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Conserved domains on  [gi|160333105|ref|NP_001103791|]
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B-cell differentiation antigen CD72 isoform 3 [Mus musculus]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10636995)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

CATH:  3.10.100.10
Gene Ontology:  GO:0030246|GO:0120153
PubMed:  16336259|10508765
SCOP:  4002453

Graphical summary

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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 ...
 208-324 7.77e-14

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: 67.24  E-value: 7.77e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   208 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEP--SKYYYEYLSDAPQVSLPS-GLEELLDRSKSYWIQMS 284
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEaeNDFVASLLKNSGSSDYYWiGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 160333105   285 -----KKWRQDSDSQSR-HCVRIKTYYQKWERTisKCAELHPCICE 324
Cdd:smart00034  81 gpvsySNWAPGEPNNSSgDCVVLSTSGGKWNDV--SCTSKLPFVCE 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
102-189 1.64e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 102 QEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEER 181
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109


                 ....*...
gi 160333105 182 RRDLDQRL 189
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 ...
 208-324 7.77e-14

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: 67.24  E-value: 7.77e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   208 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEP--SKYYYEYLSDAPQVSLPS-GLEELLDRSKSYWIQMS 284
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEaeNDFVASLLKNSGSSDYYWiGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 160333105   285 -----KKWRQDSDSQSR-HCVRIKTYYQKWERTisKCAELHPCICE 324
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); ...
 208-324 1.89e-11

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: 60.42  E-value: 1.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 208 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDepSKyyyeylsdapqvslpsglEEL-----LDRSKSYWI- 281
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKID--DE------------------EELeflqsQIGSSSYWIg 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 160333105 282 ----QMSKKWRQDSDS------------QSRHCVriktYYQKWERTISKCAELHPCICE 324
Cdd:cd03593   61 lsreKSEKPWKWIDGSplnnlfnirgstKSGNCA----YLSSTGIYSEDCSTKKRWICE 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
102-189 1.64e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 102 QEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEER 181
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109


                 ....*...
gi 160333105 182 RRDLDQRL 189
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 ...
 98-206 1.39e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.63  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105    98 SRQFQEGT-RIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLK 176
Cdd:pfam01576  202 GRQELEKAkRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLE 281

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 160333105   177 TE-------EERRRDLDQRLtstrETLRRFFSDSSDT 206
Cdd:pfam01576  282 SEraarnkaEKQRRDLGEEL----EALKTELEDTLDT 314
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 114-189 6.12e-04

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: 38.32  E-value: 6.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160333105 114 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRL 189
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERW 76
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-197 1.12e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   109 EATNSSLQQQ------LREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERR 182
Cdd:TIGR02168  666 AKTNSSILERrreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90
                   ....*....|....*
gi 160333105   183 RDLDQRLTSTRETLR 197
Cdd:TIGR02168  746 EERIAQLSKELTELE 760
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 228-324 1.18e-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: 37.84  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  228 SLEESQKYCTSLSSKLAAFdePSKYYYEYLSDapqvslpsgleELLDRSKSYWI-----QMSKKWR-------------- 288
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSI--NSAEELDFLSS-----------TLKKSNKYFWIgltdrKNEGTWKwvdgspvnytnwap 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 160333105  289 -QDSDSQSRHCVRIKTYYQKWErtISKCAELHPCICE 324
Cdd:pfam00059  70 ePNNNGENEDCVELSSSSGKWN--DENCNSKNPFVCE 104
mukB PRK04863
chromosome partition protein MukB;
110-197 1.25e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  110 ATNSSLQQQLREKisqLGQKEVELQKARKELISSQDTLQE--------------KQRTHEDAEQQLQ-----ACQ--AER 168
Cdd:PRK04863  981 AKNSDLNEKLRQR---LEQAEQERTRAREQLRQAQAQLAQynqvlaslkssydaKRQMLQELKQELQdlgvpADSgaEER 1057

