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Conserved domains on  [gi|62543519|ref|NP_001015016|]
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B-cell differentiation antigen CD72 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT super family cl02432
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 230-296 1.49e-09

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.


The actual alignment was detected with superfamily member cd03590:

Pssm-ID: 470576 [Multi-domain]  Cd Length: 126  Bit Score: 55.39  E-value: 1.49e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62543519 230 CPSGWVQHEKRCFYISNTPRSLEESRKYCTSLSSKLAVLNeppRYSLQDSlpdgLKKLLDRSKSYWI 296
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIIN---SQEEQEF----ISKILSGNRSYWI 60
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 248-351 1.60e-09

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


:

Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 54.79  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519   248 PRSLEESRKYCTSLSSKLAVLNEPPRYSLQDSLpdglkkLLDRSKSYWI----EQMSHTVYYPQNMK----NMKGRRSDS 319
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSST------LKKSNKYFWIgltdRKNEGTWKWVDGSPvnytNWAPEPNNN 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 62543519   320 HSQSSCYLIkcYHSWWYESSYTCTDLFPCICE 351
Cdd:pfam00059  75 GENEDCVEL--SSSSGKWNDENCNSKNPFVCE 104
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
137-292 1.95e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 1.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 137 LQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLRNTRD 216
Cdd:COG4372  43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62543519 217 TLRRLSSCSSDTccpsgWVQHEKRCFYISNTPRSLEESRKYCTSLSSKLAVLNEPPRYSLQDSLPDGLKKLLDRSK 292
Cdd:COG4372 123 ERQDLEQQRKQL-----EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
 
Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 230-296 1.49e-09

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: 55.39  E-value: 1.49e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62543519 230 CPSGWVQHEKRCFYISNTPRSLEESRKYCTSLSSKLAVLNeppRYSLQDSlpdgLKKLLDRSKSYWI 296
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIIN---SQEEQEF----ISKILSGNRSYWI 60
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 248-351 1.60e-09

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 54.79  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519   248 PRSLEESRKYCTSLSSKLAVLNEPPRYSLQDSLpdglkkLLDRSKSYWI----EQMSHTVYYPQNMK----NMKGRRSDS 319
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSST------LKKSNKYFWIgltdRKNEGTWKWVDGSPvnytNWAPEPNNN 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 62543519   320 HSQSSCYLIkcYHSWWYESSYTCTDLFPCICE 351
Cdd:pfam00059  75 GENEDCVEL--SSSSGKWNDENCNSKNPFVCE 104
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 230-351 7.81e-09

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: 53.37  E-value: 7.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519    230 CPSGWVQHEKRCFYISNTPRSLEESRKYCTSLSSKLAVLNEP----------PRYSLQDSLPDGLKKLLDRSKSYWIeQM 299
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEaendfvasllKNSGSSDYYWIGLSDPDSNGSWQWS-DG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 62543519    300 SHTVYYpqnmkNMKGRRSDSHSQSSCYLIkcYHSWWYESSYTCTDLFPCICE 351
Cdd:smart00034  80 SGPVSY-----SNWAPGEPNNSSGDCVVL--STSGGKWNDVSCTSKLPFVCE 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
137-292 1.95e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 1.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 137 LQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLRNTRD 216
Cdd:COG4372  43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62543519 217 TLRRLSSCSSDTccpsgWVQHEKRCFYISNTPRSLEESRKYCTSLSSKLAVLNEPPRYSLQDSLPDGLKKLLDRSK 292
Cdd:COG4372 123 ERQDLEQQRKQL-----EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
PRK12704 PRK12704
phosphodiesterase; Provisional
 121-209 2.18e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519  121 QQFEQVSRIWEATNSSLQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKES---L 197
Cdd:PRK12704  71 NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgL 150

