdd:cd19883      1 KSEISQVFEIALKRNMPVNFEVTKETGPPHMKSFVTKVSVGEFAGEGEGKSKKISKKNAAIAVLEEL 67
DSRM_STAU1_rpt2 cd19881
second double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen ...
2566-2631 5.00e-27

second double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 1 (Staufen 1) and similar proteins; Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 1 contains five double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380710  Cd Length: 79  Bit Score: 106.50  E-value: 5.00e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2566 MKLGKKPTYRPIDSYHGMRPNFNYNVRAPGPYPRYY-YPFSPVGPVLYQMEVSIGEQLFHGKGRTRQ 2631
Cdd:cd19881      1 MKLGKKPIYKPIDPYTGMRSAYNYNMRGNGAYPPRYfYPFPPVGPVLYQVELSIGGQQFHGKGRTRQ 67
DSRM_STAU_rpt1 cd19857
first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
2470-2525 1.19e-26

first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380686  Cd Length: 64  Bit Score: 105.04  E-value: 1.19e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2470 TPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHY-WEAEGTSIKKSQH 2525
Cdd:cd19857      1 TPMCLLNELARFNKIRPQYTLVDEEGPAHKKTFTVKLTLGDEEeYEASGSSIKKAQH 57
DSRM_STAU2_rpt3 cd19884
third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2669-2735 6.57e-24

third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins; Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380713  Cd Length: 67  Bit Score: 97.38  E-value: 6.57e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2669 KSEISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGNFSGDGEGKSKKIAKKNAAAAVLEEL 2735
Cdd:cd19884      1 KSEISLVFEIALKRNMPVSFEVIKESGPPHMKSFVTRVTVGEFTAEGEGNSKKLSKKRAATSVLQEL 67
DSRM_STAU_rpt3 cd19859
third double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
2671-2735 6.96e-23

third double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380688  Cd Length: 65  Bit Score: 94.00  E-value: 6.96e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564222239 2671 EISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGNFSGDGEGKSKKIAKKNAAAAVLEEL 2735
Cdd:cd19859      1 EISLVHEIALKRNLTVNFEVLRESGPPHMKNFITRCTVGSFVTEGEGNSKKVSKKRAAEKMLEEL 65
Sec7 pfam01369
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ...
733-820 8.21e-23

Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family.


Pssm-ID: 460178  Cd Length: 183  Bit Score: 98.30  E-value: 8.21e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  733 QKEIIEHGIELFNKKPKRGVQYLQEQGMLGVTPEDIAQFLHQEERLD--------------------------------- 779
Cdd:pfam01369    1 RKKLLREGIEKFNKKPKKGIEYLIEKGFIEDDPESIAKFLFETPGLDkkaigeylgkpdefnievlkafvdlfdfkglri 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  780 --------------------------------------------------------------TVKNKMTKEQYIKMNRGI 797
Cdd:pfam01369   81 dealrlflesfrlpgeaqkidrimeafaeryyeqnpgvfanadaayvlaysiimlntdlhnpNVKKKMTLEDFIRNLRGI 160
                          170       180
                   ....*....|....*....|...
gi 1564222239  798 NDSKDLPEENLSAIYDEIAGKKI 820
Cdd:pfam01369  161 NDGKDFPDEYLEEIYDSIKKNEI 183
SXM1 COG5656
Importin, protein involved in nuclear import [Posttranslational modification, protein turnover, ...
1470-2118 8.47e-20

Importin, protein involved in nuclear import [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227943 [Multi-domain]  Cd Length: 970  Bit Score: 97.62  E-value: 8.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1470 QTLTEYLRKTLDPDPAVRRPAEKFLESVEGNQNYPILLLTLLekSQDNV---IRVCAAVMFKNYIKRNWRIVEDEPNK-- 1544
Cdd:COG5656      3 EELLQCFLQTLDADAGKRTIAEAMLKDLEKQPGFVMALLHIC--SKDEGdlnVKLSAAIYFKNKIIRSWSSKRDDGIKad 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1545 ICDIDRTAIKANIVNLMLSSPEQIQKQLSDAISIIGREDFPQKWPDLLTEMVNRFQSGDFHIINGVLRTAHSLFKRYRH- 1623
Cdd:COG5656     81 EKSEAKKYLIENILDVFLYSPEVTRTALNAILVNIFSEDKPSDLWGLFPKAANLLRSSEANHVYTGLLCLEELFKAYRWk 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1624 --------------------------EFKSNELWTEI-KLVLDTF-----------------------------AQPLTE 1647
Cdd:COG5656    161 yndeqvdilmlitalfpilekvggnlESQGNYGSVETlMLILKSFksvcyyslpdflsaietfsswfqlslrilQKPLPN 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1648 --LFKDEEEAGLLELLK---------SQICD--NAALYAQKYDEEFQPYLPRF---------VTDIWnllvTTGQ----- 1700
Cdd:COG5656    241 evLSLDPEVRSLSKWVKckkwaaynlYRSFQryIKKSYKKSYLSFYITFMTRVpmilatffkQIEEW----GQGQlwlsd 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1701 EVKYDLL-----VSNAIQFLASVceRPHYKHLFEDqntltsicekVIVPNMEFRTADEEAFEDNSEEYIRRDLEGSDIDT 1775
Cdd:COG5656    317 IELYFIDffvelCVDADQTWRLM--EPHLQYIISG----------VIFPLLCLSEEEEELFENDPDEYIRRYYDFFDNGL 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1776 RRRAACDLVRGLCKFFEGPVTaiFSG---YVNSMLTEYAKSPGT--NWKHKDAAIYLVTSLASKaqtqkhgITQANELVN 1850
Cdd:COG5656    385 SPDLAALFFLIISKSKRKEET--FQGilsFLLSILGQSAATPSNidNARQAEGALRLLASIKSF-------ITKMSPAAN 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1851 LTEFF-VSHILPDLKSanvnEFPVLKADAVKYVMIFRSQLP-KEQLLVAIPLLIALLQAESIVAHTYAAHALERLFTmrg 1928
Cdd:COG5656    456 VMEYFiVNHVIPAFRS----NYGFLKSRACEFISTIEEDFKdNGILLEAYENTHNCLKNNHLPVMIEAALALQFFIF--- 528
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 1929 pNNTTLITAAEMAPFTEQLLLHLFKALSMPGSSEneyIMKAIMRSFSllqESIVPYIPTLISQLTQKLLLVS----KNPS 2004
Cdd:COG5656    529 -NEQSHEKFSAHVPETMEKLLSLSNTFEIDPLSM---VMESFVEYFS---EELSPFAPELAGSLVRQFLKIAqsllENSS 601
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2005 KPHFNH-----------YLFESLCLSVRITckanPATVSSFEEALFPVFTEILQNDVQEFVPYVFQvmslLLEMHTTSIp 2073
Cdd:COG5656    602 DTSSVVddkqmaasgilRTIESMILSLENR----PLVLKYLEVSLYPVISFILKNEISDFYQEALD----ILDGYTFMS- 672
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*
gi 1564222239 2074 psymalfpHLLQPVLWertgnipPLVRLLQAYLQKGGTTIATTAA 2118
Cdd:COG5656    673 --------KEIEPIMW-------GIFELLLNLLIDEITAVYSEEV 702
DSRM_STAU_rpt5 cd19861
fifth double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
2975-3035 5.32e-19

