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Conserved domains on  [gi|28872812|ref|NP_056173|]
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MORC family CW-type zinc finger protein 3 isoform 1 [Homo sapiens]

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. ...
 249-382 3.26e-70

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: 228.97  E-value: 3.26e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812   249 YSLRAYCSILYLK--PRMQIILRGQKVKTQLVSKSLAYIERDVYRPKFL---SKTVRITFGF--NCRNKDHYGIMMYHRN 321
Cdd:pfam17942   1 YSLRAYASILYLRlpPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGggkEVVVITTIGFlkEAPHINVHGFNVYHKN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28872812   322 RLIKAYEKVGCQlrANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTITALGEKLNDYW 382
Cdd:pfam17942  81 RLIKPFWRVGNQ--AGSKGRGVIGVLEANFIEPTHDKQDFERTSLYQRLEARLKQMLKEYW 139
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 18-135 1.23e-65

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: 215.35  E-value: 1.23e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812  18 FLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVIN-DHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNgHVP 96
Cdd:cd16931   1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLrGGFMLSFLDDGNGMTPEEAHHMISFGFSDKRSDD-HDH 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 28872812  97 VGLYGNGFKSGSMRLGKDAIVFTKNGESMSVGLLSQTYL 135
Cdd:cd16931  80 IGRYGNGFKSGSMRLGRDVIVFTKKDESQSCGLLSQTFL 118
zf-CW pfam07496
CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four ...
 409-446 2.74e-18

CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four conserved cysteine residues and a conserved tryptophan. It was first identified by, and is predicted to be a "highly specialized mononuclear four-cysteine zinc finger...that plays a role in DNA binding and/or promoting protein-protein interactions in complicated eukaryotic processes including...chromatin methylation status and early embryonic development." Weak homology to pfam00628 further evidences these predictions (personal obs: C Yeats). Twelve different CW-domain-containing protein subfamilies are described, with different subfamilies being characteriztic of vertebrates, higher plants and other animals in which these domain is found.


:

Pssm-ID: 462181  Cd Length: 46  Bit Score: 78.89  E-value: 2.74e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 28872812   409 TWVQCDACLKWRKLPDGMD--QLPEKWYCSNNPDPQFRNC 446
Cdd:pfam07496   1 YWVQCDSCLKWRRLPTEIDpyELPEPWYCSMNPDPKYNSC 40
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
673-866 1.05e-06

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 673 EAEAKIHETQETTDksaddagcQLQELRNQLLLVTEEKENYKRQchmftdqIKVLQQRILEMNDKYVKKETCHQSTETDA 752
Cdd:COG4717  75 ELEEELKEAEEKEE--------EYAELQEELEELEEELEELEAE-------LEELREELEKLEKLLQLLPLYQELEALEA 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 753 VflLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHVKAECSQCSNNESKSEMDEMAVQLDDVFRQldkcsieRDQ 832
Cdd:COG4717 140 E--LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------LAE 210

                       170       180       190
                ....*....|....*....|....*....|....
gi 28872812 833 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQ 866
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEER 244
ClpA super family cl33938
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 808-936 3.97e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0542:

Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 3.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 808 EMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEK-SQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEESVNHMD 886
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 28872812 887 GESLKLRSLRVNVGQLLAMIVPdldlqQVNYDVDvVDEIlGQVVEQMSEI 936
Cdd:COG0542 485 GKIPELEKELAELEEELAELAP-----LLREEVT-EEDI-AEVVSRWTGI 527
 
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. ...
 249-382 3.26e-70

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: 228.97  E-value: 3.26e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812   249 YSLRAYCSILYLK--PRMQIILRGQKVKTQLVSKSLAYIERDVYRPKFL---SKTVRITFGF--NCRNKDHYGIMMYHRN 321
Cdd:pfam17942   1 YSLRAYASILYLRlpPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGggkEVVVITTIGFlkEAPHINVHGFNVYHKN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28872812   322 RLIKAYEKVGCQlrANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTITALGEKLNDYW 382
Cdd:pfam17942  81 RLIKPFWRVGNQ--AGSKGRGVIGVLEANFIEPTHDKQDFERTSLYQRLEARLKQMLKEYW 139
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 18-135 1.23e-65

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: 215.35  E-value: 1.23e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812  18 FLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVIN-DHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNgHVP 96
Cdd:cd16931   1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLrGGFMLSFLDDGNGMTPEEAHHMISFGFSDKRSDD-HDH 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 28872812  97 VGLYGNGFKSGSMRLGKDAIVFTKNGESMSVGLLSQTYL 135
Cdd:cd16931  80 IGRYGNGFKSGSMRLGRDVIVFTKKDESQSCGLLSQTFL 118
zf-CW pfam07496
CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four ...
 409-446 2.74e-18

CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four conserved cysteine residues and a conserved tryptophan. It was first identified by, and is predicted to be a "highly specialized mononuclear four-cysteine zinc finger...that plays a role in DNA binding and/or promoting protein-protein interactions in complicated eukaryotic processes including...chromatin methylation status and early embryonic development." Weak homology to pfam00628 further evidences these predictions (personal obs: C Yeats). Twelve different CW-domain-containing protein subfamilies are described, with different subfamilies being characteriztic of vertebrates, higher plants and other animals in which these domain is found.


Pssm-ID: 462181  Cd Length: 46  Bit Score: 78.89  E-value: 2.74e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 28872812   409 TWVQCDACLKWRKLPDGMD--QLPEKWYCSNNPDPQFRNC 446
Cdd:pfam07496   1 YWVQCDSCLKWRRLPTEIDpyELPEPWYCSMNPDPKYNSC 40
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 29-136 1.01e-16

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: 77.76  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    29 PFSAVAELIDNAYDPDVNAKQIWIDKTVINDHIClTFTDNGNGMTSDKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGS 108
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKNRGGGTEI-VIEDDGHGMSPEELINALRLATSAKEAKRGSTDLGRYGIGLKLAS 79

                          90       100
                  ....*....|....*....|....*...
gi 28872812   109 MRLGKDAIVFTKNGESMSVGLLSQTYLE 136
Cdd:pfam13589  80 LSLGAKLTVTSKKEGKSSTLTLDRDKIS 107
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
673-866 1.05e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 673 EAEAKIHETQETTDksaddagcQLQELRNQLLLVTEEKENYKRQchmftdqIKVLQQRILEMNDKYVKKETCHQSTETDA 752
Cdd:COG4717  75 ELEEELKEAEEKEE--------EYAELQEELEELEEELEELEAE-------LEELREELEKLEKLLQLLPLYQELEALEA 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 753 VflLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHVKAECSQCSNNESKSEMDEMAVQLDDVFRQldkcsieRDQ 832
Cdd:COG4717 140 E--LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------LAE 210

                       170       180       190
                ....*....|....*....|....*....|....
gi 28872812 833 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQ 866
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEER 244
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 32-100 2.36e-05