                         90
                 ....*....|..
gi 62543519  198 KTEEQRRQDLDQ 209
Cdd:PRK12704 151 TAEEAKEILLEK 162
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-222 1.27e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519    115 RYLQVSQQFEQVSrIWEATNS--SLQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQR 192
Cdd:TIGR02168  214 RYKELKAELRELE-LALLVLRleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110
                   ....*....|....*....|....*....|
gi 62543519    193 TKESLKTEEQRRQDLDQSLRNTRDTLRRLS 222
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELE 322
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 117-204 1.11e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519    117 LQVSQQFEQVSRIWEATNSSLQQQLREEKRQLKQKVEDLRESRRELNSTQdtFQEKQKMYEVTKQQLQDCQAESQRTKES 196
Cdd:smart00935  10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAA--REKKEKELQKKVQEFQRKQQKLQQDLQK 87


                   ....*...
gi 62543519    197 LKTEEQRR 204
Cdd:smart00935  88 RQQEELQK 95
DUF874 pfam05917
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ...
 144-227 8.70e-03

Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.


Pssm-ID: 283549 [Multi-domain]  Cd Length: 398  Bit Score: 37.91  E-value: 8.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519   144 EKRQLKQKVEDLREsrRELNSTQDTFQEKQKMY----EVTKQQLQdCQAESQRTKESLKTEEQRRQDLDQSLRNTRDTLR 219
Cdd:pfam05917 128 ELEQEKKEAENAED--RANKNGIELEQEKQKTNksgiELANNQIK-AEQEQQKTEQEKQKAEKEAIELEQEKQKTIKTQR 204


                  ....*...
gi 62543519   220 RLSSCSSD 227
Cdd:pfam05917 205 DLIKEQKD 212
 
Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 230-296 1.49e-09

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: 55.39  E-value: 1.49e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62543519 230 CPSGWVQHEKRCFYISNTPRSLEESRKYCTSLSSKLAVLNeppRYSLQDSlpdgLKKLLDRSKSYWI 296
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIIN---SQEEQEF----ISKILSGNRSYWI 60
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 248-351 1.60e-09

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 54.79  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519   248 PRSLEESRKYCTSLSSKLAVLNEPPRYSLQDSLpdglkkLLDRSKSYWI----EQMSHTVYYPQNMK----NMKGRRSDS 319
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSST------LKKSNKYFWIgltdRKNEGTWKWVDGSPvnytNWAPEPNNN 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 62543519   320 HSQSSCYLIkcYHSWWYESSYTCTDLFPCICE 351
Cdd:pfam00059  75 GENEDCVEL--SSSSGKWNDENCNSKNPFVCE 104
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 230-351 7.81e-09

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: 53.37  E-value: 7.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519    230 CPSGWVQHEKRCFYISNTPRSLEESRKYCTSLSSKLAVLNEP----------PRYSLQDSLPDGLKKLLDRSKSYWIeQM 299
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEaendfvasllKNSGSSDYYWIGLSDPDSNGSWQWS-DG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 62543519    300 SHTVYYpqnmkNMKGRRSDSHSQSSCYLIkcYHSWWYESSYTCTDLFPCICE 351
Cdd:smart00034  80 SGPVSY-----SNWAPGEPNNSSGDCVVL--STSGGKWNDVSCTSKLPFVCE 124
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 230-351 2.17e-08

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: 51.95  E-value: 2.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 230 CPSGWVQHEKRCFYISNTPRSLEESRKYCTSLSSKLAVLNEppryslQDSLpDGLKKLLdRSKSYWI----EQMSHTVYY 305
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDD------EEEL-EFLQSQI-GSSSYWIglsrEKSEKPWKW 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 62543519 306 PQN--MKNMKGRRSDSHSQSSCYLikcyHSWWYESSYtCTDLFPCICE 351
Cdd:cd03593  73 IDGspLNNLFNIRGSTKSGNCAYL----SSTGIYSED-CSTKKRWICE 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
137-292 1.95e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 1.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 137 LQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLRNTRD 216
Cdd:COG4372  43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62543519 217 TLRRLSSCSSDTccpsgWVQHEKRCFYISNTPRSLEESRKYCTSLSSKLAVLNEPPRYSLQDSLPDGLKKLLDRSK 292
Cdd:COG4372 123 ERQDLEQQRKQL-----EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-223 2.41e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 2.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 118 QVSQQFEQVSRIwEATNSSLQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESL 197
Cdd:COG4372  53 ELEQAREELEQL-EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131

                        90       100
                ....*....|....*....|....*.
gi 62543519 198 KTEEQRRQDLDQSLRNTRDTLRRLSS 223
Cdd:COG4372 132 KQLEAQIAELQSEIAEREEELKELEE 157
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 121-220 1.75e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 121 QQFEQVSRIWEATNSSLQQQlREEKRQLKQKVEDLRESRRELnstqdtfQEKQKMYEVTKQQLQDCQAESQRTKESLKTE 200
Cdd:COG3883 119 DRLSALSKIADADADLLEEL-KADKAELEAKKAELEAKLAEL-------EALKAELEAAKAELEAQQAEQEALLAQLSAE 190

                        90       100
                ....*....|....*....|
gi 62543519 201 EQRRQDLDQSLRNTRDTLRR 220
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEA 210
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 120-221 1.92e-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: 1.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 120 SQQFEQVSRIWEATNSsLQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKT 199
Cdd:COG4942 128 PEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206

                        90       100
                ....*....|....*....|..
gi 62543519 200 EEQRRQDLDQSLRNTRDTLRRL 221
Cdd:COG4942 207 ELAELAAELAELQQEAEELEAL 228
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-221 2.07e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 2.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 118 QVSQQFEQVSRIWEATNS---SLQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTK 194
Cdd:COG4372  56 QAREELEQLEEELEQARSeleQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE 135

                        90       100       110
                ....*....|....*....|....*....|....
gi 62543519 195 E-------SLKTEEQRRQDLDQSLRNTRDTLRRL 221
Cdd:COG4372 136 AqiaelqsEIAEREEELKELEEQLESLQEELAAL 169
PRK12704 PRK12704
phosphodiesterase; Provisional
 121-209 2.18e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519  121 QQFEQVSRIWEATNSSLQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKES---L 197
Cdd:PRK12704  71 NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgL 150

                         90
                 ....*....|..
gi 62543519  198 KTEEQRRQDLDQ 209
Cdd:PRK12704 151 TAEEAKEILLEK 162
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
135-223 2.66e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 135 SSLQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLRNT 214
Cdd:COG4372  27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106


                ....*....
gi 62543519 215 RDTLRRLSS 223
Cdd:COG4372 107 QEEAEELQE 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 115-221 5.67e-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: 5.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 115 RYLQVSQQFEQVsriwEATNSSLQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTK 194
Cdd:COG1196 233 KLRELEAELEEL----EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                        90       100
                ....*....|....*....|....*..
gi 62543519 195 ESLKTEEQRRQDLDQSLRNTRDTLRRL 221
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEEL 335
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 135-221 6.20e-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: 44.37  E-value: 6.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 135 SSLQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLRNT 214
Cdd:COG4942  23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102


                ....*..
gi 62543519 215 RDTLRRL 221
Cdd:COG4942 103 KEELAEL 109
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 117-213 6.81e-05

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 42.90  E-value: 6.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 117 LQVSQQFEQVSRIWEATNSSLQQQLREEKRQLKQKVEDLRESRRELnsTQDTFQEKQKmyEVTKQQlQDCQAESQRTKES 196
Cdd:COG2825  35 LQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATL--SEEERQKKER--ELQKKQ-QELQRKQQEAQQD 109

