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Conserved domains on  [gi|980952224|sp|F7BJB9|]
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RecName: Full=MORC family CW-type zinc finger protein 3; AltName: Full=Nuclear matrix protein 2; AltName: Full=Zinc finger CW-type coiled-coil domain protein 3

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 2.36e-69

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: 226.65  E-value: 2.36e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  249 YSLRAYCSILYLK--PRMQIIIRGQKVKTQLVSKSLAYIERDVYRPKFLTR---TVRITFGF--NCRNKDHYGIMMYHKN 321
Cdd:pfam17942   1 YSLRAYASILYLRlpPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGGGkevVVITTIGFlkEAPHINVHGFNVYHKN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 980952224  322 RLIKAYEKVGCQlkANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTILALGEKLNDYW 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 3.06e-64

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: 211.88  E-value: 3.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  18 FLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVIS-DHICLTFTDNGNGMTADKLHKMLSFGFSDKVTMNgHVP 96
Cdd:cd16931    1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLrGGFMLSFLDDGNGMTPEEAHHMISFGFSDKRSDD-HDH 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 980952224  97 VGLYGNGFKSGSMRLGKDAMVFTKNGETMSVGFLSQTYL 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 1.18e-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: 80.05  E-value: 1.18e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 980952224  409 TWVQCDACLKWRKLPDGID--QLPEKWYCSNNPDPQFRNC 446
Cdd:pfam07496   1 YWVQCDSCLKWRRLPTEIDpyELPEPWYCSMNPDPKYNSC 40
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
698-910 2.53e-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: 51.31  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 698 QLQELRSELLVVTQERDDYKR---QCQMFTDQIQVLQQRLLEMNDKCVKKEKCHQ-----STETDAVFLLDSVNGQAESL 769
Cdd:COG4717   72 ELKELEEELKEAEEKEEEYAElqeELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEEL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 770 DHLGSQYQQALQEIERLKRQCSALQQVKSECSQASCTESKSEVDEMAVQLDDVFRQldkctieRDQYKNEVQLLEIEKSH 849
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------LAELEEELEEAQEELEE 224

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 980952224 850 IHSQCEELQTEVEQLKSTGQQAAADGSTASNAEepVSYVDGESLKLRSLRVNVGQLLAMIV 910
Cdd:COG4717  225 LEEELEQLENELEAAALEERLKEARLLLLIAAA--LLALLGLGGSLLSLILTIAGVLFLVL 283
 
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 2.36e-69

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: 226.65  E-value: 2.36e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  249 YSLRAYCSILYLK--PRMQIIIRGQKVKTQLVSKSLAYIERDVYRPKFLTR---TVRITFGF--NCRNKDHYGIMMYHKN 321
Cdd:pfam17942   1 YSLRAYASILYLRlpPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGGGkevVVITTIGFlkEAPHINVHGFNVYHKN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 980952224  322 RLIKAYEKVGCQlkANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTILALGEKLNDYW 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 3.06e-64

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: 211.88  E-value: 3.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  18 FLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVIS-DHICLTFTDNGNGMTADKLHKMLSFGFSDKVTMNgHVP 96
Cdd:cd16931    1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLrGGFMLSFLDDGNGMTPEEAHHMISFGFSDKRSDD-HDH 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 980952224  97 VGLYGNGFKSGSMRLGKDAMVFTKNGETMSVGFLSQTYL 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 1.18e-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: 80.05  E-value: 1.18e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 980952224  409 TWVQCDACLKWRKLPDGID--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 5.66e-17

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: 78.14  E-value: 5.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   29 PFSAVAELIDNAYDPDVNAKQIWIDKTVISDHIClTFTDNGNGMTADKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGS 108
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKNRGGGTEI-VIEDDGHGMSPEELINALRLATSAKEAKRGSTDLGRYGIGLKLAS 79

                          90       100
                  ....*....|....*....|....*...
gi 980952224  109 MRLGKDAMVFTKNGETMSVGFLSQTYLE 136
Cdd:pfam13589  80 LSLGAKLTVTSKKEGKSSTLTLDRDKIS 107
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
698-910 2.53e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 698 QLQELRSELLVVTQERDDYKR---QCQMFTDQIQVLQQRLLEMNDKCVKKEKCHQ-----STETDAVFLLDSVNGQAESL 769
Cdd:COG4717   72 ELKELEEELKEAEEKEEEYAElqeELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEEL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 770 DHLGSQYQQALQEIERLKRQCSALQQVKSECSQASCTESKSEVDEMAVQLDDVFRQldkctieRDQYKNEVQLLEIEKSH 849
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------LAELEEELEEAQEELEE 224

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 980952224 850 IHSQCEELQTEVEQLKSTGQQAAADGSTASNAEepVSYVDGESLKLRSLRVNVGQLLAMIV 910
Cdd:COG4717  225 LEEELEQLENELEAAALEERLKEARLLLLIAAA--LLALLGLGGSLLSLILTIAGVLFLVL 283
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 673-939 4.52e-06

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: 50.89  E-value: 4.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   673 ATLSCVGTEAK-VQETSAESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLqqrLLEMNdkcvKKEKCHQST 751
Cdd:pfam15921  324 STVSQLRSELReAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL---LADLH----KREKELSLE 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   752 ETDAVFLLDSVNGQAESLDHLGSQYQQALQEIERLKrqcSALQQVKSECS-----QASCTESKSE----VDEMAVQLDDV 822
Cdd:pfam15921  397 KEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLE---ALLKAMKSECQgqmerQMAAIQGKNEslekVSSLTAQLEST 473

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   823 FRQLDKCTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEqlkstgqqaaadgstASNAE--EPVSYVDgesLKLRSLR- 899
Cdd:pfam15921  474 KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIE---------------ATNAEitKLRSRVD---LKLQELQh 535

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 980952224   900 -VNVGQLLAMIVPDLDLQQVNY-DVDVVDEILGQVVEQMSEI 939
Cdd:pfam15921  536 lKNEGDHLRNVQTECEALKLQMaEKDKVIEILRQQIENMTQL 577
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 32-100 1.47e-05

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 44.95  E-value: 1.47e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 980952224    32 AVAELIDNAYDPDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKMLSFGFS--DKVTMNGHVPVGLY 100
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRtdKRSRKIGGTGLGLS 79
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 680-900 1.07e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   680 TEAKVQETSAESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLL-----EMNDKCVKKEKCHQSTETd 754
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEA- 812

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   755 avfLLDSVNGQAESLDHLGSQYQQALQEIERLKRQCSAlqQVKSEC-----SQASCTESKSEVDEMAVQLDDVFRQLDKC 829
Cdd:TIGR02169  813 ---RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE--QIKSIEkeienLNGKKEELEEELEELEAALRDLESRLGDL 887

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 980952224   830 TIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKST-----GQQAAADGSTASNAEEPVSYVDGESLKLRSLRV 900
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKlealeEELSEIEDPKGEDEEIPEEELSLEDVQAELQRV 963
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 31-88 1.35e-03

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 42.14  E-value: 1.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 980952224  31 SAVAELIDNAYD----PDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKMLSFGFSDK 88
Cdd:COG3290  284 TILGNLLDNAIEavekLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTK 345
mukB PRK04863
chromosome partition protein MukB;
726-881 1.50e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  726 QIQVLQQRLLEMNDKCVKKEKCHQSTETD---AVFLLDSVN---GQAESLDhlgsQYQQALQEI-ERLKRQ--CSALQQV 796
Cdd:PRK04863  301 QLAAEQYRLVEMARELAELNEAESDLEQDyqaASDHLNLVQtalRQQEKIE----RYQADLEELeERLEEQneVVEEADE 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  797 KSECSQASCTESKSEVDEMAVQLDDVFRQLDKCTIERDQYKNEVQLLEieksHIHSQCEELQTEVEQLKSTGQQAAADGS 876
Cdd:PRK04863  377 QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----RAKQLCGLPDLTADNAEDWLEEFQAKEQ 452


                  ....*
gi 980952224  877 TASNA 881
Cdd:PRK04863  453 EATEE 457
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 698-721 4.96e-03

Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269866  Cd Length: 70  Bit Score: 36.49  E-value: 4.96e-03
                         10        20
                 ....*....|....*....|....
gi 980952224 698 QLQELRSELLVVTQERDDYKRQCQ 721
Cdd:cd14718   44 QVEQLKQEVSRLARERDAYKEKYE 67
 
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 2.36e-69

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: 226.65  E-value: 2.36e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  249 YSLRAYCSILYLK--PRMQIIIRGQKVKTQLVSKSLAYIERDVYRPKFLTR---TVRITFGF--NCRNKDHYGIMMYHKN 321
Cdd:pfam17942   1 YSLRAYASILYLRlpPNFQIILRGKKVEHHNIADDLKYPEKITYKPQVGGGkevVVITTIGFlkEAPHINVHGFNVYHKN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 980952224  322 RLIKAYEKVGCQlkANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTILALGEKLNDYW 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 3.06e-64

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: 211.88  E-value: 3.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  18 FLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVIS-DHICLTFTDNGNGMTADKLHKMLSFGFSDKVTMNgHVP 96
Cdd:cd16931    1 FLHSNSTTHSWPFGAVAELVDNARDADATRLDIFIDDINLLrGGFMLSFLDDGNGMTPEEAHHMISFGFSDKRSDD-HDH 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 980952224  97 VGLYGNGFKSGSMRLGKDAMVFTKNGETMSVGFLSQTYL 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 1.18e-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: 80.05  E-value: 1.18e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 980952224  409 TWVQCDACLKWRKLPDGID--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 5.66e-17

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: 78.14  E-value: 5.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   29 PFSAVAELIDNAYDPDVNAKQIWIDKTVISDHIClTFTDNGNGMTADKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGS 108
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKNRGGGTEI-VIEDDGHGMSPEELINALRLATSAKEAKRGSTDLGRYGIGLKLAS 79

                          90       100
                  ....*....|....*....|....*...
gi 980952224  109 MRLGKDAMVFTKNGETMSVGFLSQTYLE 136
Cdd:pfam13589  80 LSLGAKLTVTSKKEGKSSTLTLDRDKIS 107
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
 30-100 1.37e-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: 1.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 980952224  30 FSAVAELIDNAYDPDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKML-SFGFSDKVTMNGHVPVGLY 100
Cdd:cd00075    2 EQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFeRFYRGDKSREGGGTGLGLA 73
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
698-910 2.53e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 698 QLQELRSELLVVTQERDDYKR---QCQMFTDQIQVLQQRLLEMNDKCVKKEKCHQ-----STETDAVFLLDSVNGQAESL 769
Cdd:COG4717   72 ELKELEEELKEAEEKEEEYAElqeELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEEL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 770 DHLGSQYQQALQEIERLKRQCSALQQVKSECSQASCTESKSEVDEMAVQLDDVFRQldkctieRDQYKNEVQLLEIEKSH 849
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------LAELEEELEEAQEELEE 224

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 980952224 850 IHSQCEELQTEVEQLKSTGQQAAADGSTASNAEepVSYVDGESLKLRSLRVNVGQLLAMIV 910
Cdd:COG4717  225 LEEELEQLENELEAAALEERLKEARLLLLIAAA--LLALLGLGGSLLSLILTIAGVLFLVL 283
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 673-939 4.52e-06

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: 50.89  E-value: 4.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   673 ATLSCVGTEAK-VQETSAESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLqqrLLEMNdkcvKKEKCHQST 751
Cdd:pfam15921  324 STVSQLRSELReAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL---LADLH----KREKELSLE 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   752 ETDAVFLLDSVNGQAESLDHLGSQYQQALQEIERLKrqcSALQQVKSECS-----QASCTESKSE----VDEMAVQLDDV 822
Cdd:pfam15921  397 KEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLE---ALLKAMKSECQgqmerQMAAIQGKNEslekVSSLTAQLEST 473

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   823 FRQLDKCTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEqlkstgqqaaadgstASNAE--EPVSYVDgesLKLRSLR- 899
Cdd:pfam15921  474 KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIE---------------ATNAEitKLRSRVD---LKLQELQh 535

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 980952224   900 -VNVGQLLAMIVPDLDLQQVNY-DVDVVDEILGQVVEQMSEI 939
Cdd:pfam15921  536 lKNEGDHLRNVQTECEALKLQMaEKDKVIEILRQQIENMTQL 577
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 32-100 1.47e-05

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 44.95  E-value: 1.47e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 980952224    32 AVAELIDNAYDPDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKMLSFGFS--DKVTMNGHVPVGLY 100
Cdd:smart00387   9 VLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRtdKRSRKIGGTGLGLS 79
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 680-892 1.60e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 680 TEAKVQETSAEsVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDKcVKK------EKCHQSTET 753
Cdd:COG3883   28 LQAELEAAQAE-LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-LGEraralyRSGGSVSYL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 754 DAVFLLDSVN---GQAESLDHLGSQYQQALQEIERLKRQcsaLQQVKSECSQAsctesKSEVDEMAVQLDDVFRQLDKct 830
Cdd:COG3883  106 DVLLGSESFSdflDRLSALSKIADADADLLEELKADKAE---LEAKKAELEAK-----LAELEALKAELEAAKAELEA-- 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 980952224 831 iERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEEPVSYVDGES 892
Cdd:COG3883  176 -QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
751-874 2.66e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 751 TETDAVFLLDSVNGQAESLDHLGSQYQQALQEIERLKRQcsaLQQVKSECSQAsctesKSEVDEMAVQLDDVFRQLDKCT 830
Cdd:COG4372   22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREE---LEQLEEELEQA-----RSELEQLEEELEELNEQLQAAQ 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 980952224 831 IERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAAD 874
Cdd:COG4372   94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 32-100 8.94e-05

