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Conserved domains on  [gi|242072598|ref|XP_002446235|]
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protein MICRORCHIDIA 7 isoform X1 [Sorghum bicolor]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Morc6_S5 pfam17942
Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. ...
 384-527 2.69e-91

Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. Arabidopsis microrchidia (MORC) ATPase family proteins are conserved among plants and animals and are involved in transcriptional silencing. In Arabidopsis, MORC6/DMS11 was reported to function in the condensation of pericentromeric heterochromatin, thereby facilitating transcriptional silencing. Further studies demonstrate that MORC6 and its homologs MORC1 and MORC2 form a complex which associates with SUVH9, required for Pol V occupancy in the RdDM (RNA-directed DNA methylation) pathway.


:

Pssm-ID: 465579  Cd Length: 139  Bit Score: 282.51  E-value: 2.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  384 HSLRSYASILYLRLPTYFQMILRGKDIEHHNIVTDMMLKKEVTYRPVAPNGhpkdSNMVADVTIGFVKDAKHhIDVQGFN 463
Cdd:pfam17942   1 YSLRAYASILYLRLPPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGGG----KEVVVITTIGFLKEAPH-INVHGFN 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242072598  464 VYHKNRLIKPFWRVWTAAGSGGRGVIGVLEANFIEPAHDKQDFERTTLLARLEARLVQMQKDYW 527
Cdd:pfam17942  76 VYHKNRLIKPFWRVGNQAGSKGRGVIGVLEANFIEPTHDKQDFERTSLYQRLEARLKQMLKEYW 139
HATPase super family cl00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
 138-266 5.37e-41

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


The actual alignment was detected with superfamily member cd16931:

Pssm-ID: 469604 [Multi-domain]  Cd Length: 118  Bit Score: 146.01  E-value: 5.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 138 FLHSNATSHKWALGALAELLDNSLDEVINGATYVNIDVLENDKGIdkeksrMLLVEDDGGGMDPDKMRQCMSLGYSVKSK 217
Cdd:cd16931    1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLRGGF------MLSFLDDGNGMTPEEAHHMISFGFSDKRS 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 242072598 218 VAST-IGQYGNGFKTSTMRLGADVLVFSRSRGksgkrpTQSIGMLSYTFL 266
Cdd:cd16931   75 DDHDhIGRYGNGFKSGSMRLGRDVIVFTKKDE------SQSCGLLSQTFL 118
DR0291 super family cl34310
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 654-791 1.11e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


The actual alignment was detected with superfamily member COG1579:

Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.31  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 654 QSSGLIERDRGRTKSqpldpkATSNRdlhtidEYESVIKQLRdenlSLKERLSKVEESLLQelvverdknksLTERVEDL 733
Cdd:COG1579   70 EVEARIKKYEEQLGN------VRNNK------EYEALQKEIE----SLKRRISDLEDEILE-----------LMERIEEL 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242072598 734 QRQFESATKEQEALIDIFSEERNRRD-------QEEESLRKKLKDASSTI-QDLLEQLNAARKGRK 791
Cdd:COG1579  123 EEELAELEAELAELEAELEEKKAELDeelaeleAELEELEAEREELAAKIpPELLALYERIRKRKN 188
 
Name Accession Description Interval E-value
Morc6_S5 pfam17942
Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. ...
 384-527 2.69e-91

Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. Arabidopsis microrchidia (MORC) ATPase family proteins are conserved among plants and animals and are involved in transcriptional silencing. In Arabidopsis, MORC6/DMS11 was reported to function in the condensation of pericentromeric heterochromatin, thereby facilitating transcriptional silencing. Further studies demonstrate that MORC6 and its homologs MORC1 and MORC2 form a complex which associates with SUVH9, required for Pol V occupancy in the RdDM (RNA-directed DNA methylation) pathway.


Pssm-ID: 465579  Cd Length: 139  Bit Score: 282.51  E-value: 2.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  384 HSLRSYASILYLRLPTYFQMILRGKDIEHHNIVTDMMLKKEVTYRPVAPNGhpkdSNMVADVTIGFVKDAKHhIDVQGFN 463
Cdd:pfam17942   1 YSLRAYASILYLRLPPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGGG----KEVVVITTIGFLKEAPH-INVHGFN 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242072598  464 VYHKNRLIKPFWRVWTAAGSGGRGVIGVLEANFIEPAHDKQDFERTTLLARLEARLVQMQKDYW 527
Cdd:pfam17942  76 VYHKNRLIKPFWRVGNQAGSKGRGVIGVLEANFIEPTHDKQDFERTSLYQRLEARLKQMLKEYW 139
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 138-266 5.37e-41

Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. In addition to the HATPase domain, MORC family proteins have a CW-type zinc finger domain containing four conserved cysteines and two conserved tryptophans, and coiled-coil domains at the carboxy-terminus. MORC1 has cross-species differential methylation in association with early life stress, and genome-wide association with major depressive disorder (MDD). MORC2 is involved in several nuclear processes, including transcription modulation and DNA damage repair, and exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY. MORC3 regulates p53, and is an antiviral factor which plays an important role during HSV-1 and HCMV infection, and is a positive regulator of influenza virus transcription. MORC4 is highly expressed in a subset of diffuse large B-cell lymphomas and has potential as a lymphoma biomarker.


Pssm-ID: 340408 [Multi-domain]  Cd Length: 118  Bit Score: 146.01  E-value: 5.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 138 FLHSNATSHKWALGALAELLDNSLDEVINGATYVNIDVLENDKGIdkeksrMLLVEDDGGGMDPDKMRQCMSLGYSVKSK 217
Cdd:cd16931    1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLRGGF------MLSFLDDGNGMTPEEAHHMISFGFSDKRS 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 242072598 218 VAST-IGQYGNGFKTSTMRLGADVLVFSRSRGksgkrpTQSIGMLSYTFL 266
Cdd:cd16931   75 DDHDhIGRYGNGFKSGSMRLGRDVIVFTKKDE------SQSCGLLSQTFL 118
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 151-275 9.17e-19

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 83.15  E-value: 9.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  151 GALAELLDNSLDEvinGATYVNIDVLENDKGIDkeksrMLLVEDDGGGMDPDKMRQCMSLGYSVKSKVAS--TIGQYGNG 228
Cdd:pfam13589   3 GALAELIDNSIDA---DATNIKIEVNKNRGGGT-----EIVIEDDGHGMSPEELINALRLATSAKEAKRGstDLGRYGIG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 242072598  229 FKTSTMRLGADVLVFSRSRGKSGKRptqsigMLSYTFLRSTGKEDII 275
Cdd:pfam13589  75 LKLASLSLGAKLTVTSKKEGKSSTL------TLDRDKISNENDWLLP 115
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 654-791 1.11e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.31  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 654 QSSGLIERDRGRTKSqpldpkATSNRdlhtidEYESVIKQLRdenlSLKERLSKVEESLLQelvverdknksLTERVEDL 733
Cdd:COG1579   70 EVEARIKKYEEQLGN------VRNNK------EYEALQKEIE----SLKRRISDLEDEILE-----------LMERIEEL 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242072598 734 QRQFESATKEQEALIDIFSEERNRRD-------QEEESLRKKLKDASSTI-QDLLEQLNAARKGRK 791
Cdd:COG1579  123 EEELAELEAELAELEAELEEKKAELDeelaeleAELEELEAEREELAAKIpPELLALYERIRKRKN 188
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 661-782 3.21e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 50.59  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  661 RDRGRTKSQPLDPKATSNRDLHtiDEYESVIKQLRD--ENLSLKER----LSKVEESLLQELvveRDKNKSLT---ERVE 731
Cdd:pfam10174 351 RLRLEEKESFLNKKTKQLQDLT--EEKSTLAGEIRDlkDMLDVKERkinvLQKKIENLQEQL---RDKDKQLAglkERVK 425

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242072598  732 DLQRQ----------FESATKEQEALIDIFSEERNRRDQ----EEESLRKKLKDAS---STIQ-DLLEQ 782
Cdd:pfam10174 426 SLQTDssntdtalttLEEALSEKERIIERLKEQREREDRerleELESLKKENKDLKekvSALQpELTEK 494
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
683-791 9.05e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 9.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 683 TIDEYESVIKQLR---DENLSLKERLSKVEEsLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEERNRRD 759
Cdd:PRK03918 586 SVEELEERLKELEpfyNEYLELKDAEKELER-EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL 664

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 242072598 760 QEE---------------ESLRKKLKDASSTIQDLLEQLNAARKGRK 791
Cdd:PRK03918 665 REEylelsrelaglraelEELEKRREEIKKTLEKLKEELEEREKAKK 711
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 678-791 2.60e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.85  E-value: 2.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598   678 NRDLHTIDEYESVIKqlrdenlSLKERLSKVEESLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEERNR 757
Cdd:smart00787 157 KEDYKLLMKELELLN-------SIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEE 229

                           90       100       110
                   ....*....|....*....|....*....|....
gi 242072598   758 RDQEEESLRKKLKDASSTIQDLLEQLNAARKGRK 791
Cdd:smart00787 230 LEEELQELESKIEDLTNKKSELNTEIAEAEKKLE 263
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 678-788 3.14e-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: 44.29  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598   678 NRDLHTIDEYESVIKQLRDENLSLKERLSKVEESL------LQELVVE----RDKNKSLTERVEDLQRQFESATKEQEAL 747
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedlraeLEEVDKEfaetRDELKDYREKLEKLKREINELKRELDRL 411

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 242072598   748 IDifseERNRRDQEEESLRKKLKDASSTIQDLLEQLNAARK 788
Cdd:TIGR02169  412 QE----ELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
 
Name Accession Description Interval E-value
Morc6_S5 pfam17942
Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. ...
 384-527 2.69e-91

Morc6 ribosomal protein S5 domain 2-like; This domain is found in MORC6 proteins in eukaryotes. Arabidopsis microrchidia (MORC) ATPase family proteins are conserved among plants and animals and are involved in transcriptional silencing. In Arabidopsis, MORC6/DMS11 was reported to function in the condensation of pericentromeric heterochromatin, thereby facilitating transcriptional silencing. Further studies demonstrate that MORC6 and its homologs MORC1 and MORC2 form a complex which associates with SUVH9, required for Pol V occupancy in the RdDM (RNA-directed DNA methylation) pathway.


Pssm-ID: 465579  Cd Length: 139  Bit Score: 282.51  E-value: 2.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  384 HSLRSYASILYLRLPTYFQMILRGKDIEHHNIVTDMMLKKEVTYRPVAPNGhpkdSNMVADVTIGFVKDAKHhIDVQGFN 463
Cdd:pfam17942   1 YSLRAYASILYLRLPPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGGG----KEVVVITTIGFLKEAPH-INVHGFN 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242072598  464 VYHKNRLIKPFWRVWTAAGSGGRGVIGVLEANFIEPAHDKQDFERTTLLARLEARLVQMQKDYW 527
Cdd:pfam17942  76 VYHKNRLIKPFWRVGNQAGSKGRGVIGVLEANFIEPTHDKQDFERTSLYQRLEARLKQMLKEYW 139
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 138-266 5.37e-41

Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. In addition to the HATPase domain, MORC family proteins have a CW-type zinc finger domain containing four conserved cysteines and two conserved tryptophans, and coiled-coil domains at the carboxy-terminus. MORC1 has cross-species differential methylation in association with early life stress, and genome-wide association with major depressive disorder (MDD). MORC2 is involved in several nuclear processes, including transcription modulation and DNA damage repair, and exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY. MORC3 regulates p53, and is an antiviral factor which plays an important role during HSV-1 and HCMV infection, and is a positive regulator of influenza virus transcription. MORC4 is highly expressed in a subset of diffuse large B-cell lymphomas and has potential as a lymphoma biomarker.


Pssm-ID: 340408 [Multi-domain]  Cd Length: 118  Bit Score: 146.01  E-value: 5.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 138 FLHSNATSHKWALGALAELLDNSLDEVINGATYVNIDVLENDKGIdkeksrMLLVEDDGGGMDPDKMRQCMSLGYSVKSK 217
Cdd:cd16931    1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLRGGF------MLSFLDDGNGMTPEEAHHMISFGFSDKRS 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 242072598 218 VAST-IGQYGNGFKTSTMRLGADVLVFSRSRGksgkrpTQSIGMLSYTFL 266
Cdd:cd16931   75 DDHDhIGRYGNGFKSGSMRLGRDVIVFTKKDE------SQSCGLLSQTFL 118
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 151-275 9.17e-19

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 83.15  E-value: 9.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  151 GALAELLDNSLDEvinGATYVNIDVLENDKGIDkeksrMLLVEDDGGGMDPDKMRQCMSLGYSVKSKVAS--TIGQYGNG 228
Cdd:pfam13589   3 GALAELIDNSIDA---DATNIKIEVNKNRGGGT-----EIVIEDDGHGMSPEELINALRLATSAKEAKRGstDLGRYGIG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 242072598  229 FKTSTMRLGADVLVFSRSRGKSGKRptqsigMLSYTFLRSTGKEDII 275
Cdd:pfam13589  75 LKLASLSLGAKLTVTSKKEGKSSTL------TLDRDKISNENDWLLP 115
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 654-791 1.11e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.31  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 654 QSSGLIERDRGRTKSqpldpkATSNRdlhtidEYESVIKQLRdenlSLKERLSKVEESLLQelvverdknksLTERVEDL 733
Cdd:COG1579   70 EVEARIKKYEEQLGN------VRNNK------EYEALQKEIE----SLKRRISDLEDEILE-----------LMERIEEL 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242072598 734 QRQFESATKEQEALIDIFSEERNRRD-------QEEESLRKKLKDASSTI-QDLLEQLNAARKGRK 791
Cdd:COG1579  123 EEELAELEAELAELEAELEEKKAELDeelaeleAELEELEAEREELAAKIpPELLALYERIRKRKN 188
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 661-782 3.21e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 50.59  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  661 RDRGRTKSQPLDPKATSNRDLHtiDEYESVIKQLRD--ENLSLKER----LSKVEESLLQELvveRDKNKSLT---ERVE 731
Cdd:pfam10174 351 RLRLEEKESFLNKKTKQLQDLT--EEKSTLAGEIRDlkDMLDVKERkinvLQKKIENLQEQL---RDKDKQLAglkERVK 425

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242072598  732 DLQRQ----------FESATKEQEALIDIFSEERNRRDQ----EEESLRKKLKDAS---STIQ-DLLEQ 782
Cdd:pfam10174 426 SLQTDssntdtalttLEEALSEKERIIERLKEQREREDRerleELESLKKENKDLKekvSALQpELTEK 494
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
656-791 4.05e-06

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 50.24  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 656 SGLIERDRGRTKSQPLDPKATSNRDL----HTIDEYESVIKQLRDENLSLKERLSkveesllqelvvERDknksltERVE 731
Cdd:COG2433  383 EELIEKELPEEEPEAEREKEHEERELteeeEEIRRLEEQVERLEAEVEELEAELE------------EKD------ERIE 444

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 732 DLQRQFESATKEQEALIDIfSEERNRRDQEEESLRKKLKDASSTIQDLLEQLNAARKGRK 791
Cdd:COG2433  445 RLERELSEARSEERREIRK-DREISRLDREIERLERELEEERERIEELKRKLERLKELWK 503
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
683-791 9.05e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 9.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 683 TIDEYESVIKQLR---DENLSLKERLSKVEEsLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEERNRRD 759
Cdd:PRK03918 586 SVEELEERLKELEpfyNEYLELKDAEKELER-EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL 664

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 242072598 760 QEE---------------ESLRKKLKDASSTIQDLLEQLNAARKGRK 791
Cdd:PRK03918 665 REEylelsrelaglraelEELEKRREEIKKTLEKLKEELEEREKAKK 711
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 674-783 4.52e-05

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 43.78  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  674 KATSNRDLHTIDEYESVIKQLRDENLSLKERLSKVEE----------SLLQELVVERDKNKSLTERVEDLQRQFESATKE 743
Cdd:pfam07926   7 QSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQnyerelvlhaEDIKALQALREELNELKAEIAELKAEAESAKAE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 242072598  744 QEALIDIFSEERNRRDQEEESLRKKLKDASSTIQDLLEQL 783
Cdd:pfam07926  87 LEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQL 126
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 684-791 4.63e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 4.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 684 IDEYESVIKQLRDENLSLKERLskveESLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEERNRRDQEEE 763
Cdd:COG1196  297 LARLEQDIARLEERRRELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                         90       100
                 ....*....|....*....|....*...
gi 242072598 764 SLRKKLKDASSTIQDLLEQLNAARKGRK 791
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAA 400
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
684-785 4.72e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 4.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 684 IDEYESVIKQLRDENLSLKERLSKVEESLLQElvveRDKNKSLTERVEDLQRQFESATKEQEALidifSEERNRRDQEEE 763
Cdd:COG4372   40 LDKLQEELEQLREELEQAREELEQLEEELEQA----RSELEQLEEELEELNEQLQAAQAELAQA----QEELESLQEEAE 111

                         90       100
                 ....*....|....*....|..
gi 242072598 764 SLRKKLKDASSTIQDLLEQLNA 785
Cdd:COG4372  112 ELQEELEELQKERQDLEQQRKQ 133
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
691-787 8.92e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 8.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 691 IKQLRDENLSLKERLSKVEESLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEERNRrdQEEESLRKKLK 770
Cdd:COG4717  365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELE 442

                         90
                 ....*....|....*..
gi 242072598 771 DASSTIQDLLEQLNAAR 787
Cdd:COG4717  443 ELEEELEELREELAELE 459
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 687-788 1.62e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 687 YESVIKQLRDENLSLKERLSKVEEsLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEERNRRDQEEESLR 766
Cdd:COG4942  141 LKYLAPARREQAEELRADLAELAA-LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219

                         90       100
                 ....*....|....*....|..
gi 242072598 767 KKLKDASSTIQDLLEQLNAARK 788
Cdd:COG4942  220 QEAEELEALIARLEAEAAAAAE 241
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 678-791 2.60e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.85  E-value: 2.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598   678 NRDLHTIDEYESVIKqlrdenlSLKERLSKVEESLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEERNR 757
Cdd:smart00787 157 KEDYKLLMKELELLN-------SIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEE 229

                           90       100       110
                   ....*....|....*....|....*....|....
gi 242072598   758 RDQEEESLRKKLKDASSTIQDLLEQLNAARKGRK 791
Cdd:smart00787 230 LEEELQELESKIEDLTNKKSELNTEIAEAEKKLE 263
Mod_r pfam07200
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ...
 680-788 2.96e-04

Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region approximately 150 residues long within a number of eukaryotic proteins that show homology with Drosophila melanogaster Modifier of rudimentary (Mod(r)) proteins. The N-terminal half of Mod(r) proteins is acidic, whereas the C-terminal half is basic, and both of these regions are represented in this family. Members of this family include the Vps37 subunit of the endosomal sorting complex ESCRT-I, a complex involved in recruiting transport machinery for protein sorting at the multivesicular body (MVB). The yeast ESCRT-I complex consists of three proteins (Vps23, Vps28 and Vps37). The mammalian homolog of Vps37 interacts with Tsg101 (Pfam: PF05743) through its mod(r) domain and its function is essential for lysosomal sorting of EGF receptors.


Pssm-ID: 462117 [Multi-domain]  Cd Length: 146  Bit Score: 41.84  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  680 DLHTIDEYESVIKQLRDENLSLKERLskveESLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEE--RNR 757
Cdd:pfam07200  24 SLPQVKALQAEKEELLAENESLAEEN----LSLEPELEELRSQLQELLEELKALKSEYEEKEQELDELLSKFSPDalLAR 99

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 242072598  758 -----RDQEEES--LRKKLKDASSTIQDLLEQLNAARK 788
Cdd:pfam07200 100 lqaaaAEAEEESeaLAESFLEGEIDLDEFLKQFKEKRK 137
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 678-788 3.14e-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: 44.29  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598   678 NRDLHTIDEYESVIKQLRDENLSLKERLSKVEESL------LQELVVE----RDKNKSLTERVEDLQRQFESATKEQEAL 747
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedlraeLEEVDKEfaetRDELKDYREKLEKLKREINELKRELDRL 411

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 242072598   748 IDifseERNRRDQEEESLRKKLKDASSTIQDLLEQLNAARK 788
Cdd:TIGR02169  412 QE----ELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 686-791 6.68e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 6.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598   686 EYESVIKQLrDENLSLKERLSKVEESLLQEL---VVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEERNR----- 757
Cdd:pfam01576  553 ELEALTQQL-EEKAAAYDKLEKTKNRLQQELddlLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRaeaea 631

                           90       100       110
                   ....*....|....*....|....*....|....
gi 242072598   758 RDQEEESLrkKLKDASSTIQDLLEQLNAARKGRK 791
Cdd:pfam01576  632 REKETRAL--SLARALEEALEAKEELERTNKQLR 663
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 665-788 1.65e-03

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: 41.98  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598   665 RTKSQPLDPKATSNRDlhTIDEYESVIKQLRDENLSLKERLSKVEESLLQELVVERDKNKsltERVEDLQRQFESATKEQ 744
Cdd:TIGR02169  743 EEDLSSLEQEIENVKS--ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREI 817

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 242072598   745 EAlidifseERNRRDQEEESLRKKLKDASSTIQDLLEQLNAARK 788
Cdd:TIGR02169  818 EQ-------KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
678-788 2.03e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 678 NRDLHTIDEYESVIKQLRDENLSLKERLSKVEE-----SLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFS 752
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKLEKllqllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 242072598 753 EERNRRDQEEESLRKKLKDASSTIQDLLEQLNAARK 788
Cdd:COG4717  171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 684-788 2.44e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 684 IDEYESVIKQLRDENLSLKERLSKVEEsllqELVVERDKNKSLTERVEDLQRQFESATKEQEALI-DI---------FSE 753
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEA----ELEELRLELEELELELEEAQAEEYELLAELARLEqDIarleerrreLEE 316

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 242072598 754 ERNRRDQEEESLRKKLKDASSTIQDLLEQLNAARK 788
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEE 351
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 685-776 2.60e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598   685 DEYESVIKQLRDENLSLKERLSKVEESLlQELVVERDKNKSL--TERVEDLQRQFESATKEQEALIDIFSEERNRRDQEE 762
Cdd:smart00935  14 PAGKAAQKQLEKEFKKRQAELEKLEKEL-QKLKEKLQKDAATlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEE 92

                           90
                   ....*....|....*
gi 242072598   763 -ESLRKKLKDASSTI 776
Cdd:smart00935  93 lQKILDKINKAIKEV 107
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
683-791 2.70e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.66  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 683 TIDEYESVIKQLRDENLSLKERLSKVEEsLLQELVVERDKnksLTERVEDLQRQFESATKEQEALIDIFSEERNRRDQee 762
Cdd:COG1340    9 SLEELEEKIEELREEIEELKEKRDELNE-ELKELAEKRDE---LNAQVKELREEAQELREKRDELNEKVKELKEERDE-- 82

                         90       100
                 ....*....|....*....|....*....
gi 242072598 763 esLRKKLKDASSTIQDLLEQLNAARKGRK 791
Cdd:COG1340   83 --LNEKLNELREELDELRKELAELNKAGG 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 152-248 3.50e-03

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 37.73  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  152 ALAELLDNSLDEViNGATYVNIDVLENDKGIdkeksrmLLVEDDGGGMDPDKMRQCMSLGYSvkskvASTIGQYGNGF-- 229
Cdd:pfam02518   9 VLSNLLDNALKHA-AKAGEITVTLSEGGELT-------LTVEDNGIGIPPEDLPRIFEPFST-----ADKRGGGGTGLgl 75

                          90       100
                  ....*....|....*....|..
gi 242072598  230 ---KTSTMRLGADVLVFSRSRG 248
Cdd:pfam02518  76 sivRKLVELLGGTITVESEPGG 97
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
681-789 5.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 5.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 681 LHTIDEYESVIKQLRDE--NLS-----LKERLSKVEESLLQELVVERDKnKSLTERVEDLQRQFESATKEQEALIDIFSE 753
Cdd:PRK03918 206 LREINEISSELPELREEleKLEkevkeLEELKEEIEELEKELESLEGSK-RKLEEKIRELEERIEELKKEIEELEEKVKE 284

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 242072598 754 ERNRRDQEEE-----SLRKKLKDASSTIQDLLEQLNAARKG 789
Cdd:PRK03918 285 LKELKEKAEEyiklsEFYEEYLDELREIEKRLSRLEEEING 325
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 680-788 5.39e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 680 DLHTIDeyeSVIKQLRDENLSLKERLSKVEESLlqelvverdknKSLTERVEDLQRQFESATKEQEAL-IDIFS-EERNR 757
Cdd:COG1579   11 DLQELD---SELDRLEHRLKELPAELAELEDEL-----------AALEARLEAAKTELEDLEKEIKRLeLEIEEvEARIK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 242072598 758 RDQ-----------------EEESLRKKLKDASSTIQDLLEQLNAARK 788
Cdd:COG1579   77 KYEeqlgnvrnnkeyealqkEIESLKRRISDLEDEILELMERIEELEE 124
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 543-787 5.76e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 40.43  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  543 RNSDAGDGEDSRENTASAQPSPYHSGKGYTQAKDMnnnIKKGGKASTSFGiqqraEKSARTKRSMKSILHGLSDSDNSDS 622
Cdd:pfam05911 631 KKHDCIDKVTLSENKVAQVDNGCSEIDNLSSDPEI---PSDGPLVSGSND-----LKTEENKRLKEEFEQLKSEKENLEV 702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  623 EFMGTLPRSRShTVNRNQKLFQNGS---TDLTTPQ-SSGLIErdrgrtkSQpLDPKATSNRDLHTideyesvikQLRDEN 698
Cdd:pfam05911 703 ELASCTENLES-TKSQLQESEQLIAelrSELASLKeSNSLAE-------TQ-LKCMAESYEDLET---------RLTELE 764

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  699 LSLKERLSKVEeSLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEERN-RRDQEEESLRKKLKDASSTIQ 777
Cdd:pfam05911 765 AELNELRQKFE-ALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDADQEDKKlQQEKEITAASEKLAECQETIL 843

                         250
                  ....*....|
gi 242072598  778 DLLEQLNAAR 787
Cdd:pfam05911 844 NLGKQLKALA 853
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
681-787 6.01e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 6.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 681 LHTIDEYESVIKQLRDENLSLKERLSKVEESLLQEL----VVERDKNKSLTERVEDLQRQFESATKEQEALidifSEERN 756
Cdd:COG4717  148 LEELEERLEELRELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEA----QEELE 223

                         90       100       110
                 ....*....|....*....|....*....|.
gi 242072598 757 RRDQEEESLRKKLkdassTIQDLLEQLNAAR 787
Cdd:COG4717  224 ELEEELEQLENEL-----EAAALEERLKEAR 249
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 685-772 6.41e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 37.67  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598  685 DEYESVIKQLRDENLS--------------LKERLSKVEESL--LQELVVERDK----NKSLTERVEDLQRQFESA---- 740
Cdd:pfam12718  17 EELEEKVKELEQENLEkeqeikslthknqqLEEEVEKLEEQLkeAKEKAEESEKlktnNENLTRKIQLLEEELEESdkrl 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 242072598  741 --TKEQEALIDIFSE--ER------NRRDQEE---ESLRKKLKDA 772
Cdd:pfam12718  97 keTTEKLRETDVKAEhlERkvqaleQERDEWEkkyEELEEKYKEA 141
PRK12704 PRK12704
phosphodiesterase; Provisional
 686-792 7.13e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 7.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 686 EYESVIKQLRDENLSLKERLSKVEESLLQELVVERDKNKSLTERVEDLQRQFESATKEQEALIDIFSEERNRRD------ 759
Cdd:PRK12704  72 EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELErisglt 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 242072598 760 QEE------ESLRKKLK-DASSTIQDLLEQ--LNAARKGRKV 792
Cdd:PRK12704 152 AEEakeillEKVEEEARhEAAVLIKEIEEEakEEADKKAKEI 193
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 155-207 8.19e-03

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 38.19  E-value: 8.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242072598 155 ELLDNSLDEvinGATYVNIDVLENdkGIDkeksrMLLVEDDGGGMDPDKMRQC 207
Cdd:cd16926   20 ELVENSIDA---GATRIDVEIEEG--GLK-----LIRVTDNGSGISREDLELA 62
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 684-788 8.28e-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: 39.65  E-value: 8.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598   684 IDEYESVIKQLRDENLSLKERLSKVEESL--LQELV--VERDKnKSLTERVEDLQRQFESAT-----------------K 742
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELyaLANEIsrLEQQK-QILRERLANLERQLEELEaqleeleskldelaeelA 340

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 242072598   743 EQEALIDIFSEERNRRDQEEESLRKKLKDASSTIQDLLEQLNAARK 788
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
693-786 8.61e-03

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 37.18  E-value: 8.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242072598 693 QLRDENLSLKErLSKVEES-----LLQELVVERDKN---KSLTERVEDLQRQFESATKeqealidifseernrrdqEEES 764
Cdd:COG1382   36 ELKEAEKALEE-LEKLPDDaevykSVGNLLVKTDKEeviKELEEKKETLELRLKTLEK------------------QEER 96

                         90       100
                 ....*....|....*....|..
gi 242072598 765 LRKKLKDASSTIQDLLEQLNAA 786
Cdd:COG1382   97 LQKQLEELQEKLQEALSGAGGG 118
 
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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