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Conserved domains on  [gi|968104248|ref|XP_015027484|]
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RB1-inducible coiled-coil protein 1 isoform X1 [Drosophila virilis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ubl_RB1CC1 cd17060
ubiquitin-like (Ubl) domain found in retinoblastoma 1-inducible coiled-coil protein 1 (RB1CC1) ...
2-74 1.29e-34

ubiquitin-like (Ubl) domain found in retinoblastoma 1-inducible coiled-coil protein 1 (RB1CC1) and similar proteins; RB1CC1, also termed FAK family kinase-interacting protein of 200 kDa (FIP200), is the mammalian counterpart of the yeast Atg17 gene and functions as a component of the ULK1/Atg13/RB1CC1/Atg101 complex essential for induction of autophagy. RB1CC1 is a key signaling node to regulate cellular proliferation and differentiation. As a DNA-binding transcription factor, RB1CC1 has been implicated in the regulation of retinoblastoma 1 (RB1) expression. RB1CC1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, as well as a nuclear localization signal (KPRK), a leucine zipper motif and a coiled-coil structure.


:

Pssm-ID: 340580  Cd Length: 75  Bit Score: 126.91  E-value: 1.29e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 968104248    2 MLYVFHVDVGRMLSFDMTVALSSVENLKETIQRLHGLPAANIVLLVSGGEMLTHSTQVSCYSAGTDTNPIFMF 74
Cdd:cd17060     1 MLYVFLVNTGTMLTFDMSLAVQSVSDLKEAIEEKTKIPVEKQVLLVSGGESLDPDKRVSSYSAGTDTNPIFLF 73
ATG11 pfam10377
Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, ...
929-1085 5.05e-22

Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, Schizosaccharomyces pombe, this protein has been shown to interact with the telomere cap complex and it is also required for dimerization and kinase activation of Atg1. However, in budding yeast, Saccharomyces cerevisiae, this protein is called ATG11 and is shown to be involved in autophagy.


:

Pssm-ID: 463063  Cd Length: 130  Bit Score: 93.05  E-value: 5.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   929 ESSVAAMRSSTYELgaagmSGTLTRSKSSGGGGGGGGSSSSsHRHITLEGCSKGDLVFVIWSMRHGQ-----FMVVQDSL 1003
Cdd:pfam10377    1 ESAVIKRFKDVETL-----AKKLTKENKSKREKLEKLQSEA-HEKITLKNFKVGDLALFLPTRRHNDlstppWAAFNVGA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  1004 TLYFVHADSLPALQLTAptttassslppgaegplavaelnhiplpyYAIGRIIDKEYCQAR---KDENRYRVSKGSKFYR 1080
Cdd:pfam10377   75 PHYFLKADSLLALKSRE-----------------------------WFVGRITSIEERVVDlsdKDSNPFKLSKGTVWYL 125

                   ....*
gi 968104248  1081 IKLAP 1085
Cdd:pfam10377  126 VTAEE 130
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
122-538 1.41e-16

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


:

Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 83.21  E-value: 1.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   122 LETVRQRATLAQRLRELGRKEELLCERLVHEQHLQQQGWSAVVANMEDLTSEFSERFHNFcLAFDRHLEQResYLELLRN 201
Cdd:pfam04108    2 LSSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNEL-KKDFKQLLKD--LDAALER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   202 FGDDLKQLARIPILPALmalaQADFHGFDELLgnDNVDEDVGQlqpetetevgesgesveksssstspnkklKMGHEQEE 281
Cdd:pfam04108   79 LEETLDKLRNTPVEPAL----PPGEEKQKTLL--DFIDEDSVE-----------------------------ILRDALKE 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   282 QEETSNSRqqqqqhqlnllqwisskgnhaalqqmcdecVQGLDTfSLEIYEKLKLEVQNIIKSAKQSD--VKEIKGLSDR 359
Cdd:pfam04108  124 LIDELQAA------------------------------QESLDS-DLKRFDDDLRDLQKELESLSSPSesISLIPTLLKE 172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   360 LYRL-DEFKYEIRKIVQVQREQATAFQQNESRAVNLRD---------NSVLPDLCLSHRSqlmvMRDNHIKIREYSRCIA 429
Cdd:pfam04108  173 LESLeEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEvlendarelDDVVPELQDRLDE----MENNYERLQKLLEQKN 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   430 NSKEELGRNLNTrlrrivwiengMSEFDNRLLFYLRCLRRAERHIS--------IIEQIHRA-------PSTYVAAVTEV 494
Cdd:pfam04108  249 SLIDELLSALQL-----------IAEIQSRLPEYLAALKEFEERWEeeketiedYLSELEDLrefyegfPSAYGSLLLEV 317
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 968104248   495 VRRKIFSDEFRLWASRLSVDFDRIHSEEMERRRLFNDSFdGHFL 538
Cdd:pfam04108  318 ERRREWAEKMKKILRKLAEELDRLQEEERKRREKFLKEV-GDFL 360
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
755-945 6.30e-04

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  755 REQLIHEHKTELESLRCRFKLMTSMErsPSDSSLEKLERPTSSASVASLDVEQLLAQQRQELLAQRERaISEAVEAERAL 834
Cdd:PRK03918  264 LEERIEELKKEIEELEEKVKELKELK--EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  835 WQSRQQLPPLNSEsvmanvsilKDVLEDKERQLDLLREqnqlLTQESYQLKTRLEMLTNEDgnswLKEKIDYLSRDKCRL 914
Cdd:PRK03918  341 EELKKKLKELEKR---------LEELEERHELYEEAKA----KKEELERLKKRLTGLTPEK----LEKELEELEKAKEEI 403
                         170       180       190
                  ....*....|....*....|....*....|.
gi 968104248  915 EEELSQEKSKRLEMESSVAAMRSSTYELGAA 945
Cdd:PRK03918  404 EEEISKITARIGELKKEIKELKKAIEELKKA 434
 
Name Accession Description Interval E-value
Ubl_RB1CC1 cd17060
ubiquitin-like (Ubl) domain found in retinoblastoma 1-inducible coiled-coil protein 1 (RB1CC1) ...
2-74 1.29e-34

ubiquitin-like (Ubl) domain found in retinoblastoma 1-inducible coiled-coil protein 1 (RB1CC1) and similar proteins; RB1CC1, also termed FAK family kinase-interacting protein of 200 kDa (FIP200), is the mammalian counterpart of the yeast Atg17 gene and functions as a component of the ULK1/Atg13/RB1CC1/Atg101 complex essential for induction of autophagy. RB1CC1 is a key signaling node to regulate cellular proliferation and differentiation. As a DNA-binding transcription factor, RB1CC1 has been implicated in the regulation of retinoblastoma 1 (RB1) expression. RB1CC1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, as well as a nuclear localization signal (KPRK), a leucine zipper motif and a coiled-coil structure.


Pssm-ID: 340580  Cd Length: 75  Bit Score: 126.91  E-value: 1.29e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 968104248    2 MLYVFHVDVGRMLSFDMTVALSSVENLKETIQRLHGLPAANIVLLVSGGEMLTHSTQVSCYSAGTDTNPIFMF 74
Cdd:cd17060     1 MLYVFLVNTGTMLTFDMSLAVQSVSDLKEAIEEKTKIPVEKQVLLVSGGESLDPDKRVSSYSAGTDTNPIFLF 73
ATG11 pfam10377
Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, ...
929-1085 5.05e-22

Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, Schizosaccharomyces pombe, this protein has been shown to interact with the telomere cap complex and it is also required for dimerization and kinase activation of Atg1. However, in budding yeast, Saccharomyces cerevisiae, this protein is called ATG11 and is shown to be involved in autophagy.


Pssm-ID: 463063  Cd Length: 130  Bit Score: 93.05  E-value: 5.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   929 ESSVAAMRSSTYELgaagmSGTLTRSKSSGGGGGGGGSSSSsHRHITLEGCSKGDLVFVIWSMRHGQ-----FMVVQDSL 1003
Cdd:pfam10377    1 ESAVIKRFKDVETL-----AKKLTKENKSKREKLEKLQSEA-HEKITLKNFKVGDLALFLPTRRHNDlstppWAAFNVGA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  1004 TLYFVHADSLPALQLTAptttassslppgaegplavaelnhiplpyYAIGRIIDKEYCQAR---KDENRYRVSKGSKFYR 1080
Cdd:pfam10377   75 PHYFLKADSLLALKSRE-----------------------------WFVGRITSIEERVVDlsdKDSNPFKLSKGTVWYL 125

                   ....*
gi 968104248  1081 IKLAP 1085
Cdd:pfam10377  126 VTAEE 130
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
122-538 1.41e-16

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 83.21  E-value: 1.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   122 LETVRQRATLAQRLRELGRKEELLCERLVHEQHLQQQGWSAVVANMEDLTSEFSERFHNFcLAFDRHLEQResYLELLRN 201
Cdd:pfam04108    2 LSSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNEL-KKDFKQLLKD--LDAALER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   202 FGDDLKQLARIPILPALmalaQADFHGFDELLgnDNVDEDVGQlqpetetevgesgesveksssstspnkklKMGHEQEE 281
Cdd:pfam04108   79 LEETLDKLRNTPVEPAL----PPGEEKQKTLL--DFIDEDSVE-----------------------------ILRDALKE 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   282 QEETSNSRqqqqqhqlnllqwisskgnhaalqqmcdecVQGLDTfSLEIYEKLKLEVQNIIKSAKQSD--VKEIKGLSDR 359
Cdd:pfam04108  124 LIDELQAA------------------------------QESLDS-DLKRFDDDLRDLQKELESLSSPSesISLIPTLLKE 172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   360 LYRL-DEFKYEIRKIVQVQREQATAFQQNESRAVNLRD---------NSVLPDLCLSHRSqlmvMRDNHIKIREYSRCIA 429
Cdd:pfam04108  173 LESLeEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEvlendarelDDVVPELQDRLDE----MENNYERLQKLLEQKN 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   430 NSKEELGRNLNTrlrrivwiengMSEFDNRLLFYLRCLRRAERHIS--------IIEQIHRA-------PSTYVAAVTEV 494
Cdd:pfam04108  249 SLIDELLSALQL-----------IAEIQSRLPEYLAALKEFEERWEeeketiedYLSELEDLrefyegfPSAYGSLLLEV 317
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 968104248   495 VRRKIFSDEFRLWASRLSVDFDRIHSEEMERRRLFNDSFdGHFL 538
Cdd:pfam04108  318 ERRREWAEKMKKILRKLAEELDRLQEEERKRREKFLKEV-GDFL 360
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
755-945 6.30e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  755 REQLIHEHKTELESLRCRFKLMTSMErsPSDSSLEKLERPTSSASVASLDVEQLLAQQRQELLAQRERaISEAVEAERAL 834
Cdd:PRK03918  264 LEERIEELKKEIEELEEKVKELKELK--EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  835 WQSRQQLPPLNSEsvmanvsilKDVLEDKERQLDLLREqnqlLTQESYQLKTRLEMLTNEDgnswLKEKIDYLSRDKCRL 914
Cdd:PRK03918  341 EELKKKLKELEKR---------LEELEERHELYEEAKA----KKEELERLKKRLTGLTPEK----LEKELEELEKAKEEI 403
                         170       180       190
                  ....*....|....*....|....*....|.
gi 968104248  915 EEELSQEKSKRLEMESSVAAMRSSTYELGAA 945
Cdd:PRK03918  404 EEEISKITARIGELKKEIKELKKAIEELKKA 434
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
662-923 8.08e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 8.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   662 GSVQRLRDALQDMSKLaLQCLAMARSNLSSLRNELTRGYQD------ELQSQMQLLQEKWQLLRmqceqREQQQAEQLEQ 735
Cdd:TIGR02169  674 AELQRLRERLEGLKRE-LSSLQSELRRIENRLDELSQELSDasrkigEIEKEIEQLEQEEEKLK-----ERLEELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   736 LRQQLLAADQDKMTAVA---QAREQLIHEHKTELESLrcrfKLMTSMERSP-SDSSLEKLERPTS--SASVASLDV---- 805
Cdd:TIGR02169  748 SLEQEIENVKSELKELEariEELEEDLHKLEEALNDL----EARLSHSRIPeIQAELSKLEEEVSriEARLREIEQklnr 823
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   806 ----EQLLAQQRQELLAQRERAISEAVEAERALWQSRQQLPPLNSE--SVMANVSILKDVLEDKERQLDLLREQNQLLTQ 879
Cdd:TIGR02169  824 ltleKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleELEAALRDLESRLGDLKKERDELEAQLRELER 903
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 968104248   880 ESYQLKTRLEMLtnEDGNSWLKEKIDYLSRDKCRLEEELSQEKS 923
Cdd:TIGR02169  904 KIEELEAQIEKK--RKRLSELKAKLEALEEELSEIEDPKGEDEE 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
686-934 7.49e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  686 RSNLSSLRN--ELTRGYQdELQSQMQLLQEKWQLLRMQCEQREQQQAEQLEQLRQQLLAADQDKMTAVAQAREQLihehK 763
Cdd:COG1196   199 ERQLEPLERqaEKAERYR-ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL----R 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  764 TELESLRCRFKLMTSMERSpSDSSLEKLERPTSSASVASLDVEQLLAQQRQELLAQRERAISEAVEAERALwQSRQQLPP 843
Cdd:COG1196   274 LELEELELELEEAQAEEYE-LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE-EELEEAEE 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  844 LNSESVMANVSILKDVLEDKERQLDLLREQNQLLTQESYQLKTRLEMLTNEDGnswLKEKIDYLSRDKCRLEEELSQEKS 923
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE---LEEAEEALLERLERLEEELEELEE 428
                         250
                  ....*....|.
gi 968104248  924 KRLEMESSVAA 934
Cdd:COG1196   429 ALAELEEEEEE 439
 
Name Accession Description Interval E-value
Ubl_RB1CC1 cd17060
ubiquitin-like (Ubl) domain found in retinoblastoma 1-inducible coiled-coil protein 1 (RB1CC1) ...
2-74 1.29e-34

ubiquitin-like (Ubl) domain found in retinoblastoma 1-inducible coiled-coil protein 1 (RB1CC1) and similar proteins; RB1CC1, also termed FAK family kinase-interacting protein of 200 kDa (FIP200), is the mammalian counterpart of the yeast Atg17 gene and functions as a component of the ULK1/Atg13/RB1CC1/Atg101 complex essential for induction of autophagy. RB1CC1 is a key signaling node to regulate cellular proliferation and differentiation. As a DNA-binding transcription factor, RB1CC1 has been implicated in the regulation of retinoblastoma 1 (RB1) expression. RB1CC1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, as well as a nuclear localization signal (KPRK), a leucine zipper motif and a coiled-coil structure.


Pssm-ID: 340580  Cd Length: 75  Bit Score: 126.91  E-value: 1.29e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 968104248    2 MLYVFHVDVGRMLSFDMTVALSSVENLKETIQRLHGLPAANIVLLVSGGEMLTHSTQVSCYSAGTDTNPIFMF 74
Cdd:cd17060     1 MLYVFLVNTGTMLTFDMSLAVQSVSDLKEAIEEKTKIPVEKQVLLVSGGESLDPDKRVSSYSAGTDTNPIFLF 73
ATG11 pfam10377
Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, ...
929-1085 5.05e-22

Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, Schizosaccharomyces pombe, this protein has been shown to interact with the telomere cap complex and it is also required for dimerization and kinase activation of Atg1. However, in budding yeast, Saccharomyces cerevisiae, this protein is called ATG11 and is shown to be involved in autophagy.


Pssm-ID: 463063  Cd Length: 130  Bit Score: 93.05  E-value: 5.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   929 ESSVAAMRSSTYELgaagmSGTLTRSKSSGGGGGGGGSSSSsHRHITLEGCSKGDLVFVIWSMRHGQ-----FMVVQDSL 1003
Cdd:pfam10377    1 ESAVIKRFKDVETL-----AKKLTKENKSKREKLEKLQSEA-HEKITLKNFKVGDLALFLPTRRHNDlstppWAAFNVGA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  1004 TLYFVHADSLPALQLTAptttassslppgaegplavaelnhiplpyYAIGRIIDKEYCQAR---KDENRYRVSKGSKFYR 1080
Cdd:pfam10377   75 PHYFLKADSLLALKSRE-----------------------------WFVGRITSIEERVVDlsdKDSNPFKLSKGTVWYL 125

                   ....*
gi 968104248  1081 IKLAP 1085
Cdd:pfam10377  126 VTAEE 130
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
122-538 1.41e-16

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 83.21  E-value: 1.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   122 LETVRQRATLAQRLRELGRKEELLCERLVHEQHLQQQGWSAVVANMEDLTSEFSERFHNFcLAFDRHLEQResYLELLRN 201
Cdd:pfam04108    2 LSSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNEL-KKDFKQLLKD--LDAALER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   202 FGDDLKQLARIPILPALmalaQADFHGFDELLgnDNVDEDVGQlqpetetevgesgesveksssstspnkklKMGHEQEE 281
Cdd:pfam04108   79 LEETLDKLRNTPVEPAL----PPGEEKQKTLL--DFIDEDSVE-----------------------------ILRDALKE 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   282 QEETSNSRqqqqqhqlnllqwisskgnhaalqqmcdecVQGLDTfSLEIYEKLKLEVQNIIKSAKQSD--VKEIKGLSDR 359
Cdd:pfam04108  124 LIDELQAA------------------------------QESLDS-DLKRFDDDLRDLQKELESLSSPSesISLIPTLLKE 172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   360 LYRL-DEFKYEIRKIVQVQREQATAFQQNESRAVNLRD---------NSVLPDLCLSHRSqlmvMRDNHIKIREYSRCIA 429
Cdd:pfam04108  173 LESLeEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEvlendarelDDVVPELQDRLDE----MENNYERLQKLLEQKN 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   430 NSKEELGRNLNTrlrrivwiengMSEFDNRLLFYLRCLRRAERHIS--------IIEQIHRA-------PSTYVAAVTEV 494
Cdd:pfam04108  249 SLIDELLSALQL-----------IAEIQSRLPEYLAALKEFEERWEeeketiedYLSELEDLrefyegfPSAYGSLLLEV 317
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 968104248   495 VRRKIFSDEFRLWASRLSVDFDRIHSEEMERRRLFNDSFdGHFL 538
Cdd:pfam04108  318 ERRREWAEKMKKILRKLAEELDRLQEEERKRREKFLKEV-GDFL 360
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
755-945 6.30e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  755 REQLIHEHKTELESLRCRFKLMTSMErsPSDSSLEKLERPTSSASVASLDVEQLLAQQRQELLAQRERaISEAVEAERAL 834
Cdd:PRK03918  264 LEERIEELKKEIEELEEKVKELKELK--EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  835 WQSRQQLPPLNSEsvmanvsilKDVLEDKERQLDLLREqnqlLTQESYQLKTRLEMLTNEDgnswLKEKIDYLSRDKCRL 914
Cdd:PRK03918  341 EELKKKLKELEKR---------LEELEERHELYEEAKA----KKEELERLKKRLTGLTPEK----LEKELEELEKAKEEI 403
                         170       180       190
                  ....*....|....*....|....*....|.
gi 968104248  915 EEELSQEKSKRLEMESSVAAMRSSTYELGAA 945
Cdd:PRK03918  404 EEEISKITARIGELKKEIKELKKAIEELKKA 434
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
662-923 8.08e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 8.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   662 GSVQRLRDALQDMSKLaLQCLAMARSNLSSLRNELTRGYQD------ELQSQMQLLQEKWQLLRmqceqREQQQAEQLEQ 735
Cdd:TIGR02169  674 AELQRLRERLEGLKRE-LSSLQSELRRIENRLDELSQELSDasrkigEIEKEIEQLEQEEEKLK-----ERLEELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   736 LRQQLLAADQDKMTAVA---QAREQLIHEHKTELESLrcrfKLMTSMERSP-SDSSLEKLERPTS--SASVASLDV---- 805
Cdd:TIGR02169  748 SLEQEIENVKSELKELEariEELEEDLHKLEEALNDL----EARLSHSRIPeIQAELSKLEEEVSriEARLREIEQklnr 823
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   806 ----EQLLAQQRQELLAQRERAISEAVEAERALWQSRQQLPPLNSE--SVMANVSILKDVLEDKERQLDLLREQNQLLTQ 879
Cdd:TIGR02169  824 ltleKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleELEAALRDLESRLGDLKKERDELEAQLRELER 903
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 968104248   880 ESYQLKTRLEMLtnEDGNSWLKEKIDYLSRDKCRLEEELSQEKS 923
Cdd:TIGR02169  904 KIEELEAQIEKK--RKRLSELKAKLEALEEELSEIEDPKGEDEE 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
686-936 1.34e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   686 RSNLSSLRNELTRGYQDELQSQMQLLQEKWQLLRMQCEQREQQQAEQLEQLRQQLLAADQDKMTAVAQAREQLIHEHKTE 765
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   766 LESLRcrfklmtsMERSPSDSSLEKLERPTSSASVASLDVEQLLAQQRQELLAQRERaISEAVEAERALWQSRQQLpPLN 845
Cdd:TIGR02168  756 LTELE--------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-LDELRAELTLLNEEAANL-RER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   846 SESVMANVSILKDVLEDKERQLDLLREQNQLLTQESYQLKTRLEMLTnEDGNSWLKEKiDYLSRDKCRLEEELSQEKSKR 925
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE-SELEALLNER-ASLEEALALLRSELEELSEEL 903
                          250
                   ....*....|.
gi 968104248   926 LEMESSVAAMR 936
Cdd:TIGR02168  904 RELESKRSELR 914
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
807-930 1.52e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248   807 QLLAQQRQELLAQRERA---ISEAVEAERA-------LWQSRQQLPPlNSESVMANVSILKDVLEDKERQLDLLREQNQL 876
Cdd:TIGR04523  422 ELLEKEIERLKETIIKNnseIKDLTNQDSVkeliiknLDNTRESLET-QLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 968104248   877 LTQESYQLKTRLEMLTNEdgNSWLKEKIDYLSRDKCRLEEELSQEKSKRLEMES 930
Cdd:TIGR04523  501 LNEEKKELEEKVKDLTKK--ISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
Ubl_IKKA_like cd17046
ubiquitin-like (Ubl) domain found in inhibitor of nuclear factor kappa-B kinases, IKK-alpha ...
2-75 2.79e-03

ubiquitin-like (Ubl) domain found in inhibitor of nuclear factor kappa-B kinases, IKK-alpha and IKK-beta, and similar proteins; IKK, also termed IkappaB kinase, is an enzyme complex involved in propagating the cellular response to inflammation. It is part of the upstream nuclear factor kappa-B kinase (NF-kappaB) signal transduction cascade, and plays an important role in regulating the NF-kappaB transcription factor. IKK is composed of three subunits, IKK-alpha/CHUK, IKK-beta/IKBKB, and IKK-gamma/NEMO. The IKK-alpha and IKK-beta subunits together are catalytically active whereas the IKK-gamma subunit serves a regulatory function. IKK-alpha and IKK-beta phosphorylate the IkappaB proteins, marking them for degradation via ubiquitination and allowing NF-kappaB transcription factors to go into the nucleus. IKK-alpha, also known as IKK-A, or IkappaB kinase A (IkBKA), or conserved helix-loop-helix ubiquitous kinase (CHUK), or I-kappa-B kinase 1 (IKK1), or nuclear factor NF-kappa-B inhibitor kinase alpha (NFKBIKA), or transcription factor 16 (TCF-16), belongs to the serine/threonine protein kinase family. In addition to NF-kappaB response, it has many additional cellular targets in an NF-kappaB-independent manner. For instance, it plays a role in epidermal differentiation, as well as in the regulation of the cell cycle protein cyclin D1. IKK-beta, also known as IKK-B, or IkappaB kinase B (IkBKB), or I-kappa-B kinase 2 (IKK2), or nuclear factor NF-kappa-B inhibitor kinase beta (NFKBIKB), belongs to the serine/threonine protein kinase family as well. It interacts with many different protein partners and has been implicated in the treatment of many inflammatory diseases and cancers. Both IKK-alpha and IKK-beta contain an N-terminal catalytic domain followed by a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340566  Cd Length: 75  Bit Score: 38.01  E-value: 2.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 968104248    2 MLYVFHVDVGRMLSFDMTVALsSVENLKETIQRLHGLPAANIVLLVSGGEMLTHSTQVSCYSAGTDTNPIFMFL 75
Cdd:cd17046     2 IVHIFNVTTYRILSYEVTEDT-SLSTLQSWIERDTGIPVEDQELLLPTGVSLDPEKPASQCWLVRGEDDYLVFL 74
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
686-934 7.49e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  686 RSNLSSLRN--ELTRGYQdELQSQMQLLQEKWQLLRMQCEQREQQQAEQLEQLRQQLLAADQDKMTAVAQAREQLihehK 763
Cdd:COG1196   199 ERQLEPLERqaEKAERYR-ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL----R 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  764 TELESLRCRFKLMTSMERSpSDSSLEKLERPTSSASVASLDVEQLLAQQRQELLAQRERAISEAVEAERALwQSRQQLPP 843
Cdd:COG1196   274 LELEELELELEEAQAEEYE-LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE-EELEEAEE 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968104248  844 LNSESVMANVSILKDVLEDKERQLDLLREQNQLLTQESYQLKTRLEMLTNEDGnswLKEKIDYLSRDKCRLEEELSQEKS 923
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE---LEEAEEALLERLERLEEELEELEE 428
                         250
                  ....*....|.
gi 968104248  924 KRLEMESSVAA 934
Cdd:COG1196   429 ALAELEEEEEE 439
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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