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 44.18  E-value: 2.36e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28872812     32 AVAELIDNAYDPDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFS--DKVTMNGHVPVGLY 100
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRtdKRSRKIGGTGLGLS 79
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 622-936 6.74e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.04  E-value: 6.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    622 TGSTSTSSSRCDQGNTAATQTEVpslvVKKEETVEDEIDVRNDAVILPSCVEAEAKIHETQETTDKsaddagcQLQELRN 701
Cdd:pfam15921  281 TGLTEKASSARSQANSIQSQLEI----IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED-------KIEELEK 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    702 QLLL----VTE---EKENYKRQCHMFTDQikvLQQRILEMNDKyvKKETCHQSTETDAvfLLESINGKSESPDHMVSQYQ 774
Cdd:pfam15921  350 QLVLanseLTEartERDQFSQESGNLDDQ---LQKLLADLHKR--EKELSLEKEQNKR--LWDRDTGNSITIDHLRRELD 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    775 QALEEIERLKkqcSALQHVKAECsqcsnnesKSEMDEMAVQLDDVFRQLDKCSierdqykSEVELLEMEKSQIRSQCEEL 854
Cdd:pfam15921  423 DRNMEVQRLE---ALLKAMKSEC--------QGQMERQMAAIQGKNESLEKVS-------SLTAQLESTKEMLRKVVEEL 484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    855 KTEVEQLKSTnQQTATDVSTS-SNIEESVNHMDGESLKLRSlRVNVG-QLLAMIVPDLD-LQQVNYDV----------DV 921
Cdd:pfam15921  485 TAKKMTLESS-ERTVSDLTASlQEKERAIEATNAEITKLRS-RVDLKlQELQHLKNEGDhLRNVQTECealklqmaekDK 562

                          330
                   ....*....|....*
gi 28872812    922 VDEILGQVVEQMSEI 936
Cdd:pfam15921  563 VIEILRQQIENMTQL 577
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 31-88 1.11e-03

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 42.53  E-value: 1.11e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28872812  31 SAVAELIDNAYD----PDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFSDK 88
Cdd:COG3290 284 TILGNLLDNAIEavekLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTK 345
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
764-894 1.12e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812  764 ESPDHMVSQYQQALEEIERLKKQCSALQHVKAECsqcsnnesKSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEME 843
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAET--------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 28872812  844 KSQIRSQCEELKTEVEQLKSTNQQTATDVS-TSSNIE---ESVNHMDGESLKLRS 894
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQaHNEEAEslrEDADDLEERAEELRE 363
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 673-897 2.34e-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: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    673 EAEAKIHETQEttDKSADDAgcQLQELRNQLLLVTEEKENYKRQCHMFTDQIkvLQQRILEMNDKYVKKETCHQSTETDA 752
Cdd:TIGR02169  741 ELEEDLSSLEQ--EIENVKS--ELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    753 VFLLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHvKAECSQCSNNESKSEMDEMAVQLDDVFRQLDKCSIERDQ 832
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK-EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    833 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDVST-----SSNIEESVNHMDGESLKLRSLRV 897
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRV 963
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 808-936 3.97e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 3.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 808 EMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEK-SQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEESVNHMD 886
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 28872812 887 GESLKLRSLRVNVGQLLAMIVPdldlqQVNYDVDvVDEIlGQVVEQMSEI 936
Cdd:COG0542 485 GKIPELEKELAELEEELAELAP-----LLREEVT-EEDI-AEVVSRWTGI 527
 
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. ...
 249-382 3.26e-70

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: 228.97  E-value: 3.26e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812   249 YSLRAYCSILYLK--PRMQIILRGQKVKTQLVSKSLAYIERDVYRPKFL---SKTVRITFGF--NCRNKDHYGIMMYHRN 321
Cdd:pfam17942   1 YSLRAYASILYLRlpPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGggkEVVVITTIGFlkEAPHINVHGFNVYHKN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28872812   322 RLIKAYEKVGCQlrANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTITALGEKLNDYW 382
Cdd:pfam17942  81 RLIKPFWRVGNQ--AGSKGRGVIGVLEANFIEPTHDKQDFERTSLYQRLEARLKQMLKEYW 139
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 18-135 1.23e-65

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: 215.35  E-value: 1.23e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812  18 FLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVIN-DHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNgHVP 96
Cdd:cd16931   1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLrGGFMLSFLDDGNGMTPEEAHHMISFGFSDKRSDD-HDH 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 28872812  97 VGLYGNGFKSGSMRLGKDAIVFTKNGESMSVGLLSQTYL 135
Cdd:cd16931  80 IGRYGNGFKSGSMRLGRDVIVFTKKDESQSCGLLSQTFL 118
zf-CW pfam07496
CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four ...
 409-446 2.74e-18

CW-type Zinc Finger; This domain appears to be a zinc finger. The alignment shows four conserved cysteine residues and a conserved tryptophan. It was first identified by, and is predicted to be a "highly specialized mononuclear four-cysteine zinc finger...that plays a role in DNA binding and/or promoting protein-protein interactions in complicated eukaryotic processes including...chromatin methylation status and early embryonic development." Weak homology to pfam00628 further evidences these predictions (personal obs: C Yeats). Twelve different CW-domain-containing protein subfamilies are described, with different subfamilies being characteriztic of vertebrates, higher plants and other animals in which these domain is found.


Pssm-ID: 462181  Cd Length: 46  Bit Score: 78.89  E-value: 2.74e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 28872812   409 TWVQCDACLKWRKLPDGMD--QLPEKWYCSNNPDPQFRNC 446
Cdd:pfam07496   1 YWVQCDSCLKWRRLPTEIDpyELPEPWYCSMNPDPKYNSC 40
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 29-136 1.01e-16

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: 77.76  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    29 PFSAVAELIDNAYDPDVNAKQIWIDKTVINDHIClTFTDNGNGMTSDKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGS 108
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKNRGGGTEI-VIEDDGHGMSPEELINALRLATSAKEAKRGSTDLGRYGIGLKLAS 79

                          90       100
                  ....*....|....*....|....*...
gi 28872812   109 MRLGKDAIVFTKNGESMSVGLLSQTYLE 136
Cdd:pfam13589  80 LSLGAKLTVTSKKEGKSSTLTLDRDKIS 107
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
673-866 1.05e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 673 EAEAKIHETQETTDksaddagcQLQELRNQLLLVTEEKENYKRQchmftdqIKVLQQRILEMNDKYVKKETCHQSTETDA 752
Cdd:COG4717  75 ELEEELKEAEEKEE--------EYAELQEELEELEEELEELEAE-------LEELREELEKLEKLLQLLPLYQELEALEA 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 753 VflLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHVKAECSQCSNNESKSEMDEMAVQLDDVFRQldkcsieRDQ 832
Cdd:COG4717 140 E--LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------LAE 210

                       170       180       190
                ....*....|....*....|....*....|....
gi 28872812 833 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQ 866
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEER 244
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
 30-100 1.19e-06

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.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 47.60  E-value: 1.19e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28872812  30 FSAVAELIDNAYDPDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKML-SFGFSDKVTMNGHVPVGLY 100
Cdd:cd00075   2 EQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFeRFYRGDKSREGGGTGLGLA 73
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
759-867 5.56e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 5.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 759 INGKSESPDHMVSQYQQALEEIERLKKQcsaLQHVKAECSQCSN--NESKSEMDEMAVQLDDVFRQLDKCSIERDQYKSE 836
Cdd:COG4372  26 IAALSEQLRKALFELDKLQEELEQLREE---LEQAREELEQLEEelEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102

                        90       100       110
                ....*....|....*....|....*....|.
gi 28872812 837 VELLEMEKSQIRSQCEELKTEVEQLKSTNQQ 867
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQ 133
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 32-100 2.36e-05

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 44.18  E-value: 2.36e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28872812     32 AVAELIDNAYDPDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFS--DKVTMNGHVPVGLY 100
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRtdKRSRKIGGTGLGLS 79
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 622-936 6.74e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.04  E-value: 6.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    622 TGSTSTSSSRCDQGNTAATQTEVpslvVKKEETVEDEIDVRNDAVILPSCVEAEAKIHETQETTDKsaddagcQLQELRN 701
Cdd:pfam15921  281 TGLTEKASSARSQANSIQSQLEI----IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED-------KIEELEK 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    702 QLLL----VTE---EKENYKRQCHMFTDQikvLQQRILEMNDKyvKKETCHQSTETDAvfLLESINGKSESPDHMVSQYQ 774
Cdd:pfam15921  350 QLVLanseLTEartERDQFSQESGNLDDQ---LQKLLADLHKR--EKELSLEKEQNKR--LWDRDTGNSITIDHLRRELD 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    775 QALEEIERLKkqcSALQHVKAECsqcsnnesKSEMDEMAVQLDDVFRQLDKCSierdqykSEVELLEMEKSQIRSQCEEL 854
Cdd:pfam15921  423 DRNMEVQRLE---ALLKAMKSEC--------QGQMERQMAAIQGKNESLEKVS-------SLTAQLESTKEMLRKVVEEL 484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    855 KTEVEQLKSTnQQTATDVSTS-SNIEESVNHMDGESLKLRSlRVNVG-QLLAMIVPDLD-LQQVNYDV----------DV 921
Cdd:pfam15921  485 TAKKMTLESS-ERTVSDLTASlQEKERAIEATNAEITKLRS-RVDLKlQELQHLKNEGDhLRNVQTECealklqmaekDK 562

                          330
                   ....*....|....*
gi 28872812    922 VDEILGQVVEQMSEI 936
Cdd:pfam15921  563 VIEILRQQIENMTQL 577
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 32-100 1.56e-04

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: 41.97  E-value: 1.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28872812    32 AVAELIDNAYDPDVNAKQIWIdKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNGHVPVGLY 100
Cdd:pfam02518   9 VLSNLLDNALKHAAKAGEITV-TLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGGGTGLGLS 76
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
 769-861 8.16e-04

Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.


Pssm-ID: 465154 [Multi-domain]  Cd Length: 99  Bit Score: 39.61  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812   769 MVSQYQQALEEIERLKKQCS-ALQHVKAecsqcsnnESKSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEKSQI 847
Cdd:pfam16515  14 QLTVAQQAQEEVEREKKQLEfELERAKE--------EAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQSGSQL 85

                          90
                  ....*....|....
gi 28872812   848 RSQCEELKTEVEQL 861
Cdd:pfam16515  86 SSQLAALQAEKEGL 99
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 31-88 1.11e-03

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 42.53  E-value: 1.11e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28872812  31 SAVAELIDNAYD----PDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFSDK 88
Cdd:COG3290 284 TILGNLLDNAIEavekLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTK 345
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
764-894 1.12e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812  764 ESPDHMVSQYQQALEEIERLKKQCSALQHVKAECsqcsnnesKSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEME 843
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAET--------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 28872812  844 KSQIRSQCEELKTEVEQLKSTNQQTATDVS-TSSNIE---ESVNHMDGESLKLRS 894
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQaHNEEAEslrEDADDLEERAEELRE 363
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 695-881 2.14e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.60  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812   695 QLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQRILEMNDkyVKKETCHQSTETDAvflLESINGKSESPDHMVSQYQ 774
Cdd:pfam05622  67 QLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTS--LAEEAQALKDEMDI---LRESSDKVKKLEATVETYK 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812   775 QALEEIERLKKQCSALQHVKAECSQ--CSNNES--------------KSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVE 838
Cdd:pfam05622 142 KKLEDLGDLRRQVKLLEERNAEYMQrtLQLEEElkkanalrgqletyKRQVQELHGKLSEESKKADKLEFEYKKLEEKLE 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 28872812   839 LLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEES 881
Cdd:pfam05622 222 ALQKEKERLIIERDTLRETNEELRCAQLQQAELSQADALLSPS 264
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
673-872 2.24e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 673 EAEAKIHETQETTDKSADDAGCQLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQRILEMNDKYVKKETCHQSTETDa 752
Cdd:COG4372  24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 753 vflLESINGksespdhmvsQYQQALEEIERLKKQCSALQHVKAECSQcSNNESKSEMDEMAVQLDDVFRQLDkcSIERDQ 832
Cdd:COG4372 103 ---LESLQE----------EAEELQEELEELQKERQDLEQQRKQLEA-QIAELQSEIAEREEELKELEEQLE--SLQEEL 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 28872812 833 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDV 872
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 673-897 2.34e-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: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    673 EAEAKIHETQEttDKSADDAgcQLQELRNQLLLVTEEKENYKRQCHMFTDQIkvLQQRILEMNDKYVKKETCHQSTETDA 752
Cdd:TIGR02169  741 ELEEDLSSLEQ--EIENVKS--ELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    753 VFLLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHvKAECSQCSNNESKSEMDEMAVQLDDVFRQLDKCSIERDQ 832
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK-EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    833 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDVST-----SSNIEESVNHMDGESLKLRSLRV 897
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRV 963
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 808-936 3.97e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 3.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 808 EMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEK-SQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEESVNHMD 886
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 28872812 887 GESLKLRSLRVNVGQLLAMIVPdldlqQVNYDVDvVDEIlGQVVEQMSEI 936
Cdd:COG0542 485 GKIPELEKELAELEEELAELAP-----LLREEVT-EEDI-AEVVSRWTGI 527
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 673-864 4.28e-03

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: 40.52  E-value: 4.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 673 EAEAKIHETQETTDKSADdagcQLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQRILEMNDKYVKKE--------TC 744
Cdd:COG4942  38 ELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelaellrAL 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 745 HQSTETDAVFLLESingkSESPD------HMVSQYQQAL-EEIERLKKQCSALQHVKAECSQcsnnesksEMDEMAVQLD 817
Cdd:COG4942 114 YRLGRQPPLALLLS----PEDFLdavrrlQYLKYLAPARrEQAEELRADLAELAALRAELEA--------ERAELEALLA 181

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 28872812 818 DVFRQLDKCSIERDQYKSEVELLEMEKSQIRSQCEELKTEVEQLKST 864
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
695-867 4.39e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 4.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 695 QLQELRNQLLLVTEEKENYKRQcHMFTD---QIKVLQQRILEMNDKYVKKetchQSTETDAVFLLESINGKSESPDHMVS 771
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQK-NGLVDlseEAKLLLQQLSELESQLAEA----RAELAEAEARLAALRAQLGSGPDALP 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812 772 QYQQAlEEIERLKKQCSALQHVKAECSQcSNNESKSEMDEMAVQLDDVFRQLDKcSIER--DQYKSEVELLEMEKSQIRS 849
Cdd:COG3206 258 ELLQS-PVIQQLRAQLAELEAELAELSA-RYTPNHPDVIALRAQIAALRAQLQQ-EAQRilASLEAELEALQAREASLQA 334

                       170
                ....*....|....*...
gi 28872812 850 QCEELKTEVEQLKSTNQQ 867
Cdd:COG3206 335 QLAQLEARLAELPELEAE 352
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 36-80 4.42e-03

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 40.55  E-value: 4.42e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 28872812  36 LIDNAYD--PDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKM 80
Cdd:COG4191 264 LLINAIDamEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERI 310
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 650-862 6.27e-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: 40.43  E-value: 6.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    650 KKEETVEDEIDVRNDAVilpscVEAEAKIHETQETTDKSADdagcQLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQ 729
Cdd:TIGR02168  740 AEVEQLEERIAQLSKEL-----TELEAEIEELEERLEEAEE----ELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872812    730 RILEMNDKYVKKETCHQSTETDAVFLLESIngksespdhmvsqyQQALEEIERLKKQCSALQHvkaecsqcsnnesksEM 809
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRL--------------EDLEEQIEELSEDIESLAA---------------EI 861

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28872812    810 DEMAVQLDDVFRQLDKCSIERDQ------------YKSEVELLEMEK--SQIRSQCEELKTEVEQLK 862
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASleealallrselEELSEELRELESkrSELRRELEELREKLAQLE 928
 
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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