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Conserved domains on  [gi|119630147|gb|EAX09742|]
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MORC family CW-type zinc finger 3 [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. ...
 251-384 3.91e-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: 228.58  E-value: 3.91e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147  251 YSLRAYCSILYLK--PRMQIILRGQKVKTQLVSKSLAYIERDVYRPKFL---SKTVRITFGF--NCRNKDHYGIMMYHRN 323
Cdd:pfam17942   1 YSLRAYASILYLRlpPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGggkEVVVITTIGFlkEAPHINVHGFNVYHKN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119630147  324 RLIKAYEKVGCQlrANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTITALGEKLNDYW 384
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 1.25e-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: 1.25e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147  18 FLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVIN-DHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNgHVP 96
Cdd:cd16931    1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLrGGFMLSFLDDGNGMTPEEAHHMISFGFSDKRSDD-HDH 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119630147  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 ...
 411-448 2.39e-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: 79.27  E-value: 2.39e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 119630147  411 TWVQCDACLKWRKLPDGMD--QLPEKWYCSNNPDPQFRNC 448
Cdd:pfam07496   1 YWVQCDSCLKWRRLPTEIDpyELPEPWYCSMNPDPKYNSC 40
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
675-868 1.02e-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: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 675 EAEAKIHETQETTDksaddagcQLQELRNQLLLVTEEKENYKRQchmftdqIKVLQQRILEMNDKYVKKETCHQSTETDA 754
Cdd:COG4717   75 ELEEELKEAEEKEE--------EYAELQEELEELEEELEELEAE-------LEELREELEKLEKLLQLLPLYQELEALEA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 755 VflLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHVKAECSQCSNNESKSEMDEMAVQLDDVFRQldkcsieRDQ 834
Cdd:COG4717  140 E--LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------LAE 210

                        170       180       190
                 ....*....|....*....|....*....|....
gi 119630147 835 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQ 868
Cdd:COG4717  211 LEEELEEAQEELEELEEELEQLENELEAAALEER 244
ClpA super family cl33938
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 810-938 4.01e-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: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 810 EMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEK-SQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEESVNHMD 888
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119630147 889 GESLKLRSLRVNVGQLLAMIVPdldlqQVNYDVDvVDEIlGQVVEQMSEI 938
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. ...
 251-384 3.91e-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: 228.58  E-value: 3.91e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147  251 YSLRAYCSILYLK--PRMQIILRGQKVKTQLVSKSLAYIERDVYRPKFL---SKTVRITFGF--NCRNKDHYGIMMYHRN 323
Cdd:pfam17942   1 YSLRAYASILYLRlpPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGggkEVVVITTIGFlkEAPHINVHGFNVYHKN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119630147  324 RLIKAYEKVGCQlrANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTITALGEKLNDYW 384
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 1.25e-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: 1.25e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147  18 FLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVIN-DHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNgHVP 96
Cdd:cd16931    1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLrGGFMLSFLDDGNGMTPEEAHHMISFGFSDKRSDD-HDH 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119630147  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 ...
 411-448 2.39e-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: 79.27  E-value: 2.39e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 119630147  411 TWVQCDACLKWRKLPDGMD--QLPEKWYCSNNPDPQFRNC 448
Cdd:pfam07496   1 YWVQCDSCLKWRRLPTEIDpyELPEPWYCSMNPDPKYNSC 40
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 29-136 1.05e-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: 77.37  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   29 PFSAVAELIDNAYDPDVNAKQIWIDKTVINDHIClTFTDNGNGMTSDKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGS 108
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKNRGGGTEI-VIEDDGHGMSPEELINALRLATSAKEAKRGSTDLGRYGIGLKLAS 79

                          90       100
                  ....*....|....*....|....*...
gi 119630147  109 MRLGKDAIVFTKNGESMSVGLLSQTYLE 136
Cdd:pfam13589  80 LSLGAKLTVTSKKEGKSSTLTLDRDKIS 107
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
675-868 1.02e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 675 EAEAKIHETQETTDksaddagcQLQELRNQLLLVTEEKENYKRQchmftdqIKVLQQRILEMNDKYVKKETCHQSTETDA 754
Cdd:COG4717   75 ELEEELKEAEEKEE--------EYAELQEELEELEEELEELEAE-------LEELREELEKLEKLLQLLPLYQELEALEA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 755 VflLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHVKAECSQCSNNESKSEMDEMAVQLDDVFRQldkcsieRDQ 834
Cdd:COG4717  140 E--LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------LAE 210

                        170       180       190
                 ....*....|....*....|....*....|....
gi 119630147 835 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQ 868
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 119630147    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. ...
 624-938 3.55e-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: 47.81  E-value: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   624 TGSTSTSSSRCDQGNTAATQTEVpslvVKKEETVEDEIDVRNDAVILPSCVEAEAKIHETQETTDKsaddagcQLQELRN 703
Cdd:pfam15921  281 TGLTEKASSARSQANSIQSQLEI----IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED-------KIEELEK 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   704 QLLL----VTE---EKENYKRQCHMFTDQikvLQQRILEMNDKyvKKETCHQSTETDAvfLLESINGKSESPDHMVSQYQ 776
Cdd:pfam15921  350 QLVLanseLTEartERDQFSQESGNLDDQ---LQKLLADLHKR--EKELSLEKEQNKR--LWDRDTGNSITIDHLRRELD 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   777 QALEEIERLKkqcSALQHVKAECsqcsnnesKSEMDEMAVQLDDVFRQLDKCSierdqykSEVELLEMEKSQIRSQCEEL 856
Cdd:pfam15921  423 DRNMEVQRLE---ALLKAMKSEC--------QGQMERQMAAIQGKNESLEKVS-------SLTAQLESTKEMLRKVVEEL 484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   857 KTEVEQLKSTnQQTATDVSTS-SNIEESVNHMDGESLKLRSlRVNVG-QLLAMIVPDLD-LQQVNYDV----------DV 923
Cdd:pfam15921  485 TAKKMTLESS-ERTVSDLTASlQEKERAIEATNAEITKLRS-RVDLKlQELQHLKNEGDhLRNVQTECealklqmaekDK 562

                          330
                   ....*....|....*
gi 119630147   924 VDEILGQVVEQMSEI 938
Cdd:pfam15921  563 VIEILRQQIENMTQL 577
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
766-896 1.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 766 ESPDHMVSQYQQALEEIERLKKQCSALQHVKAECsqcsnnesKSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEME 845
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAET--------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119630147 846 KSQIRSQCEELKTEVEQLKSTNQQTATDVS-TSSNIE---ESVNHMDGESLKLRS 896
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQaHNEEAEslrEDADDLEERAEELRE 363
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 31-88 1.17e-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: 1.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119630147  31 SAVAELIDNAYD----PDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFSDK 88
Cdd:COG3290  284 TILGNLLDNAIEavekLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTK 345
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 675-899 2.09e-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: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   675 EAEAKIHETQEttDKSADDAgcQLQELRNQLLLVTEEKENYKRQCHMFTDQIkvLQQRILEMNDKYVKKETCHQSTETDA 754
Cdd:TIGR02169  741 ELEEDLSSLEQ--EIENVKS--ELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   755 VFLLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHvKAECSQCSNNESKSEMDEMAVQLDDVFRQLDKCSIERDQ 834
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK-EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   835 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDVST-----SSNIEESVNHMDGESLKLRSLRV 899
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRV 963
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 810-938 4.01e-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: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 810 EMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEK-SQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEESVNHMD 888
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119630147 889 GESLKLRSLRVNVGQLLAMIVPdldlqQVNYDVDvVDEIlGQVVEQMSEI 938
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. ...
 251-384 3.91e-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: 228.58  E-value: 3.91e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147  251 YSLRAYCSILYLK--PRMQIILRGQKVKTQLVSKSLAYIERDVYRPKFL---SKTVRITFGF--NCRNKDHYGIMMYHRN 323
Cdd:pfam17942   1 YSLRAYASILYLRlpPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGggkEVVVITTIGFlkEAPHINVHGFNVYHKN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119630147  324 RLIKAYEKVGCQlrANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTITALGEKLNDYW 384
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 1.25e-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: 1.25e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147  18 FLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVIN-DHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNgHVP 96
Cdd:cd16931    1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLrGGFMLSFLDDGNGMTPEEAHHMISFGFSDKRSDD-HDH 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119630147  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 ...
 411-448 2.39e-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: 79.27  E-value: 2.39e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 119630147  411 TWVQCDACLKWRKLPDGMD--QLPEKWYCSNNPDPQFRNC 448
Cdd:pfam07496   1 YWVQCDSCLKWRRLPTEIDpyELPEPWYCSMNPDPKYNSC 40
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 29-136 1.05e-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: 77.37  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   29 PFSAVAELIDNAYDPDVNAKQIWIDKTVINDHIClTFTDNGNGMTSDKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGS 108
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKNRGGGTEI-VIEDDGHGMSPEELINALRLATSAKEAKRGSTDLGRYGIGLKLAS 79

                          90       100
                  ....*....|....*....|....*...
gi 119630147  109 MRLGKDAIVFTKNGESMSVGLLSQTYLE 136
Cdd:pfam13589  80 LSLGAKLTVTSKKEGKSSTLTLDRDKIS 107
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
675-868 1.02e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 675 EAEAKIHETQETTDksaddagcQLQELRNQLLLVTEEKENYKRQchmftdqIKVLQQRILEMNDKYVKKETCHQSTETDA 754
Cdd:COG4717   75 ELEEELKEAEEKEE--------EYAELQEELEELEEELEELEAE-------LEELREELEKLEKLLQLLPLYQELEALEA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 755 VflLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHVKAECSQCSNNESKSEMDEMAVQLDDVFRQldkcsieRDQ 834
Cdd:COG4717  140 E--LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------LAE 210

                        170       180       190
                 ....*....|....*....|....*....|....
gi 119630147 835 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQ 868
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 119630147  30 FSAVAELIDNAYDPDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKML-SFGFSDKVTMNGHVPVGLY 100
Cdd:cd00075    2 EQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFeRFYRGDKSREGGGTGLGLA 73
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
761-869 4.72e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 761 INGKSESPDHMVSQYQQALEEIERLKKQcsaLQHVKAECSQCSN--NESKSEMDEMAVQLDDVFRQLDKCSIERDQYKSE 838
Cdd:COG4372   26 IAALSEQLRKALFELDKLQEELEQLREE---LEQAREELEQLEEelEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102

                         90       100       110
                 ....*....|....*....|....*....|.
gi 119630147 839 VELLEMEKSQIRSQCEELKTEVEQLKSTNQQ 869
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 119630147    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. ...
 624-938 3.55e-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: 47.81  E-value: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   624 TGSTSTSSSRCDQGNTAATQTEVpslvVKKEETVEDEIDVRNDAVILPSCVEAEAKIHETQETTDKsaddagcQLQELRN 703
Cdd:pfam15921  281 TGLTEKASSARSQANSIQSQLEI----IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED-------KIEELEK 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   704 QLLL----VTE---EKENYKRQCHMFTDQikvLQQRILEMNDKyvKKETCHQSTETDAvfLLESINGKSESPDHMVSQYQ 776
Cdd:pfam15921  350 QLVLanseLTEartERDQFSQESGNLDDQ---LQKLLADLHKR--EKELSLEKEQNKR--LWDRDTGNSITIDHLRRELD 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   777 QALEEIERLKkqcSALQHVKAECsqcsnnesKSEMDEMAVQLDDVFRQLDKCSierdqykSEVELLEMEKSQIRSQCEEL 856
Cdd:pfam15921  423 DRNMEVQRLE---ALLKAMKSEC--------QGQMERQMAAIQGKNESLEKVS-------SLTAQLESTKEMLRKVVEEL 484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   857 KTEVEQLKSTnQQTATDVSTS-SNIEESVNHMDGESLKLRSlRVNVG-QLLAMIVPDLD-LQQVNYDV----------DV 923
Cdd:pfam15921  485 TAKKMTLESS-ERTVSDLTASlQEKERAIEATNAEITKLRS-RVDLKlQELQHLKNEGDhLRNVQTECealklqmaekDK 562

                          330
                   ....*....|....*
gi 119630147   924 VDEILGQVVEQMSEI 938
Cdd:pfam15921  563 VIEILRQQIENMTQL 577
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 32-100 1.57e-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: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119630147   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 ...
 771-863 6.93e-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: 39.99  E-value: 6.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147  771 MVSQYQQALEEIERLKKQCS-ALQHVKAecsqcsnnESKSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEKSQI 849
Cdd:pfam16515  14 QLTVAQQAQEEVEREKKQLEfELERAKE--------EAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQSGSQL 85

                          90
                  ....*....|....
gi 119630147  850 RSQCEELKTEVEQL 863
Cdd:pfam16515  86 SSQLAALQAEKEGL 99
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
766-896 1.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 766 ESPDHMVSQYQQALEEIERLKKQCSALQHVKAECsqcsnnesKSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEME 845
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAET--------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119630147 846 KSQIRSQCEELKTEVEQLKSTNQQTATDVS-TSSNIE---ESVNHMDGESLKLRS 896
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQaHNEEAEslrEDADDLEERAEELRE 363
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 31-88 1.17e-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: 1.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119630147  31 SAVAELIDNAYD----PDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFSDK 88
Cdd:COG3290  284 TILGNLLDNAIEavekLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTK 345
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
675-874 1.84e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 675 EAEAKIHETQETTDKSADDAGCQLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQRILEMNDKYVKKETCHQSTETDa 754
Cdd:COG4372   24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 755 vflLESINGksespdhmvsQYQQALEEIERLKKQCSALQHVKAECSQcSNNESKSEMDEMAVQLDDVFRQLDkcSIERDQ 834
Cdd:COG4372  103 ---LESLQE----------EAEELQEELEELQKERQDLEQQRKQLEA-QIAELQSEIAEREEELKELEEQLE--SLQEEL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 119630147 835 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDV 874
Cdd:COG4372  167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 697-883 1.87e-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: 41.98  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147  697 QLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQRILEMNDkyVKKETCHQSTETDAvflLESINGKSESPDHMVSQYQ 776
Cdd:pfam05622  67 QLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTS--LAEEAQALKDEMDI---LRESSDKVKKLEATVETYK 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147  777 QALEEIERLKKQCSALQHVKAECSQ--CSNNES--------------KSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVE 840
Cdd:pfam05622 142 KKLEDLGDLRRQVKLLEERNAEYMQrtLQLEEElkkanalrgqletyKRQVQELHGKLSEESKKADKLEFEYKKLEEKLE 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 119630147  841 LLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEES 883
Cdd:pfam05622 222 ALQKEKERLIIERDTLRETNEELRCAQLQQAELSQADALLSPS 264
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 675-899 2.09e-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: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   675 EAEAKIHETQEttDKSADDAgcQLQELRNQLLLVTEEKENYKRQCHMFTDQIkvLQQRILEMNDKYVKKETCHQSTETDA 754
Cdd:TIGR02169  741 ELEEDLSSLEQ--EIENVKS--ELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   755 VFLLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHvKAECSQCSNNESKSEMDEMAVQLDDVFRQLDKCSIERDQ 834
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK-EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   835 YKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDVST-----SSNIEESVNHMDGESLKLRSLRV 899
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRV 963
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 675-866 3.60e-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: 40.90  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 675 EAEAKIHETQETTDKSADdagcQLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQRILEMNDKYVKKE--------TC 746
Cdd:COG4942   38 ELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelaellrAL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 747 HQSTETDAVFLLESingkSESPD------HMVSQYQQAL-EEIERLKKQCSALQHVKAECSQcsnnesksEMDEMAVQLD 819
Cdd:COG4942  114 YRLGRQPPLALLLS----PEDFLdavrrlQYLKYLAPARrEQAEELRADLAELAALRAELEA--------ERAELEALLA 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 119630147 820 DVFRQLDKCSIERDQYKSEVELLEMEKSQIRSQCEELKTEVEQLKST 866
Cdd:COG4942  182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 810-938 4.01e-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: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 810 EMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEK-SQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEESVNHMD 888
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119630147 889 GESLKLRSLRVNVGQLLAMIVPdldlqQVNYDVDvVDEIlGQVVEQMSEI 938
Cdd:COG0542  485 GKIPELEKELAELEEELAELAP-----LLREEVT-EEDI-AEVVSRWTGI 527
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
697-869 4.40e-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: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 697 QLQELRNQLLLVTEEKENYKRQcHMFTD---QIKVLQQRILEMNDKYVKKetchQSTETDAVFLLESINGKSESPDHMVS 773
Cdd:COG3206  183 QLPELRKELEEAEAALEEFRQK-NGLVDlseEAKLLLQQLSELESQLAEA----RAELAEAEARLAALRAQLGSGPDALP 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147 774 QYQQAlEEIERLKKQCSALQHVKAECSQcSNNESKSEMDEMAVQLDDVFRQLDKcSIER--DQYKSEVELLEMEKSQIRS 851
Cdd:COG3206  258 ELLQS-PVIQQLRAQLAELEAELAELSA-RYTPNHPDVIALRAQIAALRAQLQQ-EAQRilASLEAELEALQAREASLQA 334

                        170
                 ....*....|....*...
gi 119630147 852 QCEELKTEVEQLKSTNQQ 869
Cdd:COG3206  335 QLAQLEARLAELPELEAE 352
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 36-80 4.43e-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: 4.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 119630147  36 LIDNAYD--PDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKM 80
Cdd:COG4191  264 LLINAIDamEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERI 310
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 652-864 5.63e-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: 40.81  E-value: 5.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   652 KKEETVEDEIDVRNDAVilpscVEAEAKIHETQETTDKSADdagcQLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQ 731
Cdd:TIGR02168  740 AEVEQLEERIAQLSKEL-----TELEAEIEELEERLEEAEE----ELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119630147   732 RILEMNDKYVKKETCHQSTETDAVFLLESIngksespdhmvsqyQQALEEIERLKKQCSALQHvkaecsqcsnnesksEM 811
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRL--------------EDLEEQIEELSEDIESLAA---------------EI 861

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119630147   812 DEMAVQLDDVFRQLDKCSIERDQ------------YKSEVELLEMEK--SQIRSQCEELKTEVEQLK 864
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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