fifth double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the fifth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380690  Cd Length: 68  Bit Score: 83.04  E-value: 5.32e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564222239 2975 PSEQLDFLTKVQGLQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMvrASL 3035
Cdd:cd19861      1 PKEQLEYLAKVLGFSVEFTDFPKGNKSEYLSLVSLGTEPPQVCHGSGSSVEESRDA--AAL 59
DSRM smart00358
Double-stranded RNA binding motif;
2773-2839 9.68e-16

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 73.84  E-value: 9.68e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1564222239  2773 PISRLAQIQQAKKeKEPEYSLVTERGLPRRREFIMQVQICDQI-AEGMGPNKKVAKRNAAEKMLELMG 2839
Cdd:smart00358    1 PKSLLQELAQKRK-LPPEYELVKEEGPDHAPRFTVTVKVGGKRtGEGEGSSKKEAKQRAAEAALRSLK 67
Sec7 cd00171
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ...
733-820 1.13e-15

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity.


Pssm-ID: 238100  Cd Length: 185  Bit Score: 77.65  E-value: 1.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  733 QKEIIEHGIELFNKKPKRGVQYLQEQGMLGV-TPEDIAQFLHQEERLD-------------------------------- 779
Cdd:cd00171      1 RKTLLSEGRQLFNRKPKKGISFLIEKGFLEDdSPKEIAKFLYETEGLNkkaigeylgennefnslvlhefvdlfdfsglr 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  780 ----------------------------------------------------------------TVKNKMTKEQYIKMNR 795
Cdd:cd00171     81 ldealrkflqsfrlpgeaqkidrllekfserycecnpgifsssadaaytlaysiimlntdlhnpNVKKKMTLEDFIKNLR 160
                          170       180
                   ....*....|....*....|....*
gi 1564222239  796 GINDSKDLPEENLSAIYDEIAGKKI 820
Cdd:cd00171    161 GINDGEDFPREFLKELYDSIKNNEI 185
IBN_N smart00913
Importin-beta N-terminal domain; Members of the importin-beta (karyopherin-beta) family can ...
1490-1563 8.47e-15

Importin-beta N-terminal domain; Members of the importin-beta (karyopherin-beta) family can bind and transport cargo by themselves, or can form heterodimers with importin-alpha. As part of a heterodimer, importin-beta mediates interactions with the pore complex, while importin-alpha acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo through the classical NLS import of proteins. Importin-beta is a helicoidal molecule constructed from 19 HEAT repeats. Many nuclear pore proteins contain FG sequence repeats that can bind to HEAT repeats within importins.. which is important for importin-beta mediated transport.


Pssm-ID: 197981 [Multi-domain]  Cd Length: 67  Bit Score: 71.12  E-value: 8.47e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564222239  1490 AEKFLESVEGNQNYPILLLTLLEKSQDNVIRVCAAVMFKNYIKRNWRIVEDEpnkicdiDRTAIKANIVNLMLS 1563
Cdd:smart00913    1 AEKQLEQFQKSPGFWLLLLEILANSEDQYVRQLAAITLKNKITRRWSSLPEE-------EKEEIKNSLLELLLS 67
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
2771-2838 2.59e-12

double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase III (EC 3.1.26.3; also known as ribonuclease 3) digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. It is involved in the processing of rRNA precursors, viral transcripts, some mRNAs, and at least 1 tRNA (metY, a minor form of tRNA-init-Met). It cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs. The cleavage can occur in assembled 30S, 50S, and even 70S subunits and is influenced by the presence of ribosomal proteins. The RNase III family also includes the mitochondrion-specific ribosomal protein mL44 subfamily, which is composed of mitochondrial 54S ribosomal protein L3 (MRPL3) and mitochondrial 39S ribosomal protein L44 (MRPL44). Members of this family contain an RNase III domain and a C-terminal double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380682 [Multi-domain]  Cd Length: 69  Bit Score: 64.05  E-value: 2.59e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1564222239 2771 MNPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQ-IAEGMGPNKKVAKRNAAEKMLELM 2838
Cdd:cd10845      1 KDYKTALQEYLQKRGLPLPEYELVEEEGPDHNKTFTVEVKVNGKvIGEGTGRSKKEAEQAAAKAALEKL 69
Sec7 smart00222
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for ...
731-820 2.72e-12

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for proper protein transport through the Golgi. The domain facilitates guanine nucleotide exchange on the small GTPases, ARFs (ADP ribosylation factors).


Pssm-ID: 214569 [Multi-domain]  Cd Length: 189  Bit Score: 68.09  E-value: 2.72e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239   731 KQQKEIIEHGIELFNKKPKRGVQYLQEQGMLG-VTPEDIAQFLHQEERLD------------------------------ 779
Cdd:smart00222    2 KGRKKLLSEGIVKFNDKPKKGIQSLQEKGFLAnEDPQDVADFLSKNEGLNkkaigdylgehdefnrlvlhafvdlfdfsa 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239   780 -------------------------------------------------------------------TVKNKMTKEQYIK 792
Cdd:smart00222   82 kdldqalreflesfrlpgeaqkidrlleafssrycecnpgvfskanadaaytlayslimlntdlhnpNVKKKMTLEDFIK 161
                           170       180
                    ....*....|....*....|....*...
gi 1564222239   793 MNRGINDSKDLPEENLSAIYDEIAGKKI 820
Cdd:smart00222  162 NVRGSNDGEDLPREFLEELYDSIKNNEI 189
DSRM smart00358
Double-stranded RNA binding motif;
2471-2525 4.85e-12

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 63.44  E-value: 4.85e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564222239  2471 PMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYW-EAEGTSIKKSQH 2525
Cdd:smart00358    1 PKSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTgEGEGSSKKEAKQ 56
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
2760-2839 1.48e-11

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 66.66  E-value: 1.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2760 KLQTSPEYGQGMNPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQ-IAEGMGPNKKVAKRNAAEKMLELM 2838
Cdd:COG0571    146 RLEEIAPGGAGKDYKTALQEWLQARGLPLPEYEVVEEEGPDHAKTFTVEVLVGGKvLGEGTGRSKKEAEQAAAKAALEKL 225

                   .
gi 1564222239 2839 G 2839
Cdd:COG0571    226 G 226
DSRM_SF cd00048
double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 ...
2779-2835 1.72e-11

double-stranded RNA binding motif (DSRM) superfamily; DSRM (also known as dsRBM) is a 65-70 amino acid domain that adopts an alpha-beta-beta-beta-alpha fold. It is not sequence specific, but highly specific for double-stranded RNAs (dsRNAs) of various origin and structure. The DSRM domains are found in a variety of proteins including dsRNA dependent protein kinase PKR, RNA helicases, Drosophila Staufen protein, E. coli RNase III, RNase H1, and dsRNA dependent adenosine deaminases. They are involved in numerous cellular mechanisms ranging from localization and transport of messenger RNAs, through maturation and degradation of RNAs, to viral response and signal transduction. Some members harbor tandem DSRMs that act in small RNA biogenesis.


Pssm-ID: 380679 [Multi-domain]  Cd Length: 57  Bit Score: 61.53  E-value: 1.72e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2779 QIQQAKKEKEPEYSLVTERGlPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKML 2835
Cdd:cd00048      2 ELCQKNKWPPPEYETVEEGG-PHNPRFTCTVTVNGQTFEGEGKSKKEAKQAAAEKAL 57
DSRM_PRKRA_rpt2 cd19891
second double-stranded RNA binding motif of protein activator of the interferon-induced ...
2772-2835 6.08e-11

second double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins; PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. PRKRA contains three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380720  Cd Length: 67  Bit Score: 60.34  E-value: 6.08e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564222239 2772 NPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKML 2835
Cdd:cd19891      1 NPIGSLQELAVQKGWRLPEYTLAQESGPPHKREFTITCRVETFVETGTGTSKKVAKRNAAEKLL 64
DSRM_PRKRA-like_rpt2 cd19863
second double-stranded RNA binding motif of PRKRA, TARBP2 and similar proteins; The family ...
2772-2838 9.08e-11

second double-stranded RNA binding motif of PRKRA, TARBP2 and similar proteins; The family includes protein activator of the interferon-induced protein kinase (PRKRA) and the RISC-loading complex subunit TARBP2. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. TARBP2 (also called TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)) participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. The family also includes Drosophila melanogaster Loquacious and similar proteins. Loquacious (Loqs) is a double-stranded RNA-binding domain (dsRBD) protein, a homolog of human TAR RNA binding protein (TRBP) that is a protein first identified as binding the HIV trans-activator RNA (TAR). Loqs interacts with Dicer1 (dmDcr1) to facilitate miRNA processing. PRKRA family proteins contain three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380692  Cd Length: 67  Bit Score: 59.70  E-value: 9.08e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2772 NPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLELM 2838
Cdd:cd19863      1 NPVGILQELCVQRRWRLPEYEVEQESGPPHEKEFTIACRVENFSETGSGKSKKLAKRAAAEKMLTRL 67
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
2773-2838 2.43e-10

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 58.40  E-value: 2.43e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2773 PISRLAQIQQaKKEKEPEYSLVTERGLPRRREFIMQVQICDQ-IAEGMGPNKKVAKRNAAEKMLELM 2838
Cdd:pfam00035    1 PKSLLQEYAQ-KNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKlYGSGTGSSKKEAEQLAAEKALEKL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
2471-2525 2.85e-08

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 52.62  E-value: 2.85e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564222239 2471 PMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEH-YWEAEGTSIKKSQH 2525
Cdd:pfam00035    1 PKSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKlYGSGTGSSKKEAEQ 56
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
2465-2524 3.82e-08

double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase III (EC 3.1.26.3; also known as ribonuclease 3) digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. It is involved in the processing of rRNA precursors, viral transcripts, some mRNAs, and at least 1 tRNA (metY, a minor form of tRNA-init-Met). It cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs. The cleavage can occur in assembled 30S, 50S, and even 70S subunits and is influenced by the presence of ribosomal proteins. The RNase III family also includes the mitochondrion-specific ribosomal protein mL44 subfamily, which is composed of mitochondrial 54S ribosomal protein L3 (MRPL3) and mitochondrial 39S ribosomal protein L44 (MRPL44). Members of this family contain an RNase III domain and a C-terminal double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380682 [Multi-domain]  Cd Length: 69  Bit Score: 52.49  E-value: 3.82e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564222239 2465 NPKEKtpmcLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYW-EAEGTSIKKSQ 2524
Cdd:cd10845      2 DYKTA----LQEYLQKRGLPLPEYELVEEEGPDHNKTFTVEVKVNGKVIgEGTGRSKKEAE 58
DSRM smart00358
Double-stranded RNA binding motif;
2672-2715 5.51e-08

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 51.88  E-value: 5.51e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1564222239  2672 ISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGN---FSGDG 2715
Cdd:smart00358    2 KSLLQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGkrtGEGEG 48
DSRM_TARBP2_rpt2 cd10844
second double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and ...
2772-2835 1.04e-07

second double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar proteins; TARBP2 (also known as TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)) participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. TARBP2 contains three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380681  Cd Length: 67  Bit Score: 51.26  E-value: 1.04e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564222239 2772 NPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKML 2835
Cdd:cd10844      1 NPVGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKML 64
DSRM_STAU2_rpt5 cd19888
fifth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2974-3037 1.15e-07

fifth double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins; Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the fifth motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380717  Cd Length: 68  Bit Score: 51.11  E-value: 1.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564222239 2974 RPSEQLDFLTKVQGLQVEYKDfpKNNKNEFVSLINCSSQpPLISHGIGKDVESCHDMVRASLRK 3037
Cdd:cd19888      2 QPSKQLEYLARIQGFQVQYSD--RQNGKECMTCLTLSPV-QMTFHGIGSSIEASHDQAALSALK 62
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
2770-2840 2.02e-07

double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known as Bax antagonist selected in saccharomyces 1 (BASS1), negative regulatory element-binding protein (NRE-binding protein), or protein DBP-5, or SON3) is an RNA-binding protein which acts as an mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. It specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Members of this group contain a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380699  Cd Length: 75  Bit Score: 50.74  E-value: 2.02e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564222239 2770 GMNPISRLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQ--IAEGMGPNKKVAKRNAAEKMLELMGF 2840
Cdd:cd19870      1 GKHPVSALMELCNKRKWGPPEFRLVEESGPPHRKHFLFKVVVNGVeyQPSVASGNKKDAKAQAATVALQALGL 73
DSRM_STRBP_RED-like_rpt2 cd19866
second double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
2772-2836 2.03e-07

second double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3), as well as two RNA-editing deaminases, RED1 and RED2. STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. RED1 (EC 3.5.4.37; also called double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. RED2 (also called double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA but also to ssRNA. RED2 lacks editing activity for currently known substrate RNAs. Members of this group contain two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380695  Cd Length: 63  Bit Score: 50.24  E-value: 2.03e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564222239 2772 NPISRLAQIQQAKKekepeYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLE 2836
Cdd:cd19866      2 NPVMLLNELRPGLK-----YKCLSESGESHAKSFVMSVTVDGQTFEGTGRSKKLAKAAAAQAALA 61
DSRM_PRKRA-like_rpt1 cd19862
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
2469-2525 3.70e-07

first double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins; This family includes protein activator of the interferon-induced protein kinase (PRKRA) and the RISC-loading complex subunit TARBP2. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. TARBP2 (also called TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)), participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. This family also includes Drosophila melanogaster Loquacious and similar proteins. Loquacious (Loqs) is a double-stranded RNA-binding domain (dsRBD) protein, a homolog of human TAR RNA binding protein (TRBP) that is a protein first identified as binding the HIV trans-activator RNA (TAR). Loqs interacts with Dicer1 (dmDcr1) to facilitate miRNA processing. PRKRA family proteins contain three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380691 [Multi-domain]  Cd Length: 70  Bit Score: 49.57  E-value: 3.70e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2469 KTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQH 2525
Cdd:cd19862      1 KTPISVLQELCAKRGITPKYELISSEGAVHEPTFTFRVTVGDITATGSGTSKKKAKH 57
IBN_N pfam03810
Importin-beta N-terminal domain;
1490-1563 7.19e-07

Importin-beta N-terminal domain;


Pssm-ID: 397745 [Multi-domain]  Cd Length: 72  Bit Score: 48.77  E-value: 7.19e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564222239 1490 AEKFLESVEGNQNYPILLLTLLEKSQ-DNVIRVCAAVMFKNYIKRNWRiveDEPNKICDIDRTAIKANIVNLMLS 1563
Cdd:pfam03810    1 AEKQLEQFEKSPGFWSKLLQILSNSEnPLEVRQLAALYLKNLITRHWE---EEKNSLPPEEKEQIKNNLLNLLGS 72
DSRM_STRBP_rpt1 cd19909
first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) ...
2471-2524 8.80e-07

first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins; STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. STRBP contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380738  Cd Length: 84  Bit Score: 49.26  E-value: 8.80e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564222239 2471 PMclvNELARFNKIQP--EYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQ 2524
Cdd:cd19909      5 PM---NALMRLNQIRPglQYKLLSQSGPVHAPVFTMSVDVDGTTYEASGPSKKTAK 57
DSRM_STRBP_rpt2 cd19911
second double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) ...
2772-2836 3.68e-06

second double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins; STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. STRBP contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380740  Cd Length: 64  Bit Score: 46.66  E-value: 3.68e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564222239 2772 NPISRLAQiqqakKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLE 2836
Cdd:cd19911      2 NPVMELNE-----KRRGLKYELISETGGSHDKRFVMEVEVDGQKFRGAGPNKKVAKASAALAALE 61
Rnc COG0571
dsRNA-specific ribonuclease [Transcription];
2478-2524 4.23e-06

dsRNA-specific ribonuclease [Transcription];


Pssm-ID: 440336 [Multi-domain]  Cd Length: 229  Bit Score: 50.48  E-value: 4.23e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1564222239 2478 LARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYW-EAEGTSIKKSQ 2524
Cdd:COG0571    167 LQARGLPLPEYEVVEEEGPDHAKTFTVEVLVGGKVLgEGTGRSKKEAE 214
DSRM_STRBP-like_rpt2 cd19897
second double-stranded RNA binding motif of STRBP, ILF3 and similar proteins; This family ...
2772-2836 4.64e-06

second double-stranded RNA binding motif of STRBP, ILF3 and similar proteins; This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3). STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Members of this STRBP/ILF3 group contain an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380726  Cd Length: 64  Bit Score: 46.59  E-value: 4.64e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564222239 2772 NPISRLAQiqqakKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLE 2836
Cdd:cd19897      2 NPVMELNE-----KRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKANAALAALE 61
DSRM_STAU2_rpt2 cd19882
second double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen ...
2559-2632 6.11e-06

second double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins; Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380711  Cd Length: 82  Bit Score: 46.63  E-value: 6.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2559 VELNALCMKLGKKPTYRPIDS--YHGMRPNFN----YNVRAPGpypryyypfsPVGPVLYqMEVSIGEQLFHGKGRTRQA 2632
Cdd:cd19882      1 VELNGLAMKRGEPAIYRPIDPkpPPNYRPNYNfrgmYNQRYHY----------PMPKTFY-VSLTVGNREFIGEGRTRQA 69
DSRM_ILF3_rpt2 cd19912
second double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and ...
2769-2836 6.68e-06

second double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and similar proteins; ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. ILF3 contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380741  Cd Length: 72  Bit Score: 46.18  E-value: 6.68e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1564222239 2769 QGMNPISRLAQiqqakKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLE 2836
Cdd:cd19912      5 HGKNPVMELNE-----KRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALE 67
DSRM_STRBP-like_rpt1 cd19894
first double-stranded RNA binding motif of STRBP, ILF3 and similar proteins; This family ...
2476-2524 8.75e-06

first double-stranded RNA binding motif of STRBP, ILF3 and similar proteins; This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3). STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Members of this STRBP/ILF3 group contain an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380723  Cd Length: 63  Bit Score: 45.45  E-value: 8.75e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1564222239 2476 NELARFNKIQP--EYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQ 2524
Cdd:cd19894      2 NALMRLNQLRPglQYKLASQTGPVHAPQFTMSVEVDGVTYEASGPSKKTAK 52
DSRM_STRBP_RED-like_rpt1 cd19865
first double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
2771-2836 1.00e-05

first double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3), as well as two RNA-editing deaminases, RED1 and RED2. STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. RED1 (EC 3.5.4.37; also called double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. RED2 (also called double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA, but also to ssRNA. RED2 lacks editing activity for currently known substrate RNAs. Members of this group contain two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380694  Cd Length: 63  Bit Score: 45.42  E-value: 1.00e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1564222239 2771 MNPISRLAQIQQAKKekepeYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLE 2836
Cdd:cd19865      1 KNALMQLNELRPGLQ-----YKLTSQTGPVHAPVFTMSVEVNGQTFEGTGRSKKKAKLEAAEKALR 61
DSRM_STRBP_rpt1 cd19909
first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) ...
2769-2840 1.40e-05

first double-stranded RNA binding motif of spermatid perinuclear RNA-binding protein (STRBP) and similar proteins; STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. STRBP contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380738  Cd Length: 84  Bit Score: 45.79  E-value: 1.40e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564222239 2769 QGMNPISRLAQIQQAKkekepEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLELMGF 2840
Cdd:cd19909      4 QPMNALMRLNQIRPGL-----QYKLLSQSGPVHAPVFTMSVDVDGTTYEASGPSKKTAKLHVAVKVLQAMGY 70
DSRM_PRKRA-like_rpt1 cd19862
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
2669-2735 2.14e-05

first double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins; This family includes protein activator of the interferon-induced protein kinase (PRKRA) and the RISC-loading complex subunit TARBP2. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. TARBP2 (also called TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)), participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. This family also includes Drosophila melanogaster Loquacious and similar proteins. Loquacious (Loqs) is a double-stranded RNA-binding domain (dsRBD) protein, a homolog of human TAR RNA binding protein (TRBP) that is a protein first identified as binding the HIV trans-activator RNA (TAR). Loqs interacts with Dicer1 (dmDcr1) to facilitate miRNA processing. PRKRA family proteins contain three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380691 [Multi-domain]  Cd Length: 70  Bit Score: 44.56  E-value: 2.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2669 KSEISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGNFSGDGEGKSKKIAKKNAAAAVLEEL 2735
Cdd:cd19862      1 KTPISVLQELCAKRGITPKYELISSEGAVHEPTFTFRVTVGDITATGSGTSKKKAKHAAAENALEQL 67
DSRM_ILF3_rpt1 cd19910
first double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and ...
2471-2538 2.17e-05

first double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and similar proteins; ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. ILF3 contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380739  Cd Length: 73  Bit Score: 44.75  E-value: 2.17e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2471 PMCLVNELARFNKIQP--EYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQHAAAARALAETTLP 2538
Cdd:cd19910      2 PPQAMNALMRLNQLKPglQYKLISQTGPVHAPVFTMSVEVDGKTFEASGPSKKTAKLHVAVKVLQDMGLP 71
DSRM_RED1_rpt1 cd19895
first double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins; ...
2471-2524 2.41e-05

first double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins; RED1 (EC 3.5.4.37; also known as double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. It contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the first DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380724  Cd Length: 72  Bit Score: 44.69  E-value: 2.41e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564222239 2471 PMCLVNELARFNKIQP--EYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQ 2524
Cdd:cd19895      2 PVLPKNALMQLNEIKPglQYKLLSQTGPVHAPVFVMSVEVNGQVFEGSGPTKKKAK 57
DSRM_STAU_rpt3 cd19859
third double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
2471-2524 3.38e-05

third double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380688  Cd Length: 65  Bit Score: 43.93  E-value: 3.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1564222239 2471 PMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQ 2524
Cdd:cd19859      1 EISLVHEIALKRNLTVNFEVLRESGPPHMKNFITRCTVGSFVTEGEGNSKKVSK 54
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
2668-2710 4.87e-05

double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known as Bax antagonist selected in saccharomyces 1 (BASS1), negative regulatory element-binding protein (NRE-binding protein), or protein DBP-5, or SON3) is an RNA-binding protein which acts as an mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. It specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Members of this group contain a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380699  Cd Length: 75  Bit Score: 43.81  E-value: 4.87e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1564222239 2668 NKSEISQVFEIALKRN-MPVNFEVLRETGPPHMKSFVMKVSVGN 2710
Cdd:cd19870      1 GKHPVSALMELCNKRKwGPPEFRLVEESGPPHRKHFLFKVVVNG 44
DSRM_STRBP_RED-like_rpt1 cd19865
first double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This ...
2476-2525 4.92e-05

first double-stranded RNA binding motif of STRBP, ILF3, RED1, RED2 and similar proteins; This family includes spermatid perinuclear RNA-binding protein (STRBP) and interleukin enhancer-binding factor 3 (ILF3), as well as two RNA-editing deaminases, RED1 and RED2. STRBP is a double-stranded DNA and RNA binding protein that is involved in spermatogenesis and sperm function. It plays a role in regulation of cell growth. ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. RED1 (EC 3.5.4.37; also called double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. RED2 (also called double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA, but also to ssRNA. RED2 lacks editing activity for currently known substrate RNAs. Members of this group contain two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380694  Cd Length: 63  Bit Score: 43.49  E-value: 4.92e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1564222239 2476 NELARFNKIQP--EYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQH 2525
Cdd:cd19865      2 NALMQLNELRPglQYKLTSQTGPVHAPVFTMSVEVNGQTFEGTGRSKKKAKL 53
RNaseIII TIGR02191
ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. ...
2478-2524 8.52e-05

ribonuclease III, bacterial; This family consists of bacterial examples of ribonuclease III. This enzyme cleaves double-stranded rRNA. It is involved in processing ribosomal RNA precursors. It is found even in minimal genones such as Mycoplasma genitalium and Buchnera aphidicola, and in some cases has been shown to be an essential gene. These bacterial proteins contain a double-stranded RNA binding motif (pfam00035) and a ribonuclease III domain (pfam00636). Eukaryotic homologs tend to be much longer proteins with additional domains, localized to the nucleus, and not included in this family. [Transcription, RNA processing]