                        90
                ....*....|....*..
gi 62543519 197 LkteEQRRQDLDQSLRN 213
Cdd:COG2825 110 L---QKRQQELLQPILE 123
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-222 1.27e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519    115 RYLQVSQQFEQVSrIWEATNS--SLQQQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQR 192
Cdd:TIGR02168  214 RYKELKAELRELE-LALLVLRleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110
                   ....*....|....*....|....*....|
gi 62543519    193 TKESLKTEEQRRQDLDQSLRNTRDTLRRLS 222
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELE 322
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
118-219 1.95e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519  118 QVSQQFEQVSRIweatnsslQQQLREEKRQLK---------QKVEDLRESRRELNSTQDTFQ--EKQKMYEVTKQQLQDC 186
Cdd:COG4913  229 ALVEHFDDLERA--------HEALEDAREQIEllepirelaERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEEL 300

                         90       100       110
                 ....*....|....*....|....*....|...
gi 62543519  187 QAESQRTKESLKTEEQRRQDLDQSLRNTRDTLR 219
Cdd:COG4913  301 RAELARLEAELERLEARLDALREELDELEAQIR 333
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 140-212 2.18e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 2.18e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62543519 140 QLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKT----EEQRRQDLDQSLR 212
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaeaeIEERREELGERAR 93
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 240-351 3.03e-04

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: 39.91  E-value: 3.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 240 RCFYISNTPRSLEESRKYCTSLSSKLAVLNEPPRYS-LQDSLPD--------GLKKLLDRSKSYWIeQMSHTVYYpqnmK 310
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDfLASLLKKssssdvwiGLNDLSSEGTWKWS-DGSPLVDY----T 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 62543519 311 NMKGRRSDSHSQSSCYLIKCYHSW-WYesSYTCTDLFPCICE 351
Cdd:cd00037  76 NWAPGEPNPGGSEDCVVLSSSSDGkWN--DVSCSSKLPFICE 115
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 121-221 4.71e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.25  E-value: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519  121 QQFEQVSRIWeatnsslqQQLREEKRQLKQKVEDLRE--SRRELNSTQDTFQ---EKQKMYEVTKQQLQDCQAESQRTKE 195
Cdd:COG3096  934 EQFEQLQADY--------LQAKEQQRRLKQQIFALSEvvQRRPHFSYEDAVGllgENSDLNEKLRARLEQAEEARREARE 1005

                         90       100       110
                 ....*....|....*....|....*....|...
gi 62543519  196 SLKTEE-------QRRQDLDQSLRNTRDTLRRL 221
Cdd:COG3096 1006 QLRQAQaqysqynQVLASLKSSRDAKQQTLQEL 1038
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
138-212 5.03e-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: 5.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62543519  138 QQQLREEKRQLKQKVEDLRESRRELnstqdtfqeKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLR 212
Cdd:COG4913  304 LARLEAELERLEARLDALREELDEL---------EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 139-221 5.41e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 5.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 139 QQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQkmyEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLRNTRDTL 218
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDI---ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346


                ...
gi 62543519 219 RRL 221
Cdd:COG1196 347 EEA 349
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 137-213 5.59e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519   137 LQQQLREEKR---QLKQKVEDLRESRRELNSTQdtfQEKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLRN 213
Cdd:TIGR04523 326 IQNQISQNNKiisQLNEQISQLKKELTNSESEN---SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 116-189 6.97e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 39.82  E-value: 6.97e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62543519 116 YLQVSQQFEQVSRIWEATNSSLQQQLREEKRQLKQKV-----EDLRESRRELNSTQDTFQEKQKMYEvtkQQLQDCQAE 189
Cdd:COG2825  41 GKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAatlseEERQKKERELQKKQQELQRKQQEAQ---QDLQKRQQE 116
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 138-221 8.37e-04

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 39.22  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519  138 QQQLREEKRQLKQKVEDLRESRRELNST-QDTFQEKQKMYevtKQQLQDCQAESQRTKESLKTE-EQRRQDLDQSLRNTR 215
Cdd:PRK07353  49 KERLAEAEKLEAQYEQQLASARKQAQAViAEAEAEADKLA---AEALAEAQAEAQASKEKARREiEQQKQAALAQLEQQV 125


                 ....*.
gi 62543519  216 DTLRRL 221
Cdd:PRK07353 126 DALSRQ 131
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 139-221 1.05e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 139 QQLREEKRQLKQK--VEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLRNTRD 216
Cdd:COG1196 216 RELKEELKELEAEllLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295


                ....*
gi 62543519 217 TLRRL 221
Cdd:COG1196 296 ELARL 300
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 117-204 1.11e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519    117 LQVSQQFEQVSRIWEATNSSLQQQLREEKRQLKQKVEDLRESRRELNSTQdtFQEKQKMYEVTKQQLQDCQAESQRTKES 196
Cdd:smart00935  10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAA--REKKEKELQKKVQEFQRKQQKLQQDLQK 87


                   ....*...
gi 62543519    197 LKTEEQRR 204
Cdd:smart00935  88 RQQEELQK 95
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
146-223 1.25e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62543519  146 RQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLRNTRDTLRRLSS 223
Cdd:COG4913  664 ASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 137-205 1.65e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 1.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62543519  137 LQQQLREEKR--QLKQKVEDLREsrRELNSTQDTFQEKQKmyEVTKQQLQDCQAESQRTKESLKTEEQRRQ 205
Cdd:PRK09510  67 QQQQQKSAKRaeEQRKKKEQQQA--EELQQKQAAEQERLK--QLEKERLAAQEQKKQAEEAAKQAALKQKQ 133
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 139-223 2.02e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519    139 QQLREE----KRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSLRNT 214
Cdd:TIGR02168  785 EELEAQieqlKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864


                   ....*....
gi 62543519    215 RDTLRRLSS 223
Cdd:TIGR02168  865 EELIEELES 873
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 118-221 2.30e-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: 40.04  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519    118 QVSQQFEQVSRIWEATNSSLQ------QQLREEKRQLKQKVEDLRESRRELNSTQDTFQEK----QKMYEVTKQQLQDCQ 187
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISrleqqkQILRERLANLERQLEELEAQLEELESKLDELAEElaelEEKLEELKEELESLE 357

                           90       100       110
                   ....*....|....*....|....*....|....
gi 62543519    188 AESQRTKESLKTEEQRRQDLDQSLRNTRDTLRRL 221
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQL 391
PTZ00121 PTZ00121
MAEBL; Provisional
 114-206 2.31e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519   114 VRYLQVSQQFEQVSRIWEATNSSLQQQLREEKR--QLKQKVEDLRESRRELNSTQDTFQEKQKMYEVTKQQLQDCQAESQ 191
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKaeEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR 1278

                          90
                  ....*....|....*
gi 62543519   192 RTKESLKTEEQRRQD 206
Cdd:PTZ00121 1279 KADELKKAEEKKKAD 1293
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
121-223 2.32e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 121 QQFEQVSRIWEATN--SSLQQQLREEK---RQLKQKVEDLRESRRELNSTQDTFQEKQ-KMYEVTKQQLQDCQAESQRTK 194
Cdd:COG4717 119 EKLEKLLQLLPLYQelEALEAELAELPerlEELEERLEELRELEEELEELEAELAELQeELEELLEQLSLATEEELQDLA 198

                        90       100
                ....*....|....*....|....*....
gi 62543519 195 ESLKTEEQRRQDLDQSLRNTRDTLRRLSS 223
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEE 227
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
136-223 2.40e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519  136 SLQQQLRE----EKRQLKQKVEDLRESRRELNSTQDTFQEKQKMYEV----TKQQLQDCQAESQRTKESLKTE----EQR 203
Cdd:COG4913  327 ELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLplpaSAEEFAALRAEAAALLEALEEElealEEA 406

                         90       100
                 ....*....|....*....|
gi 62543519  204 RQDLDQSLRNTRDTLRRLSS 223
Cdd:COG4913  407 LAEAEAALRDLRRELRELEA 426
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-218 2.66e-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: 40.04  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519    112 LGVRYLQVSQQFEQVSR---IWEATNSSLQQQLREEKRQ---LKQKVEDLRESRRELnstQDTFQEKQKMYEVTKQQLQD 185
Cdd:TIGR02168  815 LNEEAANLRERLESLERriaATERRLEDLEEQIEELSEDiesLAAEIEELEELIEEL---ESELEALLNERASLEEALAL 891

                           90       100       110
                   ....*....|....*....|....*....|...
gi 62543519    186 CQAESQRTKESLKTEEQRRQDLDQSLRNTRDTL 218
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKL 924
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 139-223 3.28e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 3.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519    139 QQLREEKRQLKQKVEDLRESRRELNSTQDTFQEKQKMY-----------EVTKQQLQDCQAESQRTKESLKTEEQRRQ-- 205
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLseeladlnaaiAGIEAKINELEEEKEDKALEIKKQEWKLEql 460

                           90       100
                   ....*....|....*....|...
gi 62543519    206 -----DLDQSLRNTRDTLRRLSS 223
Cdd:TIGR02169  461 aadlsKYEQELYDLKEEYDRVEK 483
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
115-220 6.43e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 6.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519 115 RYLQVSQQFEQVSR-IWEATNSSLQQQLREEKRQLKQKVEDLRESRRELNSTqdtFQEKQKMYEVTKQQLQdcqAESQRT 193
Cdd:COG3206 241 RLAALRAQLGSGPDaLPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPD---VIALRAQIAALRAQLQ---QEAQRI 314

                        90       100
                ....*....|....*....|....*..
gi 62543519 194 KESLKTEEQRRQDLDQSLRNTRDTLRR 220
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEA 341
mukB PRK04863
chromosome partition protein MukB;
132-215 7.99e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.40  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519   132 ATNSSLQQQLREekrQLKQKVEDLRESRRELNSTQDTFQEKQKM-------YEVTKQQLQDCQAESQ----RTKESLktE 200
Cdd:PRK04863  981 AKNSDLNEKLRQ---RLEQAEQERTRAREQLRQAQAQLAQYNQVlaslkssYDAKRQMLQELKQELQdlgvPADSGA--E 1055

                          90
                  ....*....|....*...
gi 62543519   201 EQ---RRQDLDQSLRNTR 215
Cdd:PRK04863 1056 ERaraRRDELHARLSANR 1073
DUF874 pfam05917
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ...
 144-227 8.70e-03

Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.


Pssm-ID: 283549 [Multi-domain]  Cd Length: 398  Bit Score: 37.91  E-value: 8.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519   144 EKRQLKQKVEDLREsrRELNSTQDTFQEKQKMY----EVTKQQLQdCQAESQRTKESLKTEEQRRQDLDQSLRNTRDTLR 219
Cdd:pfam05917 128 ELEQEKKEAENAED--RANKNGIELEQEKQKTNksgiELANNQIK-AEQEQQKTEQEKQKAEKEAIELEQEKQKTIKTQR 204


                  ....*...
gi 62543519   220 RLSSCSSD 227
Cdd:pfam05917 205 DLIKEQKD 212
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 115-213 9.41e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 38.01  E-value: 9.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62543519   115 RYLQVSQQFEQVSRIWEAtnssLQQQLREEKRQLKQKVEDLREsrrelNSTQDTFQEKQKMYEVTKQQLQdcqaesqrtK 194
Cdd:PRK11448  167 QSQALAEAQQQELVALEG----LAAELEEKQQELEAQLEQLQE-----KAAETSQERKQKRKEITDQAAK---------R 228

                          90
                  ....*....|....*....
gi 62543519   195 ESLkTEEQRRQDLDQSLRN 213
Cdd:PRK11448  229 LEL-SEEETRILIDQQLRK 246
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 133-211 9.75e-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: 37.80  E-value: 9.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62543519   133 TNSSLQQQLREEKRQLKQKVEDLRESRRELnstqDTFQEKQKMYEVTKQQLQDCQAESQRTKESLKTEEQRRQDLDQSL 211
Cdd:pfam05557 105 VISCLKNELSELRRQIQRAELELQSTNSEL----EELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEI 179
 
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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