                          90       100       110
                  ....*....|....*....|....*....|....
gi 160333105  169 AKTK-----ENLKTEEERRRDLDQRLTSTRETLR 197
Cdd:PRK04863 1058 ARARrdelhARLSANRSRRNQLEKQLTFCEAEMD 1091
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 208-323 2.20e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 38.31  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 208 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEPSKyyYEYLSDAPQVslpsgleelldrsKSYWIQMSKKW 287
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKE--VLFVSRYKGG-------------QDLWIGIEKKK 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 160333105 288 RQDSDSQSRHCVRIK------TYYQKWERTISKCAELHPCIC 323
Cdd:PHA03097 111 GDDDDREVLDKVVKPpksgkcAYLKDKTIISSNCNATKGWIC 152
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 208-324 7.77e-14

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: 67.24  E-value: 7.77e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   208 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEP--SKYYYEYLSDAPQVSLPS-GLEELLDRSKSYWIQMS 284
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEaeNDFVASLLKNSGSSDYYWiGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 160333105   285 -----KKWRQDSDSQSR-HCVRIKTYYQKWERTisKCAELHPCICE 324
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); ...
 208-324 1.89e-11

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: 60.42  E-value: 1.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 208 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDepSKyyyeylsdapqvslpsglEEL-----LDRSKSYWI- 281
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKID--DE------------------EELeflqsQIGSSSYWIg 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 160333105 282 ----QMSKKWRQDSDS------------QSRHCVriktYYQKWERTISKCAELHPCICE 324
Cdd:cd03593   61 lsreKSEKPWKWIDGSplnnlfnirgstKSGNCA----YLSSTGIYSEDCSTKKRWICE 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
102-189 1.64e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 102 QEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEER 181
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109


                 ....*...
gi 160333105 182 RRDLDQRL 189
Cdd:COG4372  110 AEELQEEL 117
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 109-198 1.95e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 109 EATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 188
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                         90
                 ....*....|
gi 160333105 189 LTSTRETLRR 198
Cdd:COG1196  360 LAEAEEALLE 369
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 118-189 4.05e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 4.05e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160333105 118 QLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKT----EEERRRDLDQRL 189
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaeaeIEERREELGERA 92
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 218-324 9.96e-06

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: 44.15  E-value: 9.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 218 RCFYISHTLGSLEESQKYCTSLSSKLAAFDEPSKYYY--EYLSDAPQVSLPSGLEELLDRSKSYWIQMSK-----KWR-- 288
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFlaSLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPlvdytNWApg 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 160333105 289 QDSDSQSRHCVRIKTYYQ-KWERTisKCAELHPCICE 324
Cdd:cd00037   81 EPNPGGSEDCVVLSSSSDgKWNDV--SCSSKLPFICE 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 109-198 1.00e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 109 EATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 188
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324

                         90
                 ....*....|
gi 160333105 189 LTSTRETLRR 198
Cdd:COG1196  325 LAELEEELEE 334
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 113-199 1.18e-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: 46.68  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 113 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 192
Cdd:COG4942  142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221


                 ....*..
gi 160333105 193 RETLRRF 199
Cdd:COG4942  222 AEELEAL 228
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 93-198 1.28e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  93 RYLQVSRQFQEgTRIWEATNS--SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAK 170
Cdd:COG1196  214 RYRELKEELKE-LEAELLLLKlrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                         90       100
                 ....*....|....*....|....*...
gi 160333105 171 TKENLKTEEERRRDLDQRLTSTRETLRR 198
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEE 320
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 113-198 1.64e-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: 46.30  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 113 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 192
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102


                 ....*.
gi 160333105 193 RETLRR 198
Cdd:COG4942  103 KEELAE 108
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 109-198 2.17e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 109 EATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 188
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                         90
                 ....*....|
gi 160333105 189 LTSTRETLRR 198
Cdd:COG1196  332 LEELEEELEE 341
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
113-198 2.27e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 113 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 192
Cdd:COG4372   83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162


                 ....*.
gi 160333105 193 RETLRR 198
Cdd:COG4372  163 QEELAA 168
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
113-198 2.37e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 113 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 192
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106


                 ....*.
gi 160333105 193 RETLRR 198
Cdd:COG4372  107 QEEAEE 112
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 208-281 2.87e-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: 43.06  E-value: 2.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160333105 208 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDepskyyyeylSDAPQvslpSGLEELLDRSKSYWI 281
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIIN----------SQEEQ----EFISKILSGNRSYWI 60
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
109-198 9.27e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 9.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 109 EATNSSLQQ---QLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDL 185
Cdd:COG4372   62 EQLEEELEQarsELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141

                         90
                 ....*....|...
gi 160333105 186 DQRLTSTRETLRR 198
Cdd:COG4372  142 QSEIAEREEELKE 154
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 114-180 1.10e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 1.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160333105 114 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEE 180
Cdd:COG3883  140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
117-199 1.23e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  117 QQLREKISqlgqkevELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETL 196
Cdd:COG4913   664 ASAEREIA-------ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736


                  ...
gi 160333105  197 RRF 199
Cdd:COG4913   737 EAA 739
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 208-324 1.28e-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: 41.20  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 208 CPCGWIPYQERCFYISHTLGSLEESQKYCTSL--SSKLAAFDEP------SKYYYEYLSDAPQVSLpsGLEELLDRSKSY 279
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPaeaaaiASLISSYQKAYQPVWI--GLHDPQQSRGWE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 160333105 280 WIQMSKK----WRQDSDSQSR-HCVRI--KTYYQKWERtiSKCAELHPCICE 324
Cdd:cd03594   79 WSDGSKLdyrsWDRNPPYARGgYCAELsrSTGFLKWND--ANCEERNPFICK 128
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 98-206 1.39e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.63  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105    98 SRQFQEGT-RIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLK 176
Cdd:pfam01576  202 GRQELEKAkRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLE 281

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 160333105   177 TE-------EERRRDLDQRLtstrETLRRFFSDSSDT 206
Cdd:pfam01576  282 SEraarnkaEKQRRDLGEEL----EALKTELEDTLDT 314
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 92-204 1.42e-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: 43.21  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  92 VRYLQVSRQFQEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKT 171
Cdd:COG4942  135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214

                         90       100       110
                 ....*....|....*....|....*....|...
gi 160333105 172 KENLKTEEERRRDLDQRLTSTRETLRRFFSDSS 204
Cdd:COG4942  215 LAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 113-198 2.24e-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: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 113 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 192
Cdd:COG3883  125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204


                 ....*.
gi 160333105 193 RETLRR 198
Cdd:COG3883  205 LAAAEA 210
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
115-188 2.60e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 2.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160333105 115 LQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 188
Cdd:COG4372   57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 124-198 3.85e-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: 3.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160333105 124 SQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETLRR 198
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
95-198 4.72e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   95 LQVSRQFQEGTRIWEA-----TNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTH-----EDAEQQLQAC 164
Cdd:COG4913   271 LAELEYLRAALRLWFAqrrleLLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERL 350

                          90       100       110
                  ....*....|....*....|....*....|....
gi 160333105  165 QAERAKTKENLKTEEERRRDLDQRLTSTRETLRR 198
Cdd:COG4913   351 ERELEERERRRARLEALLAALGLPLPASAEEFAA 384
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 114-189 6.12e-04

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: 38.32  E-value: 6.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160333105 114 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRL 189
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERW 76
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-197 1.12e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   109 EATNSSLQQQ------LREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERR 182
Cdd:TIGR02168  666 AKTNSSILERrreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90
                   ....*....|....*
gi 160333105   183 RDLDQRLTSTRETLR 197
Cdd:TIGR02168  746 EERIAQLSKELTELE 760
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
109-196 1.13e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 109 EATNSSLQQ------QLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERR 182
Cdd:COG4372   83 EELNEQLQAaqaelaQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162

                         90
                 ....*....|....
gi 160333105 183 RDLDQRLTSTRETL 196
Cdd:COG4372  163 QEELAALEQELQAL 176
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 228-324 1.18e-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: 37.84  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  228 SLEESQKYCTSLSSKLAAFdePSKYYYEYLSDapqvslpsgleELLDRSKSYWI-----QMSKKWR-------------- 288
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSI--NSAEELDFLSS-----------TLKKSNKYFWIgltdrKNEGTWKwvdgspvnytnwap 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 160333105  289 -QDSDSQSRHCVRIKTYYQKWErtISKCAELHPCICE 324
Cdd:pfam00059  70 ePNNNGENEDCVELSSSSGKWN--DENCNSKNPFVCE 104
mukB PRK04863
chromosome partition protein MukB;
110-197 1.25e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  110 ATNSSLQQQLREKisqLGQKEVELQKARKELISSQDTLQE--------------KQRTHEDAEQQLQ-----ACQ--AER 168
Cdd:PRK04863  981 AKNSDLNEKLRQR---LEQAEQERTRAREQLRQAQAQLAQynqvlaslkssydaKRQMLQELKQELQdlgvpADSgaEER 1057

                          90       100       110
                  ....*....|....*....|....*....|....
gi 160333105  169 AKTK-----ENLKTEEERRRDLDQRLTSTRETLR 197
Cdd:PRK04863 1058 ARARrdelhARLSANRSRRNQLEKQLTFCEAEMD 1091
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-194 1.33e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   115 LQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRE 194
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
117-198 1.39e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 117 QQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQ--AERAKTKENLKTEEERRRDLDQRLTSTRE 194
Cdd:COG4717   81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160


                 ....
gi 160333105 195 TLRR 198
Cdd:COG4717  161 LEEE 164
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 95-191 1.66e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.11  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   95 LQVSRQFQEGTRIWEATNSSLQQQLREKISQLGQK-----------EVELQKARKELISSQDTLQEKQRTHEDAEQQLQA 163
Cdd:pfam05557  78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNElselrrqiqraELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157

                          90       100
                  ....*....|....*....|....*...
gi 160333105  164 CQaerAKTKEnLKTEEERRRDLDQRLTS 191
Cdd:pfam05557 158 LE---KQQSS-LAEAEQRIKELEFEIQS 181
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
93-199 1.85e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  93 RYLQVSRQFQEG-TRIWEATNSSLQQQLREKISQLGQKEVEL-----------QKARKELISSQDTL-QEKQRTHEDAEQ 159
Cdd:COG3206  241 RLAALRAQLGSGpDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpdvIALRAQIAALRAQLqQEAQRILASLEA 320

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 160333105 160 QLQACQAERAKTKENLKTEEERR----------RDLDQRLTSTRETLRRF 199
Cdd:COG3206  321 ELEALQAREASLQAQLAQLEARLaelpeleaelRRLEREVEVARELYESL 370
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 115-194 1.88e-03

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 37.56  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  115 LQQQLREKISQLGQKEVELQK---ARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENL----KTEEERRRDLDQ 187
Cdd:pfam18595  31 VEKDLRSCIKLLEEIEAELAKleeAKKKLKELRDALEEKEIELRELERREERLQRQLENAQEKLerlrEQAEEKREAAQA 110


                  ....*..
gi 160333105  188 RLTSTRE 194
Cdd:pfam18595 111 RLEELRE 117
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
117-198 2.12e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 117 QQLREKISQLGQKEVELQKARKELISSQDTLqEKQRTHEDAEQQLQACQAERAKTK---ENLKTEEERRRDLDQRLTSTR 193
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPerlEELEERLEELRELEEELEELE 169


                 ....*
gi 160333105 194 ETLRR 198
Cdd:COG4717  170 AELAE 174
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 208-323 2.20e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 38.31  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 208 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEPSKyyYEYLSDAPQVslpsgleelldrsKSYWIQMSKKW 287
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKE--VLFVSRYKGG-------------QDLWIGIEKKK 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 160333105 288 RQDSDSQSRHCVRIK------TYYQKWERTISKCAELHPCIC 323
Cdd:PHA03097 111 GDDDDREVLDKVVKPpksgkcAYLKDKTIISSNCNATKGWIC 152
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 117-193 2.49e-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: 38.75  E-value: 2.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160333105 117 QQLREKISQLGQKEVELQKARKELissQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTR 193
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAEL---EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 110-198 2.80e-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: 39.36  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 110 ATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRL 189
Cdd:COG4942   13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92


                 ....*....
gi 160333105 190 TSTRETLRR 198
Cdd:COG4942   93 AELRAELEA 101
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-198 2.82e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  109 EATNSSLQQqLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTE---------- 178
Cdd:COG4913   681 DASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlleerfaaal 759

                          90       100
                  ....*....|....*....|.
gi 160333105  179 -EERRRDLDQRLTSTRETLRR 198
Cdd:COG4913   760 gDAVERELRENLEERIDALRA 780
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 113-185 2.82e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 38.49  E-value: 2.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160333105 113 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTE-----EERRRDL 185
Cdd:cd07596  113 ADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEISERLKEElkrfhEERARDL 190
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
119-198 3.16e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  119 LREKISQLGQkEVELQKARKELISSQDTLQE--KQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETL 196
Cdd:COG4913   247 AREQIELLEP-IRELAERYAAARERLAELEYlrAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325


                  ..
gi 160333105  197 RR 198
Cdd:COG4913   326 DE 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 116-187 3.64e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 3.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160333105 116 QQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQAcQAERAKtkeNLKTEEERRRDLDQ 187
Cdd:PRK12704  95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ-ELERIS---GLTAEEAKEILLEK 162
PRK12704 PRK12704
phosphodiesterase; Provisional
 117-198 3.94e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 117 QQLREKISQ-LGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLkteEERRRDLDQRLTSTRET 195
Cdd:PRK12704  67 HKLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL---EKKEEELEELIEEQLQE 143


                 ...
gi 160333105 196 LRR 198
Cdd:PRK12704 144 LER 146
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
96-193 4.71e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105  96 QVSRQFQEGTRIWEATNSSLQQ------QLREKISQLGQKEVELQKARKELISSQDTLQEKQrthEDAEQQLQACQAERA 169
Cdd:COG4372   84 ELNEQLQAAQAELAQAQEELESlqeeaeELQEELEELQKERQDLEQQRKQLEAQIAELQSEI---AEREEELKELEEQLE 160

                         90       100
                 ....*....|....*....|....
gi 160333105 170 KTKENLKTEEERRRDLDQRLTSTR 193
Cdd:COG4372  161 SLQEELAALEQELQALSEAEAEQA 184
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
115-194 4.92e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 4.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105 115 LQQQLREKISQLGQKEVELQKARKEL-ISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTR 193
Cdd:COG4717  161 LEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240


                 .
gi 160333105 194 E 194
Cdd:COG4717  241 L 241
PTZ00121 PTZ00121
MAEBL; Provisional
 92-183 5.30e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   92 VRYLQVSRQFQEGTRIWEATNSSLQQQLRE--KISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQlQACQAERA 169
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAvkKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ-AAIKAEEA 1277

                          90
                  ....*....|....
gi 160333105  170 KTKENLKTEEERRR 183
Cdd:PTZ00121 1278 RKADELKKAEEKKK 1291
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-199 6.45e-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: 38.50  E-value: 6.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   114 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTR 193
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907


                   ....*.
gi 160333105   194 ETLRRF 199
Cdd:TIGR02168  908 SKRSEL 913
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 99-198 9.79e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 36.45  E-value: 9.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333105   99 RQFQEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISS--------QDTLQEKQRTHEDAEQQLQACQAERAK 170
Cdd:pfam08614  10 NRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSleqllaqlREELAELYRSRGELAQRLVDLNEELQE 89

                          90       100
                  ....*....|....*....|....*...
gi 160333105  171 TKENLKTEEERRRDLDQRLTSTRETLRR 198
Cdd:pfam08614  90 LEKKLREDERRLAALEAERAQLEEKLKD 117
 
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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