Pssm-ID: 274024 [Multi-domain]  Cd Length: 220  Bit Score: 46.43  E-value: 8.52e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1564222239 2478 LARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYW-EAEGTSIKKSQ 2524
Cdd:TIGR02191  162 AQARGKPLPEYRLIKEEGPDHDKEFTVEVSVNGEPYgEGKGKSKKEAE 209
DSRM_DHX9_rpt1 cd19854
first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; ...
2784-2831 9.35e-05

first double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; DHX9 (EC 3.6.4.13; also known as ATP-dependent RNA helicase A, DExH-box helicase 9 (DDX9), Leukophysin (LKP), nuclear DNA helicase II (NDH II), NDH2, or RNA helicase A) is a multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation, and RNA-mediated gene silencing. It contains two double-stranded RNA binding motifs (DSRMs) at the N-terminal region. This model corresponds to the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380683  Cd Length: 69  Bit Score: 42.64  E-value: 9.35e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2784 KKEKEPEYSlVTERGLPRRREFIMQVQI--CDQIAEGMGPNKKVAKRNAA 2831
Cdd:cd19854     12 KKKLTPEYD-IKEAGNKHRQRFKCEVRVegFDYVGTGNATNKKDAQTNAA 60
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
2772-2838 9.82e-05

first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380732  Cd Length: 68  Bit Score: 42.76  E-value: 9.82e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1564222239 2772 NPISRLAQIQQAKKEKEpEYSLVTERGLPRRREFIMQVQICDQ-IAEGMGPNKKVAKRNAAEKMLELM 2838
Cdd:cd19903      2 NYMGKLNEYCQKQKVVL-DYVEVPTSGPSHDPRFTFQVVIDGKeYPEGEGKSKKEAKQAAAKLALEIL 68
DSRM_RED1_rpt2 cd19898
second double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar ...
2769-2835 1.02e-04

second double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins; RED1 (EC 3.5.4.37; also known as double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. It contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the second DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380727  Cd Length: 70  Bit Score: 42.87  E-value: 1.02e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2769 QGMNPISRLAQIQQAKKekepeYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKML 2835
Cdd:cd19898      1 SGKNPVMILNELRPGLK-----YEFVSESGESHAKNFVMSVTVDGQTFEGSGRNKKLAKARAAQAAL 62
COG5137 COG5137
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ...
262-365 1.19e-04

Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];


Pssm-ID: 227466 [Multi-domain]  Cd Length: 279  Bit Score: 46.91  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  262 MESQAALEAREVEKERLRQQQSPVMPSV-SDSPRLTRTQ------------PPEQPGTPEtsAEQEDGEQEDGEQEDGEQ 328
Cdd:COG5137    117 YPGITKLEKSDVEEPSEKVDEEDVEREIlAEKPRVTRFNivwdndedndeaPPAQPDVDN--EEEERLEESDGREEEEDE 194
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1564222239  329 EDGEQENGEQENG----DSEPENGAVQNKANLGQEAKLPDD 365
Cdd:COG5137    195 EVGSDSYGEGNRElneeEEEEAEGSDDGEDVVDYEGERIDK 235
DSRM_RED1_rpt1 cd19895
first double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins; ...
2773-2835 1.35e-04

first double-stranded RNA binding motif of RNA-editing deaminase 1 (RED1) and similar proteins; RED1 (EC 3.5.4.37; also known as double-stranded RNA-specific editase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase, ADARB1, ADAR2, or DRADA2) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. It contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the first DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380724  Cd Length: 72  Bit Score: 42.37  E-value: 1.35e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564222239 2773 PISRLAQIQQAKKEKEpeYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKML 2835
Cdd:cd19895      5 PKNALMQLNEIKPGLQ--YKLLSQTGPVHAPVFVMSVEVNGQVFEGSGPTKKKAKLHAAEKAL 65
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
2672-2715 1.36e-04

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 42.22  E-value: 1.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1564222239 2672 ISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGNF---SGDG 2715
Cdd:pfam00035    2 KSLLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKlygSGTG 48
DSRM_RED2_rpt1 cd19896
first double-stranded RNA binding motif of RNA-editing deaminase 2 (RED2) and similar proteins; ...
2476-2524 1.45e-04

first double-stranded RNA binding motif of RNA-editing deaminase 2 (RED2) and similar proteins; RED2 (also known as double-stranded RNA-specific editase B2, RNA-dependent adenosine deaminase 3, RNA-editing enzyme 2, dsRNA adenosine deaminase B2, ADAR3, or ADARB2) prevents the binding of other ADAR enzymes to targets in vitro, and decreases the efficiency of these enzymes. It is capable of binding to dsRNA but also to ssRNA. RED2 contains two double-stranded RNA binding motifs (DSRMs) and a C-terminal RNA-specific adenosine-deaminase (editase) domain. This model describes the first DSRM. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure. RED2 lacks editing activity for currently known substrate RNAs, and may have an inactive editase domain.


Pssm-ID: 380725  Cd Length: 74  Bit Score: 42.39  E-value: 1.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1564222239 2476 NELARFNKIQP--EYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQ 2524
Cdd:cd19896      7 NALVQLNELKPglQYRMVSQTGPVHAPVFAVAVEVNGLTFEGTGPTKKKAK 57
DSRM_ILF3_rpt1 cd19910
first double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and ...
2769-2840 1.79e-04

first double-stranded RNA binding motif of interleukin enhancer-binding factor 3 (ILF3) and similar proteins; ILF3 (also known as double-stranded RNA-binding protein 76 (DRBP76), M-phase phosphoprotein 4 (MPP4), nuclear factor associated with dsRNA (NFAR), nuclear factor of activated T-cells 90 kDa (NF-AT-90), or translational control protein 80 (TCP80)) is an RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. ILF3 contains an N-terminal DZF domain and two double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380739  Cd Length: 73  Bit Score: 42.43  E-value: 1.79e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564222239 2769 QGMNPISRLAQIQQAKkekepEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLELMGF 2840
Cdd:cd19910      4 QAMNALMRLNQLKPGL-----QYKLISQTGPVHAPVFTMSVEVDGKTFEASGPSKKTAKLHVAVKVLQDMGL 70
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
301-380 2.19e-04

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 46.71  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239  301 PEQPGTPETSAEQEDGEQEDGEQEDGEQEDGEQENGEQENGDSEPENGAVQNKANLGQEAKLPDDQFLPFCSFPKASDLH 380
Cdd:COG4547    227 GEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAEEGESEAAEAESDEMAEEAEGEDSEEPGEPWRPNAPPPDDPADPDYK 306
DSRM_TARBP2_rpt1 cd19890
first double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar ...
2770-2838 2.47e-04

first double-stranded RNA binding motif of the RISC-loading complex subunit TARBP2 and similar proteins; TARBP2 (also known as TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)), participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. TARBP2 contains three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380719  Cd Length: 72  Bit Score: 41.66  E-value: 2.47e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1564222239 2770 GMNPISrLAQIQQAKKEKEPEYSLVTERGLPRRREFIMQVQICDQIAEGMGPNKKVAKRNAAEKMLELM 2838
Cdd:cd19890      2 GKTPIS-LLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDISCTGQGPSKKAAKHKAAEVALKLL 69
DSRM_DRADA cd19902
double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) ...
2772-2835 2.81e-04

double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) and similar proteins; DRADA (EC 3.5.4.37; also known as 136 kDa double-stranded RNA-binding protein (p136), interferon-inducible protein 4 (IFI-4), K88DSRBP, ADAR1, G1P1, or ADAR) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. DRADA family members contain at least one double-stranded RNA binding motifs (DSRM); vertebrate proteins contain three. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380731  Cd Length: 71  Bit Score: 41.51  E-value: 2.81e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564222239 2772 NPISRLAQIQQAKKEkEPEYSLVTERGLPRRREFIMQVQICD-QIAEGMGPNKKVAKRNAAEKML 2835
Cdd:cd19902      2 NPVSALMEYAQSRGV-TAEIEVLSQSGPPHNPRFKAAVFVGGrRFPSVEASSKKDAKQEAADLAL 65
DSRM_DRADA_rpt2 cd19914
second double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase ...
2772-2839 2.87e-04

second double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) and similar proteins; DRADA (EC 3.5.4.37; also known as 136 kDa double-stranded RNA-binding protein (p136), interferon-inducible protein 4 (IFI-4), K88DSRBP, ADAR1, G1P1, or ADAR) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. Vertebrate DRADA contains three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380743  Cd Length: 71  Bit Score: 41.37  E-value: 2.87e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564222239 2772 NPISRLAQIQQaKKEKEPEYSLVTERGLPRRREFIMQVQICDQI-AEGMGPNKKVAKRNAAEK-MLELMG 2839
Cdd:cd19914      2 NPISVLMEHSQ-KSGNMCEFQLLSQEGPPHDPKFTYCVKVGEQTfPSVVANSKKVAKQMAAEEaVKELMG 70
DSRM_PRKRA-like_rpt3 cd19864
third double-stranded RNA binding motif of PRKRA, TARBP2 and similar proteins; The family ...
2975-3036 4.13e-04

third double-stranded RNA binding motif of PRKRA, TARBP2 and similar proteins; The family includes protein activator of the interferon-induced protein kinase (PRKRA) and the RISC-loading complex subunit TARBP2. PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. TARBP2 (also called TAR RNA-binding protein 2, or trans-activation-responsive RNA-binding protein (TRBP)) participates in the formation of the RNA-induced silencing complex (RISC). It is part of the RISC-loading complex (RLC), together with dicer1 and eif2c2/ago2, and is required to process precursor miRNAs. The family also includes Drosophila melanogaster Loquacious and similar proteins. Loquacious (Loqs) is a double-stranded RNA-binding domain (dsRBD) protein, a homolog of human TAR RNA binding protein (TRBP) that is a protein first identified as binding the HIV trans-activator RNA (TAR). Loqs interacts with Dicer1 (dmDcr1) to facilitate miRNA processing. PRKRA family proteins contain three double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380693  Cd Length: 72  Bit Score: 41.06  E-value: 4.13e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564222239 2975 PSEQLDFLTKVQGLQVEYKDFPKNNKN-EFVSLINCSSQPPLISHGIGKDVESCH-DMVRASLR 3036
Cdd:cd19864      3 YCELLQELAEEQKFKVTYVDIEELSSSgKYQCLVQLSTLPPTVCHGSGASLEEAKeEAARNALE 66
DSRM_RNAse_III_family cd10845
double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase ...
2673-2718 6.32e-04

double-stranded RNA binding motif of ribonuclease III (RNase III) and similar proteins; RNase III (EC 3.1.26.3; also known as ribonuclease 3) digests double-stranded RNA formed within single-strand substrates, but not RNA-DNA hybrids. It is involved in the processing of rRNA precursors, viral transcripts, some mRNAs, and at least 1 tRNA (metY, a minor form of tRNA-init-Met). It cleaves the 30S primary rRNA transcript to yield the immediate precursors to the 16S and 23S rRNAs. The cleavage can occur in assembled 30S, 50S, and even 70S subunits and is influenced by the presence of ribosomal proteins. The RNase III family also includes the mitochondrion-specific ribosomal protein mL44 subfamily, which is composed of mitochondrial 54S ribosomal protein L3 (MRPL3) and mitochondrial 39S ribosomal protein L44 (MRPL44). Members of this family contain an RNase III domain and a C-terminal double-stranded RNA binding motif (DSRM). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380682 [Multi-domain]  Cd Length: 69  Bit Score: 40.55  E-value: 6.32e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1564222239 2673 SQVFEIALKRNMP-VNFEVLRETGPPHMKSFVMKVSV-GNFSGDGEGK 2718
Cdd:cd10845      5 TALQEYLQKRGLPlPEYELVEEEGPDHNKTFTVEVKVnGKVIGEGTGR 52
DSRM_PRKRA_rpt1 cd19889
first double-stranded RNA binding motif of protein activator of the interferon-induced protein ...
2469-2525 1.36e-03

first double-stranded RNA binding motif of protein activator of the interferon-induced protein kinase (PRKRA) and similar proteins; PRKRA (also known as interferon-inducible double-stranded RNA-dependent protein kinase activator A, PKR-associated protein X (RAX), PKR-associating protein X, protein kinase, interferon-inducible double-stranded RNA-dependent activator, PACT, or HSD14) is a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. PRKRA contains three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380718 [Multi-domain]  Cd Length: 71  Bit Score: 39.51  E-value: 1.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564222239 2469 KTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQH 2525
Cdd:cd19889      2 KTPIQLLHEYGTKTGNIPVYELEKSEGQAHLPSFTFRVTVGDITCTGEGTSKKLAKH 58
DSRM_DCL_plant cd19869
double-stranded RNA binding motif of plant Dicer-like proteins; The family includes plant ...
2486-2516 3.86e-03

double-stranded RNA binding motif of plant Dicer-like proteins; The family includes plant Dicer-like (DCL) proteins and other ribonuclease (RNase) III-like (RTL) proteins. DCLs are endoribonucleases involved in RNA-mediated post-transcriptional gene silencing (PTGS). They function in the microRNA (miRNA) biogenesis pathway by cleaving primary miRNAs (pri-miRNAs) and precursor miRNAs (pre-miRNAs). Family members contain a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380698  Cd Length: 70  Bit Score: 38.50  E-value: 3.86e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1564222239 2486 PEYKLLSEQGPAHSK--VFSVRLTLNEHYWEAE 2516
Cdd:cd19869     12 PVYRCVEEEGPAHAKrfTYMVRVKIPERGWTIE 44
DSRM_STAU_rpt1 cd19857
first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
2672-2715 3.87e-03

first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380686  Cd Length: 64  Bit Score: 38.02  E-value: 3.87e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1564222239 2672 ISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVGN---FSGDG 2715
Cdd:cd19857      3 MCLLNELARFNKIRPQYTLVDEEGPAHKKTFTVKLTLGDeeeYEASG 49
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
2472-2524 4.36e-03

first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380732  Cd Length: 68  Bit Score: 38.14  E-value: 4.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1564222239 2472 MCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNE-HYWEAEGTSIKKSQ 2524
Cdd:cd19903      4 MGKLNEYCQKQKVVLDYVEVPTSGPSHDPRFTFQVVIDGkEYPEGEGKSKKEAK 57
DSRM_DRADA cd19902
double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) ...
2669-2709 4.40e-03

double-stranded RNA binding motif of double-stranded RNA-specific adenosine deaminase (DRADA) and similar proteins; DRADA (EC 3.5.4.37; also known as 136 kDa double-stranded RNA-binding protein (p136), interferon-inducible protein 4 (IFI-4), K88DSRBP, ADAR1, G1P1, or ADAR) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA), referred to as A-to-I RNA editing. DRADA family members contain at least one double-stranded RNA binding motifs (DSRM); vertebrate proteins contain three. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380731  Cd Length: 71  Bit Score: 38.04  E-value: 4.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1564222239 2669 KSEISQVFEIALKRNMPVNFEVLRETGPPHMKSFVMKVSVG 2709
Cdd:cd19902      1 KNPVSALMEYAQSRGVTAEIEVLSQSGPPHNPRFKAAVFVG 41
DSRM_STAU_rpt1 cd19857
first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein ...
2772-2835 4.49e-03

first double-stranded RNA binding motif of Drosophila melanogaster maternal effect protein Staufen and similar proteins; Staufen is a double-stranded RNA binding protein required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. The family also includes two Staufen homologs from vertebrates, Staufen 1 and Staufen 2. They are present in distinct ribonucleoprotein complexes and associate with different mRNAs. Staufen 1 may play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. It binds double-stranded RNA (regardless of the sequence) and tubulin. Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen proteins contain five double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380686  Cd Length: 64  Bit Score: 38.02  E-value: 4.49e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1564222239 2772 NPISRLAQIqqAKKEK-EPEYSLVTERGLPRRREFIMQVQICDQIA-EGMGPNKKVAKRNAAEKML 2835
Cdd:cd19857      1 TPMCLLNEL--ARFNKiRPQYTLVDEEGPAHKKTFTVKLTLGDEEEyEASGSSIKKAQHAAAEKAL 64
DSRM_STAU2_rpt3 cd19884
third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog ...
2469-2524 7.23e-03

third double-stranded RNA binding motif of double-stranded RNA-binding protein Staufen homolog 2 (Staufen 2) and similar proteins; Staufen 2 is an RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. Staufen 2 contains five double-stranded RNA binding motifs (DSRMs). This model describes the third motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380713  Cd Length: 67  Bit Score: 37.68  E-value: 7.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564222239 2469 KTPMCLVNELARFNKIQPEYKLLSEQGPAHSKVFSVRLTLNEHYWEAEGTSIKKSQ 2524
Cdd:cd19884      1 KSEISLVFEIALKRNMPVSFEVIKESGPPHMKSFVTRVTVGEFTAEGEGNSKKLSK 56
DSRM_SON-like cd19870
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ...
2469-2509 9.27e-03

double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known as Bax antagonist selected in saccharomyces 1 (BASS1), negative regulatory element-binding protein (NRE-binding protein), or protein DBP-5, or SON3) is an RNA-binding protein which acts as an mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. It specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Members of this group contain a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380699  Cd Length: 75  Bit Score: 37.26  E-value: 9.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1564222239 2469 KTPMCLVNELARFNK-IQPEYKLLSEQGPAHSKVFSVRLTLN 2509
Cdd:cd19870      2 KHPVSALMELCNKRKwGPPEFRLVEESGPPHRKHFLFKVVVN 43
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH