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Conserved domains on  [gi|578816790|ref|XP_006716956|]
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B-cell differentiation antigen CD72 isoform X1 [Homo sapiens]

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 ...
 233-319 3.97e-17

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: 76.87  E-value: 3.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790   233 CPSGWIMHQKSCFYISLTSKNWQESQKQCETLSSKLATFseiypqsHSYY---FLNSLLPNGGSGNSYWTGLS---SNKD 306
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASI-------HSEAendFVASLLKNSGSSDYYWIGLSdpdSNGS 73

                           90
                   ....*....|...
gi 578816790   307 WKLTDDTQRTRHS 319
Cdd:smart00034  74 WQWSDGSGPVSYS 86
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-220 4.18e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 117 RYLQVSQQLQQTNRVLEVTN-SSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKT 195
Cdd:COG1196  214 RYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                         90       100
                 ....*....|....*....|....*
gi 578816790 196 KETLQSEEQQRRALEQKLSNMENRL 220
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERL 318
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 233-319 3.97e-17

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: 76.87  E-value: 3.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790   233 CPSGWIMHQKSCFYISLTSKNWQESQKQCETLSSKLATFseiypqsHSYY---FLNSLLPNGGSGNSYWTGLS---SNKD 306
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASI-------HSEAendFVASLLKNSGSSDYYWIGLSdpdSNGS 73

                           90
                   ....*....|...
gi 578816790   307 WKLTDDTQRTRHS 319
Cdd:smart00034  74 WQWSDGSGPVSYS 86
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 233-313 2.12e-14

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: 68.90  E-value: 2.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 233 CPSGWIMHQKSCFYISLTSKNWQESQKQCETLSSKLATF---SEIypqshsyYFLNSLLPNggsgNSYWTGLS---SNKD 306
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIddeEEL-------EFLQSQIGS----SSYWIGLSrekSEKP 69


                 ....*..
gi 578816790 307 WKLTDDT 313
Cdd:cd03593   70 WKWIDGS 76
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 251-316 1.41e-07

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 49.40  E-value: 1.41e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578816790  251 SKNWQESQKQCETLSSKLATFseiyPQSHSYYFLNSLLPNggSGNSYWTGLS---SNKDWKLTDDTQRT 316
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSI----NSAEELDFLSSTLKK--SNKYFWIGLTdrkNEGTWKWVDGSPVN 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-220 4.18e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 117 RYLQVSQQLQQTNRVLEVTN-SSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKT 195
Cdd:COG1196  214 RYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                         90       100
                 ....*....|....*....|....*
gi 578816790 196 KETLQSEEQQRRALEQKLSNMENRL 220
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERL 318
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 233-313 1.11e-05

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 45.88  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 233 CPSGWIMHQKSCFYISLTSKNWQESQKQCETLSsklATFSEIYPQSHsyyfLNsLLPNGGSGNSYWTGL---SSNKDWKL 309
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLG---ATLVKVETEEE----LN-FLKRYKDSSDHWIGLnreSSNHPWKW 159


                 ....
gi 578816790 310 TDDT 313
Cdd:PHA02642 160 ADNS 163
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 126-211 1.71e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.26  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 126 QQTNRVLEVTNSSLR-QQLRLKITQlgQSAEDLQgsRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQSEEQ 204
Cdd:PRK09510  62 EQYNRQQQQQKSAKRaEEQRKKKEQ--QQAEELQ--QKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA 137


                 ....*..
gi 578816790 205 QRRALEQ 211
Cdd:PRK09510 138 AAKAAAA 144
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 117-219 4.71e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 42.05  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790  117 RYLQVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQE----ALQ-----VEQR-AHQAAEGQLQ 186
Cdd:pfam07111 521 QLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygqALQekvaeVETRlREQLSDTKRR 600

                          90       100       110
                  ....*....|....*....|....*....|...
gi 578816790  187 ACQADRQKTKETLQSEEQQRRALEQKLSNMENR 219
Cdd:pfam07111 601 LNEARREQAKAVVSLRQIQHRATQEKERNQELR 633
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 119-213 2.95e-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: 37.56  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790   119 LQVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQgsRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKET 198
Cdd:smart00935  10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQ--KDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQK 87

                           90
                   ....*....|....*
gi 578816790   199 LQSEEQQRraLEQKL 213
Cdd:smart00935  88 RQQEELQK--ILDKI 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 120-220 3.80e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790   120 QVSQQLQQTNRVLEVTNSSLrQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLqacQADRQKTKETL 199
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL---ERQLEELEAQL 325

                           90       100
                   ....*....|....*....|.
gi 578816790   200 QSEEQQRRALEQKLSNMENRL 220
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKL 346
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 233-319 3.97e-17

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: 76.87  E-value: 3.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790   233 CPSGWIMHQKSCFYISLTSKNWQESQKQCETLSSKLATFseiypqsHSYY---FLNSLLPNGGSGNSYWTGLS---SNKD 306
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASI-------HSEAendFVASLLKNSGSSDYYWIGLSdpdSNGS 73

                           90
                   ....*....|...
gi 578816790   307 WKLTDDTQRTRHS 319
Cdd:smart00034  74 WQWSDGSGPVSYS 86
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 233-313 2.12e-14

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: 68.90  E-value: 2.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 233 CPSGWIMHQKSCFYISLTSKNWQESQKQCETLSSKLATF---SEIypqshsyYFLNSLLPNggsgNSYWTGLS---SNKD 306
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIddeEEL-------EFLQSQIGS----SSYWIGLSrekSEKP 69


                 ....*..
gi 578816790 307 WKLTDDT 313
Cdd:cd03593   70 WKWIDGS 76
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 233-313 1.28e-12

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: 64.25  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 233 CPSGWIMHQKSCFYISLTSKNWQESQKQCETLSSKLATFSEIYPQShsyyFLNSLLPnggSGNSYWTGLS-SNKD--WKL 309
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQE----FISKILS---GNRSYWIGLSdEETEgeWKW 73


                 ....
gi 578816790 310 TDDT 313
Cdd:cd03590   74 VDGT 77
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 243-313 1.51e-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.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 55.32  E-value: 1.51e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578816790 243 SCFYISLTSKNWQESQKQCETLSSKLATFseiypqsHSYY---FLNSLLPNGGSgNSYWTGLS---SNKDWKLTDDT 313
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASI-------HSEEendFLASLLKKSSS-SDVWIGLNdlsSEGTWKWSDGS 69
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 251-316 1.41e-07

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 49.40  E-value: 1.41e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578816790  251 SKNWQESQKQCETLSSKLATFseiyPQSHSYYFLNSLLPNggSGNSYWTGLS---SNKDWKLTDDTQRT 316
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSI----NSAEELDFLSSTLKK--SNKYFWIGLTdrkNEGTWKWVDGSPVN 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-220 4.18e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 117 RYLQVSQQLQQTNRVLEVTN-SSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKT 195
Cdd:COG1196  214 RYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                         90       100
                 ....*....|....*....|....*
gi 578816790 196 KETLQSEEQQRRALEQKLSNMENRL 220
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERL 318
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
115-221 5.17e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 115 GVRYLQVSQQLQQTNRVLEvtnsSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQK 194
Cdd:COG4372   23 GILIAALSEQLRKALFELD----KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98

                         90       100
                 ....*....|....*....|....*..
gi 578816790 195 TKETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:COG4372   99 AQEELESLQEEAEELQEELEELQKERQ 125
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
120-221 1.02e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 120 QVSQQLQQTNRVLEVTNSSL---RQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTK 196
Cdd:COG4372   49 QLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128

                         90       100
                 ....*....|....*....|....*
gi 578816790 197 ETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:COG4372  129 QQRKQLEAQIAELQSEIAEREEELK 153
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 123-220 1.30e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 123 QQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQSE 202
Cdd:COG1196  319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                         90
                 ....*....|....*...
gi 578816790 203 EQQRRALEQKLSNMENRL 220
Cdd:COG1196  399 AAQLEELEEAEEALLERL 416
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 120-221 1.93e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 120 QVSQQLQQTNRVLEVTNSSLRQ------QLRLKITQLGQSAEDLQGSRREL----AQSQEALQVEQRAHQAAEGQLQACQ 189
Cdd:COG1196  243 ELEAELEELEAELEELEAELAEleaeleELRLELEELELELEEAQAEEYELlaelARLEQDIARLEERRRELEERLEELE 322

                         90       100       110
                 ....*....|....*....|....*....|..
gi 578816790 190 ADRQKTKETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELE 354
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
120-221 2.89e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 2.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 120 QVSQQLQQTNRVLEVTNSSLRQ---QLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTK 196
Cdd:COG4372   63 QLEEELEQARSELEQLEEELEElneQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142

                         90       100
                 ....*....|....*....|....*
gi 578816790 197 ETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:COG4372  143 SEIAEREEELKELEEQLESLQEELA 167
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
120-219 6.90e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 120 QVSQQLQQTNRVLEVTNSSLRQQLRlKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETL 199
Cdd:COG4372   77 QLEEELEELNEQLQAAQAELAQAQE-ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155

                         90       100
                 ....*....|....*....|....
gi 578816790 200 QSE----EQQRRALEQKLSNMENR 219
Cdd:COG4372  156 EEQleslQEELAALEQELQALSEA 179
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 233-313 1.11e-05

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 45.88  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 233 CPSGWIMHQKSCFYISLTSKNWQESQKQCETLSsklATFSEIYPQSHsyyfLNsLLPNGGSGNSYWTGL---SSNKDWKL 309
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLG---ATLVKVETEEE----LN-FLKRYKDSSDHWIGLnreSSNHPWKW 159


                 ....
gi 578816790 310 TDDT 313
Cdd:PHA02642 160 ADNS 163
PHA02867 PHA02867
C-type lectin protein; Provisional
 220-268 1.59e-05

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 44.67  E-value: 1.59e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578816790 220 LKPFFTCGSADTCCPSGWIMHQKSCFYISLTSKNWQESQKQCETLSSKL 268
Cdd:PHA02867  36 CKWYYAFPYFSKVCPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSL 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-221 1.66e-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: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 117 RYLQVSQQLQQTNRVLEVTNSSLRQ---QLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQ 193
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEEleaELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100
                 ....*....|....*....|....*...
gi 578816790 194 KTKETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELE 340
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 122-221 1.76e-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: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 122 SQQLQQTNRVLEVTNSsLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQS 201
Cdd:COG4942  128 PEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206

                         90       100
                 ....*....|....*....|
gi 578816790 202 EEQQRRALEQKLSNMENRLK 221
Cdd:COG4942  207 ELAELAAELAELQQEAEELE 226
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
120-217 2.09e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 120 QVSQQLQQTNRVLEvtnsSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETL 199
Cdd:COG4372   42 KLQEELEQLREELE----QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                         90
                 ....*....|....*...
gi 578816790 200 QSEEQQRRALEQKLSNME 217
Cdd:COG4372  118 EELQKERQDLEQQRKQLE 135
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-219 6.93e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790  120 QVSQQLQQTNRVLEVTNSSLR-QQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKET 198
Cdd:COG4913   642 ALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721

                          90       100
                  ....*....|....*....|.
gi 578816790  199 LQSEEQQRRALEQKLSNMENR 219
Cdd:COG4913   722 LEQAEEELDELQDRLEAAEDL 742
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 123-221 9.17e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 9.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 123 QQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQSE 202
Cdd:COG1196  284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                         90
                 ....*....|....*....
gi 578816790 203 EQQRRALEQKLSNMENRLK 221
Cdd:COG1196  364 EEALLEAEAELAEAEEELE 382
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 126-211 1.71e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.26  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 126 QQTNRVLEVTNSSLR-QQLRLKITQlgQSAEDLQgsRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQSEEQ 204
Cdd:PRK09510  62 EQYNRQQQQQKSAKRaEEQRKKKEQ--QQAEELQ--QKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA 137


                 ....*..
gi 578816790 205 QRRALEQ 211
Cdd:PRK09510 138 AAKAAAA 144
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 116-222 1.80e-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: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 116 VRYLQVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLqacQADRQKT 195
Cdd:COG4942  135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL---EKELAEL 211

                         90       100
                 ....*....|....*....|....*..
gi 578816790 196 KETLQSEEQQRRALEQKLSNMENRLKP 222
Cdd:COG4942  212 AAELAELQQEAEELEALIARLEAEAAA 238
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 123-220 1.97e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 123 QQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQSE 202
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         90
                 ....*....|....*...
gi 578816790 203 EQQRRALEQKLSNMENRL 220
Cdd:COG1196  378 EEELEELAEELLEALRAA 395
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 149-221 2.12e-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: 42.83  E-value: 2.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578816790 149 QLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-221 4.42e-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: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790  120 QVSQQLQQTNRVLEvtnsSLRQQLRL--KITQLGQSAEDLQGSRRELAQSQEALQVEQRAH---QAAEGQLQACQADRQK 194
Cdd:COG4913   628 EAEERLEALEAELD----ALQERREAlqRLAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEE 703

                          90       100
                  ....*....|....*....|....*..
gi 578816790  195 TKETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:COG4913   704 LEEELDELKGEIGRLEKELEQAEEELD 730
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-221 4.63e-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: 41.67  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 117 RYLQVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTK 196
Cdd:COG4942  108 ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187

                         90       100
                 ....*....|....*....|....*
gi 578816790 197 ETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:COG4942  188 AALEALKAERQKLLARLEKELAELA 212
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 117-219 4.71e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 42.05  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790  117 RYLQVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQE----ALQ-----VEQR-AHQAAEGQLQ 186
Cdd:pfam07111 521 QLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygqALQekvaeVETRlREQLSDTKRR 600

                          90       100       110
                  ....*....|....*....|....*....|...
gi 578816790  187 ACQADRQKTKETLQSEEQQRRALEQKLSNMENR 219
Cdd:pfam07111 601 LNEARREQAKAVVSLRQIQHRATQEKERNQELR 633
PRK11637 PRK11637
AmiB activator; Provisional
 140-221 7.48e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 7.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 140 RQQlrlKITQLGQSAEDLQGSRRELAQSQE---ALQVEQRAHQAaegQLQACQADRQKTKETLQSEEQQRRALEQKLSNM 216
Cdd:PRK11637 168 RQE---TIAELKQTREELAAQKAELEEKQSqqkTLLYEQQAQQQ---KLEQARNERKKTLTGLESSLQKDQQQLSELRAN 241


                 ....*
gi 578816790 217 ENRLK 221
Cdd:PRK11637 242 ESRLR 246
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 122-212 1.03e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.36  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790   122 SQQLQQTNRVLEVTNSSLRQQ-------LRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQAC--QADR 192
Cdd:pfam12128  557 PELLHRTDLDPEVWDGSVGGElnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQAngELEK 636

                           90       100
                   ....*....|....*....|....*.
gi 578816790   193 QKTKETL------QSEEQQRRALEQK 212
Cdd:pfam12128  637 ASREETFartalkNARLDLRRLFDEK 662
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 120-220 1.79e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790   120 QVSQQLQQTNRVLEVTNSSLRQQ---LRLKIT----QLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADR 192
Cdd:pfam01576  201 KGRQELEKAKRKLEGESTDLQEQiaeLQAQIAelraQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL 280

                           90       100
                   ....*....|....*....|....*...
gi 578816790   193 QKTKETLQSEEQQRRALEQKLSNMENRL 220
Cdd:pfam01576  281 ESERAARNKAEKQRRDLGEELEALKTEL 308
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
 233-272 1.88e-03

C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS); CLECT_DGCR2_like: C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DGS is also known velo-cardio-facial syndrome (VCFS). DGS is a genetic abnormality that results in malformations of the heart, face, and limbs and is associated with schizophrenia and depressive disorders. DGCR2 is a candidate for involvement in the pathogenesis of DGS since the DGCR2 gene lies within the minimal DGS critical region (MDGRC) of 22q11, which when deleted gives rise to DGS, and the DGCR2 gene is in close proximity to the balanced translocation breakpoint in a DGS patient having a balanced translocation.


Pssm-ID: 153069  Cd Length: 153  Bit Score: 38.36  E-value: 1.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 578816790 233 CPSGWIMHQK--SCFYISLTSKNWQESQKQCETLSSKLATFS 272
Cdd:cd03599    1 CPSGWHHYEGtaSCYKVYLSGENYWDAVQTCQKVNGSLATFT 42
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
141-221 2.11e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790  141 QQLRLKITQLGQSAE--DLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQSEEQQRR--------ALE 210
Cdd:COG4913   265 AAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLE 344

                          90
                  ....*....|.
gi 578816790  211 QKLSNMENRLK 221
Cdd:COG4913   345 REIERLERELE 355
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
119-221 2.44e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 119 LQVSQQLQQTNRVLEVTNSSLRQqLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEG--QLQACQADRQKTK 196
Cdd:COG4717   70 LKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPERL 148

                         90       100
                 ....*....|....*....|....*
gi 578816790 197 ETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELA 173
mukB PRK04863
chromosome partition protein MukB;
120-221 2.73e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790  120 QVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAE---DLQGSRR-------ELAQSQEALQVeqrahQAAEGQLQACQ 189
Cdd:PRK04863  985 DLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQvlaSLKSSYDakrqmlqELKQELQDLGV-----PADSGAEERAR 1059

                          90       100       110
                  ....*....|....*....|....*....|..
gi 578816790  190 ADRQKTKETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:PRK04863 1060 ARRDELHARLSANRSRRNQLEKQLTFCEAEMD 1091
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 119-213 2.95e-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: 37.56  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790   119 LQVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQgsRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKET 198
Cdd:smart00935  10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQ--KDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQK 87

                           90
                   ....*....|....*
gi 578816790   199 LQSEEQQRraLEQKL 213
Cdd:smart00935  88 RQQEELQK--ILDKI 100
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 152-220 3.28e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 3.28e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578816790   152 QSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQSEEQQRRALEQKLSNMENRL 220
Cdd:pfam01576  458 KLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQL 526
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
117-221 3.71e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 117 RYLQVSQQLQQTNRVL-EVTNSSLRQQLRLKITQLGQSAEDLQGS-----------RRELAQSQEALQVE-QRAHQAAEG 183
Cdd:COG3206  241 RLAALRAQLGSGPDALpELLQSPVIQQLRAQLAELEAELAELSARytpnhpdvialRAQIAALRAQLQQEaQRILASLEA 320

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 578816790 184 QLQACQADRQKTKETLQSEEQQRRAL---EQKLSNMENRLK 221
Cdd:COG3206  321 ELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVE 361
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 120-220 3.80e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790   120 QVSQQLQQTNRVLEVTNSSLrQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLqacQADRQKTKETL 199
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL---ERQLEELEAQL 325

                           90       100
                   ....*....|....*....|.
gi 578816790   200 QSEEQQRRALEQKLSNMENRL 220
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKL 346
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
117-214 4.01e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 117 RYLQVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAE-DLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKT 195
Cdd:COG4717  153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232

                         90
                 ....*....|....*....
gi 578816790 196 KETLQSEEQQRRALEQKLS 214
Cdd:COG4717  233 ENELEAAALEERLKEARLL 251
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 233-311 4.41e-03

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: 36.97  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 233 CPSGWIMHQKSCFYISLTSKNWQESQKQCETL--SSKLATFSEiyPQSHSyyFLNSLLPNGGSGNSY-WTGL---SSNKD 306
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHS--PAEAA--AIASLISSYQKAYQPvWIGLhdpQQSRG 76


                 ....*
gi 578816790 307 WKLTD 311
Cdd:cd03594   77 WEWSD 81
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 123-216 4.48e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790   123 QQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALqveqrahqAAEGQLQACQADRQKTKETLQSE 202
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL--------SEEYSLTLEEAEALENKIEDDEE 968

                           90
                   ....*....|....*.
gi 578816790   203 EQQRR--ALEQKLSNM 216
Cdd:TIGR02168  969 EARRRlkRLENKIKEL 984
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
117-221 4.57e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790 117 RYLQVSQQLQQTNRVLEVTNSSLRQQLRLKITQLgQSAEDLQGsRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTK 196
Cdd:COG4717  361 EELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKE-ELEELEEQLEELLGELEELLEALDEEELEEELEELE 438

                         90       100
                 ....*....|....*....|....*
gi 578816790 197 ETLQSEEQQRRALEQKLSNMENRLK 221
Cdd:COG4717  439 EELEELEEELEELREELAELEAELE 463
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 120-213 5.83e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 38.29  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790  120 QVSQQLQQTNRVLEVTNSSLRQQLRLKITQLGQSAEDLQGSRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETL 199
Cdd:TIGR02794  54 RIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAK 133

                          90
                  ....*....|....
gi 578816790  200 QSEEQQRralEQKL 213
Cdd:TIGR02794 134 AKAEAEA---ERKA 144
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 121-218 9.46e-03

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: 38.08  E-value: 9.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816790  121 VSQQLQQTNRVLEVTNSSLRQQLRlKITQLGQSAEDLqgsRRELAQSQEALQVEQRAHQAAEGQLQACQADRQKTKETLQ 200
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNK-IISQLNEQISQL---KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387

                          90
                  ....*....|....*...
gi 578816790  201 SEEQQRRALEQKLSNMEN 218
Cdd:TIGR04523 388 NLESQINDLESKIQNQEK 405
 
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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