NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568926002|ref|XP_006537644|]
View 

B-cell differentiation antigen CD72 isoform X6 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 127-243 1.94e-13

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 65.31  E-value: 1.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002   127 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEP--SKYYYEYLSDAPQVSLPS-GLEELLDRSKSYWIQMS 203
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEaeNDFVASLLKNSGSSDYYWiGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568926002   204 -----KKWRQDSDSQSR-HCVRIKTYYQKWERTisKCAELHPCICE 243
Cdd:smart00034  81 gpvsySNWAPGEPNNSSgDCVVLSTSGGKWNDV--SCTSKLPFVCE 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-108 8.45e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 8.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  21 QEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEER 100
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109


                 ....*...
gi 568926002 101 RRDLDQRL 108
Cdd:COG4372  110 AEELQEEL 117
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 127-243 1.94e-13

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 65.31  E-value: 1.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002   127 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEP--SKYYYEYLSDAPQVSLPS-GLEELLDRSKSYWIQMS 203
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEaeNDFVASLLKNSGSSDYYWiGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568926002   204 -----KKWRQDSDSQSR-HCVRIKTYYQKWERTisKCAELHPCICE 243
Cdd:smart00034  81 gpvsySNWAPGEPNNSSgDCVVLSTSGGKWNDV--SCTSKLPFVCE 124
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 127-243 2.43e-10

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 56.57  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002 127 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDepSKyyyeylsdapqvslpsglEEL-----LDRSKSYWI- 200
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKID--DE------------------EELeflqsQIGSSSYWIg 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568926002 201 ----QMSKKWRQDSDS------------QSRHCVriktYYQKWERTISKCAELHPCICE 243
Cdd:cd03593   61 lsreKSEKPWKWIDGSplnnlfnirgstKSGNCA----YLSSTGIYSEDCSTKKRWICE 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-108 8.45e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 8.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  21 QEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEER 100
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109


                 ....*...
gi 568926002 101 RRDLDQRL 108
Cdd:COG4372  110 AEELQEEL 117
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 17-125 1.74e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002    17 SRQFQEGT-RIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLK 95
Cdd:pfam01576  202 GRQELEKAkRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLE 281

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 568926002    96 TE-------EERRRDLDQRLtstrETLRRFFSDSSDT 125
Cdd:pfam01576  282 SEraarnkaEKQRRDLGEEL----EALKTELEDTLDT 314
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 37-116 2.22e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002    37 QLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETLR 116
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 33-108 2.65e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.00  E-value: 2.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568926002  33 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRL 108
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERW 76
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 147-243 2.82e-03

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 36.30  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  147 SLEESQKYCTSLSSKLAAFdePSKYYYEYLSDapqvslpsgleELLDRSKSYWI-----QMSKKWR-------------- 207
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSI--NSAEELDFLSS-----------TLKKSNKYFWIgltdrKNEGTWKwvdgspvnytnwap 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568926002  208 -QDSDSQSRHCVRIKTYYQKWErtISKCAELHPCICE 243
Cdd:pfam00059  70 ePNNNGENEDCVELSSSSGKWN--DENCNSKNPFVCE 104
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 127-242 3.11e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 37.15  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002 127 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEPSKyyYEYLSDAPQVslpsgleelldrsKSYWIQMSKKW 206
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKE--VLFVSRYKGG-------------QDLWIGIEKKK 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568926002 207 RQDSDSQSRHCVRIK------TYYQKWERTISKCAELHPCIC 242
Cdd:PHA03097 111 GDDDDREVLDKVVKPpksgkcAYLKDKTIISSNCNATKGWIC 152
mukB PRK04863
chromosome partition protein MukB;
29-116 3.60e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.40  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002   29 ATNSSLQQQLREKisqLGQKEVELQKARKELISSQDTLQE--------------KQRTHEDAEQQLQ-----ACQ--AER 87
Cdd:PRK04863  981 AKNSDLNEKLRQR---LEQAEQERTRAREQLRQAQAQLAQynqvlaslkssydaKRQMLQELKQELQdlgvpADSgaEER 1057

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568926002   88 AKTK-----ENLKTEEERRRDLDQRLTSTRETLR 116
Cdd:PRK04863 1058 ARARrdelhARLSANRSRRNQLEKQLTFCEAEMD 1091
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 127-243 1.94e-13

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 65.31  E-value: 1.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002   127 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEP--SKYYYEYLSDAPQVSLPS-GLEELLDRSKSYWIQMS 203
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEaeNDFVASLLKNSGSSDYYWiGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568926002   204 -----KKWRQDSDSQSR-HCVRIKTYYQKWERTisKCAELHPCICE 243
Cdd:smart00034  81 gpvsySNWAPGEPNNSSgDCVVLSTSGGKWNDV--SCTSKLPFVCE 124
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 127-243 2.43e-10