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: 42.74  E-value: 8.94e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 980952224   32 AVAELIDNAYDPDVNAKQIWIdKTVISDHICLTFTDNGNGMTADKLHKMLSFGFSDKVTMNGHVPVGLY 100
Cdd:pfam02518   9 VLSNLLDNALKHAAKAGEITV-TLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGGGTGLGLS 76
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 680-900 1.07e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   680 TEAKVQETSAESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLL-----EMNDKCVKKEKCHQSTETd 754
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEA- 812

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   755 avfLLDSVNGQAESLDHLGSQYQQALQEIERLKRQCSAlqQVKSEC-----SQASCTESKSEVDEMAVQLDDVFRQLDKC 829
Cdd:TIGR02169  813 ---RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE--QIKSIEkeienLNGKKEELEEELEELEAALRDLESRLGDL 887

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 980952224   830 TIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKST-----GQQAAADGSTASNAEEPVSYVDGESLKLRSLRV 900
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKlealeEELSEIEDPKGEDEEIPEEELSLEDVQAELQRV 963
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 696-860 1.57e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   696 SHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDkcvkkekchqstetdavfLLDSVNgqaESLDHLGSQ 775
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ------------------LLEELN---KKIKDLGEE 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   776 YQQALQ--------EIERLKRQCSALQQvKSECSQASCTESKSEVDEMAVQLDDVFRQLDKCTIERDQYKNEVQLLEIEK 847
Cdd:TIGR02169  288 EQLRVKekigeleaEIASLERSIAEKER-ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366

                          170
                   ....*....|...
gi 980952224   848 SHIHSQCEELQTE 860
Cdd:TIGR02169  367 EDLRAELEEVDKE 379
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
724-873 1.67e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  724 TDQIQVLQQRLLEMNDKCVKKEKchQSTETDAvfLLDSVNGQAESLDHLgSQYQQALQEIERLKRQCSALQQVKSECSQA 803
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEE--RLEALEA--ELDALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLDAS 683

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  804 ScteskSEVDEMAVQLDDVFRQLDKCTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAA 873
Cdd:COG4913   684 S-----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 680-886 2.30e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 680 TEAKVQETSAEsVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDKCVKKEK---------CHQS 750
Cdd:COG4942   39 LEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellralYRLG 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 751 TETDAVFLL--DSVNGQAESLDHLGSQYQQALQEIERLKRQCSALQQVKsecsqascTESKSEVDEMAVQLDDVFRQLDK 828
Cdd:COG4942  118 RQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR--------AELEAERAELEALLAELEEERAA 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 980952224 829 CTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEEPVS 886
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 697-889 3.54e-04

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: 44.29  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  697 HQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMndkcvkkekchQSTETDAVFLLDSVNGQAESLDHLG--- 773
Cdd:pfam05622  66 KQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEEL-----------TSLAEEAQALKDEMDILRESSDKVKkle 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  774 ---SQYQQALQEIERLKRQCSALQ-----------QVKSECSQASCTES-----KSEVDEMAVQLDDVFRQLDKCTIERD 834
Cdd:pfam05622 135 atvETYKKKLEDLGDLRRQVKLLEernaeymqrtlQLEEELKKANALRGqletyKRQVQELHGKLSEESKKADKLEFEYK 214

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 980952224  835 QYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEEPVSYVD 889
Cdd:pfam05622 215 KLEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGD 269
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
657-874 3.73e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 657 KKEESMEEDMGVRNGTATLscVGTEAKVQETSAESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLE 736
Cdd:COG4372    7 KVGKARLSLFGLRPKTGIL--IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 737 MNDKCVKKEKCHQSTETDavflLDSVNGQAESLDhlgSQYQQALQEIERLKRQCSALQQVKSecsqasctESKSEVDEMA 816
Cdd:COG4372   85 LNEQLQAAQAELAQAQEE----LESLQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIA--------ELQSEIAERE 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 980952224 817 VQLDDVFRQLDKctIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAAD 874
Cdd:COG4372  150 EELKELEEQLES--LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEA 205
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 681-883 5.12e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 5.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   681 EAKVQETSAEsVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDKcvKKEKCHQSTETDAvflld 760
Cdd:TIGR02168  259 TAELQELEEK-LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ--LEELEAQLEELES----- 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   761 SVNGQAESLDHLGSQYQQALQEIERLKRQCSALQQVKSecsqasctESKSEVDEMAVQLDDVFRQLDKCTIERDQYKNEV 840
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELE--------ELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 980952224   841 QLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEE 883
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 681-873 5.63e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   681 EAKVQETSaESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDKCVKKEKCHQSTETDAVFLLD 760
Cdd:TIGR02168  301 EQQKQILR-ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   761 SVNGQA-------ESLDHLGSQYQQALQEIERLKRQCSALQQVKSECS-----------QASCTESKSEVDEMAVQLDDV 822
Cdd:TIGR02168  380 QLETLRskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeaelkelQAELEELEEELEELQEELERL 459

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 980952224   823 FRQLDKCTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAA 873
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 31-88 1.35e-03

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 42.14  E-value: 1.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 980952224  31 SAVAELIDNAYD----PDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKMLSFGFSDK 88
Cdd:COG3290  284 TILGNLLDNAIEavekLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTK 345
mukB PRK04863
chromosome partition protein MukB;
726-881 1.50e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  726 QIQVLQQRLLEMNDKCVKKEKCHQSTETD---AVFLLDSVN---GQAESLDhlgsQYQQALQEI-ERLKRQ--CSALQQV 796
Cdd:PRK04863  301 QLAAEQYRLVEMARELAELNEAESDLEQDyqaASDHLNLVQtalRQQEKIE----RYQADLEELeERLEEQneVVEEADE 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224  797 KSECSQASCTESKSEVDEMAVQLDDVFRQLDKCTIERDQYKNEVQLLEieksHIHSQCEELQTEVEQLKSTGQQAAADGS 876
Cdd:PRK04863  377 QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----RAKQLCGLPDLTADNAEDWLEEFQAKEQ 452


                  ....*
gi 980952224  877 TASNA 881
Cdd:PRK04863  453 EATEE 457
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 681-883 1.77e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 681 EAKVQETSAEsVDATSHQLQELRSELLVVTQErddykrqcqmftdqIQVLQQRLLEMNDKCVKKEKCHQSTETDAVFLLD 760
Cdd:COG1196  252 EAELEELEAE-LAELEAELEELRLELEELELE--------------LEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 761 SVNGQAESLDHLGSQYQQALQEIERLKRQCSALQQVKSEcSQASCTESKSEVDEMAVQLDDVFRQLDKCTIERDQYKNEV 840
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 980952224 841 QLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEE 883
Cdd:COG1196  396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 36-80 2.08e-03

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 41.32  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 980952224  36 LIDNAYD--PDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKM 80
Cdd:COG4191  264 LLINAIDamEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERI 310
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 697-870 4.00e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   697 HQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNdKCVKKEKCHQSTETDAVFLLDSVNGQAESLD-HLGSQ 775
Cdd:TIGR00618  701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN-QSLKELMHQARTVLKARTEAHFNNNEEVTAAlQTGAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224   776 YQQALQEIERLKRQCSALQQVKSECSQASCTESKSEVDEMAVQlddvfrqldkCTIERDQYKNEVQLLEIEKSHIHsqce 855
Cdd:TIGR00618  780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ----------CETLVQEEEQFLSRLEEKSATLG---- 845

                          170
                   ....*....|....*
gi 980952224   856 ELQTEVEQLKSTGQQ 870
Cdd:TIGR00618  846 EITHQLLKYEECSKQ 860
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 698-721 4.96e-03

Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269866  Cd Length: 70  Bit Score: 36.49  E-value: 4.96e-03
                         10        20
                 ....*....|....*....|....
gi 980952224 698 QLQELRSELLVVTQERDDYKRQCQ 721
Cdd:cd14718   44 QVEQLKQEVSRLARERDAYKEKYE 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
680-940 6.22e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 680 TEAKVQETSAEsVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDKCVKKEKCHQSTETDAVFLL 759
Cdd:COG4372   50 LREELEQAREE-LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 760 DSVNGQAESLDHLGSQYQQALQEIERLKRQCSALQQ----VKSECSQASCTESKSEVDEM-------AVQLDDVFRQLDK 828
Cdd:COG4372  129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAEQALDELlkeanrnAEKEEELAEAEKL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 980952224 829 CTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEEPVSYVDGESLKLRSLRVNVGQLLAM 908
Cdd:COG4372  209 IESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288

                        250       260       270
                 ....*....|....*....|....*....|..
gi 980952224 909 IVPDLDLQQVNYDVDVVDEILGQVVEQMSEIS 940
Cdd:COG4372  289 EEAALELKLLALLLNLAALSLIGALEDALLAA 320
 
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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