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 56.57  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002 127 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDepSKyyyeylsdapqvslpsglEEL-----LDRSKSYWI- 200
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKID--DE------------------EELeflqsQIGSSSYWIg 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568926002 201 ----QMSKKWRQDSDS------------QSRHCVriktYYQKWERTISKCAELHPCICE 243
Cdd:cd03593   61 lsreKSEKPWKWIDGSplnnlfnirgstKSGNCA----YLSSTGIYSEDCSTKKRWICE 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-108 8.45e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 8.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  21 QEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEER 100
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109


                 ....*...
gi 568926002 101 RRDLDQRL 108
Cdd:COG4372  110 AEELQEEL 117
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 28-117 2.92e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  28 EATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 107
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                         90
                 ....*....|
gi 568926002 108 LTSTRETLRR 117
Cdd:COG1196  360 LAEAEEALLE 369
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 37-108 6.01e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 6.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568926002  37 QLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKT----EEERRRDLDQRL 108
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaeaeIEERREELGERA 92
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 28-117 1.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  28 EATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 107
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324

                         90
                 ....*....|
gi 568926002 108 LTSTRETLRR 117
Cdd:COG1196  325 LAELEEELEE 334
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 32-118 1.83e-05

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: 45.14  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  32 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 111
Cdd:COG4942  142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221


                 ....*..
gi 568926002 112 RETLRRF 118
Cdd:COG4942  222 AEELEAL 228
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 34-117 2.17e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  34 LQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRE 113
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316


                 ....
gi 568926002 114 TLRR 117
Cdd:COG1196  317 RLEE 320
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 137-243 2.66e-05

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 42.61  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002 137 RCFYISHTLGSLEESQKYCTSLSSKLAAFDEPSKYYY--EYLSDAPQVSLPSGLEELLDRSKSYWIQMSKKWR------- 207
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFlaSLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDytnwapg 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568926002 208 QDSDSQSRHCVRIKTYYQ-KWERTisKCAELHPCICE 243
Cdd:cd00037   81 EPNPGGSEDCVVLSSSSDgKWNDV--SCSSKLPFICE 115
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 32-117 2.85e-05

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: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  32 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 111
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102


                 ....*.
gi 568926002 112 RETLRR 117
Cdd:COG4942  103 KEELAE 108
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 28-117 3.32e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  28 EATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 107
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                         90
                 ....*....|
gi 568926002 108 LTSTRETLRR 117
Cdd:COG1196  332 LEELEEELEE 341
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 127-200 8.28e-05

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 41.14  E-value: 8.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568926002 127 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDepskyyyeylSDAPQvslpSGLEELLDRSKSYWI 200
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIIN----------SQEEQ----EFISKILSGNRSYWI 60
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 33-99 1.39e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568926002  33 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEE 99
Cdd:COG3883  140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
51-118 1.92e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568926002   51 ELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETLRRF 118
Cdd:COG4913   672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 11-123 2.19e-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: 42.06  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  11 VRYLQVSRQFQEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKT 90
Cdd:COG4942  135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568926002  91 KENLKTEEERRRDLDQRLTSTRETLRRFFSDSS 123
Cdd:COG4942  215 LAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 32-117 2.84e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  32 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 111
Cdd:COG3883  125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204


                 ....*.
gi 568926002 112 RETLRR 117
Cdd:COG3883  205 LAAAEA 210
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 127-243 3.90e-04

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 39.28  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002 127 CPCGWIPYQERCFYISHTLGSLEESQKYCTSL--SSKLAAFDEP------SKYYYEYLSDAPQVSLpsGLEELLDRSKSY 198
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPaeaaaiASLISSYQKAYQPVWI--GLHDPQQSRGWE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568926002 199 WIQMSKK----WRQDSDSQSR-HCVRI--KTYYQKWERtiSKCAELHPCICE 243
Cdd:cd03594   79 WSDGSKLdyrsWDRNPPYARGgYCAELsrSTGFLKWND--ANCEERNPFICK 128
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
32-117 5.59e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 5.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  32 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 111
Cdd:COG4372   83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162


                 ....*.
gi 568926002 112 RETLRR 117
Cdd:COG4372  163 QEELAA 168
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
32-117 5.59e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 5.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  32 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 111
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106


                 ....*.
gi 568926002 112 RETLRR 117
Cdd:COG4372  107 QEEAEE 112
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 43-117 6.03e-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: 40.52  E-value: 6.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568926002  43 SQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETLRR 117
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
14-117 9.35e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 9.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002   14 LQVSRQFQEGTRIWEA-----TNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTH-----EDAEQQLQAC 83
Cdd:COG4913   271 LAELEYLRAALRLWFAqrrleLLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERL 350

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568926002   84 QAERAKTKENLKTEEERRRDLDQRLTSTRETLRR 117
Cdd:COG4913   351 ERELEERERRRARLEALLAALGLPLPASAEEFAA 384
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
12-118 1.48e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  12 RYLQVSRQFQEG-TRIWEATNSSLQQQLREKISQLGQKEVEL-----------QKARKELISSQDTL-QEKQRTHEDAEQ 78
Cdd:COG3206  241 RLAALRAQLGSGpDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpdvIALRAQIAALRAQLqQEAQRILASLEA 320

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568926002  79 QLQACQAERAKTKENLKTEEERR----------RDLDQRLTSTRETLRRF 118
Cdd:COG3206  321 ELEALQAREASLQAQLAQLEARLaelpeleaelRRLEREVEVARELYESL 370
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 17-125 1.74e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002    17 SRQFQEGT-RIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLK 95
Cdd:pfam01576  202 GRQELEKAkRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLE 281

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 568926002    96 TE-------EERRRDLDQRLtstrETLRRFFSDSSDT 125
Cdd:pfam01576  282 SEraarnkaEKQRRDLGEEL----EALKTELEDTLDT 314
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
32-117 1.96e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  32 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 111
Cdd:COG4372   69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148


                 ....*.
gi 568926002 112 RETLRR 117
Cdd:COG4372  149 EEELKE 154
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 37-116 2.22e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002    37 QLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETLR 116
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 34-113 2.49e-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: 38.88  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002    34 LQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRE 113
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 33-108 2.65e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.00  E-value: 2.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568926002  33 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRL 108
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERW 76
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 147-243 2.82e-03

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 36.30  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  147 SLEESQKYCTSLSSKLAAFdePSKYYYEYLSDapqvslpsgleELLDRSKSYWI-----QMSKKWR-------------- 207
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSI--NSAEELDFLSS-----------TLKKSNKYFWIgltdrKNEGTWKwvdgspvnytnwap 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568926002  208 -QDSDSQSRHCVRIKTYYQKWErtISKCAELHPCICE 243
Cdd:pfam00059  70 ePNNNGENEDCVELSSSSGKWN--DENCNSKNPFVCE 104
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 127-242 3.11e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 37.15  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002 127 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEPSKyyYEYLSDAPQVslpsgleelldrsKSYWIQMSKKW 206
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKE--VLFVSRYKGG-------------QDLWIGIEKKK 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568926002 207 RQDSDSQSRHCVRIK------TYYQKWERTISKCAELHPCIC 242
Cdd:PHA03097 111 GDDDDREVLDKVVKPpksgkcAYLKDKTIISSNCNATKGWIC 152
mukB PRK04863
chromosome partition protein MukB;
29-116 3.60e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.40  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002   29 ATNSSLQQQLREKisqLGQKEVELQKARKELISSQDTLQE--------------KQRTHEDAEQQLQ-----ACQ--AER 87
Cdd:PRK04863  981 AKNSDLNEKLRQR---LEQAEQERTRAREQLRQAQAQLAQynqvlaslkssydaKRQMLQELKQELQdlgvpADSgaEER 1057

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568926002   88 AKTK-----ENLKTEEERRRDLDQRLTSTRETLR 116
Cdd:PRK04863 1058 ARARrdelhARLSANRSRRNQLEKQLTFCEAEMD 1091
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 29-117 4.18e-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: 37.82  E-value: 4.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  29 ATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRL 108
Cdd:COG4942   13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92


                 ....*....
gi 568926002 109 TSTRETLRR 117
Cdd:COG4942   93 AELRAELEA 101
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
34-107 4.64e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 4.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568926002  34 LQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 107
Cdd:COG4372   57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
PRK12704 PRK12704
phosphodiesterase; Provisional
 35-106 4.94e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 4.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568926002  35 QQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQAcQAERAKtkeNLKTEEERRRDLDQ 106
Cdd:PRK12704  95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ-ELERIS---GLTAEEAKEILLEK 162
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
36-117 5.44e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.82  E-value: 5.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  36 QQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQ--AERAKTKENLKTEEERRRDLDQRLTSTRE 113
Cdd:COG4717   81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160


                 ....
gi 568926002 114 TLRR 117
Cdd:COG4717  161 LEEE 164
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-117 5.65e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.97  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002   38 LREKISQLGQkEVELQKARKELISSQDTLQE--KQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETL 115
Cdd:COG4913   247 AREQIELLEP-IRELAERYAAARERLAELEYlrAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325


                  ..
gi 568926002  116 RR 117
Cdd:COG4913   326 DE 327
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
28-117 5.76e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.97  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002   28 EATNSSLQQqLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTE---------- 97
Cdd:COG4913   681 DASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlleerfaaal 759

                          90       100
                  ....*....|....*....|.
gi 568926002   98 -EERRRDLDQRLTSTRETLRR 117
Cdd:COG4913   760 gDAVERELRENLEERIDALRA 780
PRK12704 PRK12704
phosphodiesterase; Provisional
 36-117 5.80e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 5.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926002  36 QQLREKISQ-LGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLkteEERRRDLDQRLTSTRET 114
Cdd:PRK12704  67 HKLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL---EKKEEELEELIEEQLQE 143


                 ...
gi 568926002 115 LRR 117
Cdd:PRK12704 144 LER 146
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 28-95 6.37e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 37.40  E-value: 6.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568926002   28 EATNSSLQQQLREKISQLGQ-KEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLK 95
Cdd:TIGR04320 288 QTAYAAAQAALATAQKELANaQAQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 36-112 8.23e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 36.83  E-value: 8.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568926002  36 QQLREKISQLGQKEVELQKARKELissQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTR 112
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAEL---EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH