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Conserved domains on  [gi|2496213732|ref|NP_001406902|]
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B-cell differentiation antigen CD72 isoform 5 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 264-373 1.54e-14

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 69.55  E-value: 1.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  264 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEPskyyYEVSLPSGLEELLDRSKSYWI-------QMSKKW 336
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSE----AENDFVASLLKNSGSSDYYWIglsdpdsNGSWQW 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2496213732  337 RQDS-------------DSQSRHCVRIKTYYQKWERTisKCAELHPCICE 373
Cdd:smart00034  77 SDGSgpvsysnwapgepNNSSGDCVVLSTSGGKWNDV--SCTSKLPFVCE 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
158-245 2.75e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 58.38  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 158 QEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEER 237
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109


                  ....*...
gi 2496213732 238 RRDLDQRL 245
Cdd:COG4372   110 AEELQEEL 117
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 264-373 1.54e-14

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 69.55  E-value: 1.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  264 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEPskyyYEVSLPSGLEELLDRSKSYWI-------QMSKKW 336
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSE----AENDFVASLLKNSGSSDYYWIglsdpdsNGSWQW 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2496213732  337 RQDS-------------DSQSRHCVRIKTYYQKWERTisKCAELHPCICE 373
Cdd:smart00034  77 SDGSgpvsysnwapgepNNSSGDCVVLSTSGGKWNDV--SCTSKLPFVCE 124
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 264-373 2.91e-12

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: 63.12  E-value: 2.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 264 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDepSKyyyevslpsglEEL-----LDRSKSYWI-----QMS 333
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKID--DE-----------EELeflqsQIGSSSYWIglsreKSE 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2496213732 334 KKWRQDSDS------------QSRHCVriktYYQKWERTISKCAELHPCICE 373
Cdd:cd03593    68 KPWKWIDGSplnnlfnirgstKSGNCA----YLSSTGIYSEDCSTKKRWICE 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
158-245 2.75e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 58.38  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 158 QEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEER 237
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109


                  ....*...
gi 2496213732 238 RRDLDQRL 245
Cdd:COG4372   110 AEELQEEL 117
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 154-262 5.27e-05

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: 45.55  E-value: 5.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  154 SRQFQEGT-RIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLK 232
Cdd:pfam01576  202 GRQELEKAkRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLE 281

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496213732  233 TE-------EERRRDLDQRLtstrETLRRFFSDSSDT 262
Cdd:pfam01576  282 SEraarnkaEKQRRDLGEEL----EALKTELEDTLDT 314
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 170-245 2.66e-04

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


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 39.47  E-value: 2.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2496213732 170 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRL 245
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERW 76
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 264-372 3.50e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 40.62  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 264 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEPSKYYYEVSLPSGleelldrsKSYWIQMSKKWRQDSDSQ 343
Cdd:PHA03097   46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGG--------QDLWIGIEKKKGDDDDRE 117

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2496213732 344 SRHCVRIK------TYYQKWERTISKCAELHPCIC 372
Cdd:PHA03097  118 VLDKVVKPpksgkcAYLKDKTIISSNCNATKGWIC 152
mukB PRK04863
chromosome partition protein MukB;
166-253 7.06e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 7.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  166 ATNSSLQQQLREKisqLGQKEVELQKARKELISSQDTLQE--------------KQRTHEDAEQQLQ-----ACQ--AER 224
Cdd:PRK04863   981 AKNSDLNEKLRQR---LEQAEQERTRAREQLRQAQAQLAQynqvlaslkssydaKRQMLQELKQELQdlgvpADSgaEER 1057

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2496213732  225 AKTK-----ENLKTEEERRRDLDQRLTSTRETLR 253
Cdd:PRK04863  1058 ARARrdelhARLSANRSRRNQLEKQLTFCEAEMD 1091
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-253 8.23e-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: 41.58  E-value: 8.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  165 EATNSSLQQQ------LREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERR 238
Cdd:TIGR02168  666 AKTNSSILERrreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90
                   ....*....|....*
gi 2496213732  239 RDLDQRLTSTRETLR 253
Cdd:TIGR02168  746 EERIAQLSKELTELE 760
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 284-373 8.91e-04

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 38.61  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 284 SLEESQKYCTSLSSKLAAFDEPSKYYYEVSLpsgleeLLDRSKSYWI-----QMSKKWR---------------QDSDSQ 343
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSST------LKKSNKYFWIgltdrKNEGTWKwvdgspvnytnwapePNNNGE 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 2496213732 344 SRHCVRIKTYYQKWErtISKCAELHPCICE 373
Cdd:pfam00059  77 NEDCVELSSSSGKWN--DENCNSKNPFVCE 104
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 164-244 4.00e-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: 37.18  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  164 WEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRthEDAEQQLQacqaerAKTKENLKTEEERRRDLDQ 243
Cdd:smart00935  16 GKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAR--EKKEKELQ------KKVQEFQRKQQKLQQDLQK 87


                   .
gi 2496213732  244 R 244
Cdd:smart00935  88 R 88
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 264-373 1.54e-14

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 69.55  E-value: 1.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  264 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEPskyyYEVSLPSGLEELLDRSKSYWI-------QMSKKW 336
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSE----AENDFVASLLKNSGSSDYYWIglsdpdsNGSWQW 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2496213732  337 RQDS-------------DSQSRHCVRIKTYYQKWERTisKCAELHPCICE 373
Cdd:smart00034  77 SDGSgpvsysnwapgepNNSSGDCVVLSTSGGKWNDV--SCTSKLPFVCE 124
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 264-373 2.91e-12

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: 63.12  E-value: 2.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 264 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDepSKyyyevslpsglEEL-----LDRSKSYWI-----QMS 333
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKID--DE-----------EELeflqsQIGSSSYWIglsreKSE 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2496213732 334 KKWRQDSDS------------QSRHCVriktYYQKWERTISKCAELHPCICE 373
Cdd:cd03593    68 KPWKWIDGSplnnlfnirgstKSGNCA----YLSSTGIYSEDCSTKKRWICE 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
158-245 2.75e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 58.38  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 158 QEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEER 237
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109


                  ....*...
gi 2496213732 238 RRDLDQRL 245
Cdd:COG4372   110 AEELQEEL 117
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-254 1.37e-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: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 165 EATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 244
Cdd:COG1196   280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                          90
                  ....*....|
gi 2496213732 245 LTSTRETLRR 254
Cdd:COG1196   360 LAEAEEALLE 369
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 174-245 2.39e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 2.39e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2496213732 174 QLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKT----EEERRRDLDQRL 245
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaeaeIEERREELGERA 92
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
169-254 5.61e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 5.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 169 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 248
Cdd:COG4372    83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162


                  ....*.
gi 2496213732 249 RETLRR 254
Cdd:COG4372   163 QEELAA 168
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
169-254 5.66e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 169 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 248
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106


                  ....*.
gi 2496213732 249 RETLRR 254
Cdd:COG4372   107 QEEAEE 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-254 7.45e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 7.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 165 EATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 244
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324

                          90
                  ....*....|
gi 2496213732 245 LTSTRETLRR 254
Cdd:COG1196   325 LAELEEELEE 334
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 169-255 8.05e-06

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: 47.45  E-value: 8.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 169 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 248
Cdd:COG4942   142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221


                  ....*..
gi 2496213732 249 RETLRRF 255
Cdd:COG4942   222 AEELEAL 228
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 264-330 8.13e-06

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: 44.99  E-value: 8.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496213732 264 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEPSKyyyevslPSGLEELLDRSKSYWI 330
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEE-------QEFISKILSGNRSYWI 60
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 149-254 9.10e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 9.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 149 RYLQVSRQFQEgTRIWEATNS--SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAK 226
Cdd:COG1196   214 RYRELKEELKE-LEAELLLLKlrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100
                  ....*....|....*....|....*...
gi 2496213732 227 TKENLKTEEERRRDLDQRLTSTRETLRR 254
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELEERLEE 320
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 169-254 1.17e-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: 47.07  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 169 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 248
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102


                  ....*.
gi 2496213732 249 RETLRR 254
Cdd:COG4942   103 KEELAE 108
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-254 1.59e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 165 EATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 244
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                          90
                  ....*....|
gi 2496213732 245 LTSTRETLRR 254
Cdd:COG1196   332 LEELEEELEE 341
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
165-254 2.03e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 165 EATNSSLQQ---QLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDL 241
Cdd:COG4372    62 EQLEEELEQarsELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141

                          90
                  ....*....|...
gi 2496213732 242 DQRLTSTRETLRR 254
Cdd:COG4372   142 QSEIAEREEELKE 154
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 154-262 5.27e-05

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: 45.55  E-value: 5.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  154 SRQFQEGT-RIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLK 232
Cdd:pfam01576  202 GRQELEKAkRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLE 281

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496213732  233 TE-------EERRRDLDQRLtstrETLRRFFSDSSDT 262
Cdd:pfam01576  282 SEraarnkaEKQRRDLGEEL----EALKTELEDTLDT 314
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
171-244 7.13e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 7.13e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2496213732 171 LQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 244
Cdd:COG4372    57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 170-236 7.76e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 7.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496213732 170 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEE 236
Cdd:COG3883   140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
173-255 9.18e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 9.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  173 QQLREKISqlgqkevELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETL 252
Cdd:COG4913    664 ASAEREIA-------ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736


                   ...
gi 2496213732  253 RRF 255
Cdd:COG4913    737 EAA 739
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 148-260 9.76e-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: 43.98  E-value: 9.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 148 VRYLQVSRQFQEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKT 227
Cdd:COG4942   135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2496213732 228 KENLKTEEERRRDLDQRLTSTRETLRRFFSDSS 260
Cdd:COG4942   215 LAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 274-373 1.08e-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: 41.45  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 274 RCFYISHTLGSLEESQKYCTSLSSKLAAFDEPSKYYYevslpsgLEELLDRSKS--YWI-----QMSKKWR--------- 337
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDF-------LASLLKKSSSsdVWIglndlSSEGTWKwsdgsplvd 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2496213732 338 -------QDSDSQSRHCVRIKTYYQ-KWERTisKCAELHPCICE 373
Cdd:cd00037    74 ytnwapgEPNPGGSEDCVVLSSSSDgKWNDV--SCSSKLPFICE 115
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 169-254 1.53e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 169 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTST 248
Cdd:COG3883   125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204


                  ....*.
gi 2496213732 249 RETLRR 254
Cdd:COG3883   205 LAAAEA 210
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 170-245 2.66e-04

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


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 39.47  E-value: 2.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2496213732 170 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRL 245
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDELVERW 76
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 180-254 2.70e-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: 2.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2496213732 180 SQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETLRR 254
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
165-252 2.78e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 165 EATNSSLQQ------QLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERR 238
Cdd:COG4372    83 EELNEQLQAaqaelaQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162

                          90
                  ....*....|....
gi 2496213732 239 RDLDQRLTSTRETL 252
Cdd:COG4372   163 QEELAALEQELQAL 176
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 264-372 3.50e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 40.62  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 264 CPCGWIPYQERCFYISHTLGSLEESQKYCTSLSSKLAAFDEPSKYYYEVSLPSGleelldrsKSYWIQMSKKWRQDSDSQ 343
Cdd:PHA03097   46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGG--------QDLWIGIEKKKGDDDDRE 117

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2496213732 344 SRHCVRIK------TYYQKWERTISKCAELHPCIC 372
Cdd:PHA03097  118 VLDKVVKPpksgkcAYLKDKTIISSNCNATKGWIC 152
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
151-254 3.55e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  151 LQVSRQFQEGTRIWEA-----TNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTH-----EDAEQQLQAC 220
Cdd:COG4913    271 LAELEYLRAALRLWFAqrrleLLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERL 350

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2496213732  221 QAERAKTKENLKTEEERRRDLDQRLTSTRETLRR 254
Cdd:COG4913    351 ERELEERERRRARLEALLAALGLPLPASAEEFAA 384
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 171-250 5.75e-04

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


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 39.10  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 171 LQQQLREKISQLGQKEVELQK---ARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENL----KTEEERRRDLDQ 243
Cdd:pfam18595  31 VEKDLRSCIKLLEEIEAELAKleeAKKKLKELRDALEEKEIELRELERREERLQRQLENAQEKLerlrEQAEEKREAAQA 110


                  ....*..
gi 2496213732 244 RLTSTRE 250
Cdd:pfam18595 111 RLEELRE 117
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
173-254 6.91e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 173 QQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQ--AERAKTKENLKTEEERRRDLDQRLTSTRE 250
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160


                  ....
gi 2496213732 251 TLRR 254
Cdd:COG4717   161 LEEE 164
mukB PRK04863
chromosome partition protein MukB;
166-253 7.06e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 7.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  166 ATNSSLQQQLREKisqLGQKEVELQKARKELISSQDTLQE--------------KQRTHEDAEQQLQ-----ACQ--AER 224
Cdd:PRK04863   981 AKNSDLNEKLRQR---LEQAEQERTRAREQLRQAQAQLAQynqvlaslkssydaKRQMLQELKQELQdlgvpADSgaEER 1057

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2496213732  225 AKTK-----ENLKTEEERRRDLDQRLTSTRETLR 253
Cdd:PRK04863  1058 ARARrdelhARLSANRSRRNQLEKQLTFCEAEMD 1091
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 151-247 7.28e-04

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: 41.65  E-value: 7.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 151 LQVSRQFQEGTRIWEATNSSLQQQLREKISQLGQK-----------EVELQKARKELISSQDTLQEKQRTHEDAEQQLQA 219
Cdd:pfam05557  78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNElselrrqiqraELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157

                          90       100
                  ....*....|....*....|....*...
gi 2496213732 220 CQaerAKTKEnLKTEEERRRDLDQRLTS 247
Cdd:pfam05557 158 LE---KQQSS-LAEAEQRIKELEFEIQS 181
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-253 8.23e-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: 41.58  E-value: 8.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  165 EATNSSLQQQ------LREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERR 238
Cdd:TIGR02168  666 AKTNSSILERrreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90
                   ....*....|....*
gi 2496213732  239 RDLDQRLTSTRETLR 253
Cdd:TIGR02168  746 EERIAQLSKELTELE 760
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 284-373 8.91e-04

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 38.61  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 284 SLEESQKYCTSLSSKLAAFDEPSKYYYEVSLpsgleeLLDRSKSYWI-----QMSKKWR---------------QDSDSQ 343
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSST------LKKSNKYFWIgltdrKNEGTWKwvdgspvnytnwapePNNNGE 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 2496213732 344 SRHCVRIKTYYQKWErtISKCAELHPCICE 373
Cdd:pfam00059  77 NEDCVELSSSSGKWN--DENCNSKNPFVCE 104
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
173-254 9.53e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 9.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 173 QQLREKISQLGQKEVELQKARKELISSQDTLqEKQRTHEDAEQQLQACQAERAKTK---ENLKTEEERRRDLDQRLTSTR 249
Cdd:COG4717    91 AELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPerlEELEERLEELRELEEELEELE 169


                  ....*
gi 2496213732 250 ETLRR 254
Cdd:COG4717   170 AELAE 174
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 264-373 9.83e-04

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


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 38.89  E-value: 9.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 264 CPCGWIPYQERCFYISHTLGSLEESQKYCTSL--SSKLAAFDEPSKYYYEVSLPS-----------GLEELLDRSKSYWI 330
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISsyqkayqpvwiGLHDPQQSRGWEWS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2496213732 331 QMSKK----WRQDSDSQSR-HCVRI--KTYYQKWERtiSKCAELHPCICE 373
Cdd:cd03594    81 DGSKLdyrsWDRNPPYARGgYCAELsrSTGFLKWND--ANCEERNPFICK 128
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
152-249 9.99e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 152 QVSRQFQEGTRIWEATNSSLQQ------QLREKISQLGQKEVELQKARKELISSQDTLQEKQrthEDAEQQLQACQAERA 225
Cdd:COG4372    84 ELNEQLQAAQAELAQAQEELESlqeeaeELQEELEELQKERQDLEQQRKQLEAQIAELQSEI---AEREEELKELEEQLE 160

                          90       100
                  ....*....|....*....|....
gi 2496213732 226 KTKENLKTEEERRRDLDQRLTSTR 249
Cdd:COG4372   161 SLQEELAALEQELQALSEAEAEQA 184
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-250 1.03e-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: 41.20  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  171 LQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRE 250
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
149-255 1.25e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 149 RYLQVSRQFQEG-TRIWEATNSSLQQQLREKISQLGQKEVEL-----------QKARKELISSQDTL-QEKQRTHEDAEQ 215
Cdd:COG3206   241 RLAALRAQLGSGpDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpdvIALRAQIAALRAQLqQEAQRILASLEA 320

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2496213732 216 QLQACQAERAKTKENLKTEEERR----------RDLDQRLTSTRETLRRF 255
Cdd:COG3206   321 ELEALQAREASLQAQLAQLEARLaelpeleaelRRLEREVEVARELYESL 370
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 173-249 1.26e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 1.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496213732 173 QQLREKISQLGQKEVELQKARKELissQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTR 249
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAEL---EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 169-241 1.49e-03

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


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 39.65  E-value: 1.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2496213732 169 SSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTE-----EERRRDL 241
Cdd:cd07596   113 ADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEISERLKEElkrfhEERARDL 190
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-262 1.89e-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: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  165 EATNSSLQQqLREKISQLGQKEVELQKARKELISSQDTLQEKqrtHEDAEQQLQACQAERAKTKEnlKTEEERRRDLDQR 244
Cdd:COG4913    681 DASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAED--LARLELRALLEER 754

                           90       100
                   ....*....|....*....|...
gi 2496213732  245 L-----TSTRETLRRFFSDSSDT 262
Cdd:COG4913    755 FaaalgDAVERELRENLEERIDA 777
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 166-254 2.01e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 166 ATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRL 245
Cdd:COG4942    13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92


                  ....*....
gi 2496213732 246 TSTRETLRR 254
Cdd:COG4942    93 AELRAELEA 101
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-254 2.28e-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: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  175 LREKISQLGQkEVELQKARKELISSQDTLQE--KQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTRETL 252
Cdd:COG4913    247 AREQIELLEP-IRELAERYAAARERLAELEYlrAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325


                   ..
gi 2496213732  253 RR 254
Cdd:COG4913    326 DE 327
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
171-250 2.59e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 171 LQQQLREKISQLGQKEVELQKARKEL-ISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTR 249
Cdd:COG4717   161 LEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240


                  .
gi 2496213732 250 E 250
Cdd:COG4717   241 L 241
PRK12704 PRK12704
phosphodiesterase; Provisional
 172-234 2.79e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 2.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2496213732 172 QQQLREKISQLGQKEVELQKARKELISSQDTLQEKQ----RTHEDAEQQLQAC---QAERAK------TKENLKTE 234
Cdd:PRK12704   95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEeeleELIEEQLQELERIsglTAEEAKeillekVEEEARHE 170
PRK12704 PRK12704
phosphodiesterase; Provisional
 173-254 3.32e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 173 QQLREKISQ-LGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLkteEERRRDLDQRLTSTRET 251
Cdd:PRK12704   67 HKLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL---EKKEEELEELIEEQLQE 143


                  ...
gi 2496213732 252 LRR 254
Cdd:PRK12704  144 LER 146
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 164-244 4.00e-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: 37.18  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  164 WEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRthEDAEQQLQacqaerAKTKENLKTEEERRRDLDQ 243
Cdd:smart00935  16 GKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAR--EKKEKELQ------KKVQEFQRKQQKLQQDLQK 87


                   .
gi 2496213732  244 R 244
Cdd:smart00935  88 R 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-255 5.10e-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: 5.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  170 SLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQRLTSTR 249
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907


                   ....*.
gi 2496213732  250 ETLRRF 255
Cdd:TIGR02168  908 SKRSEL 913
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 155-254 5.12e-03

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


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 37.60  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 155 RQFQEGTRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISS--------QDTLQEKQRTHEDAEQQLQACQAERAK 226
Cdd:pfam08614  10 NRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSleqllaqlREELAELYRSRGELAQRLVDLNEELQE 89

                          90       100
                  ....*....|....*....|....*...
gi 2496213732 227 TKENLKTEEERRRDLDQRLTSTRETLRR 254
Cdd:pfam08614  90 LEKKLREDERRLAALEAERAQLEEKLKD 117
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 173-258 7.06e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 38.34  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 173 QQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHE----DAEQQLQACqAERAKTKE---------------NLKT 233
Cdd:pfam07888  90 RQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEarirELEEDIKTL-TQRVLEREtelermkerakkagaQRKE 168

                          90       100
                  ....*....|....*....|....*
gi 2496213732 234 EEERRRDLDQRLTSTRETLRRFFSD 258
Cdd:pfam07888 169 EEAERKQLQAKLQQTEEELRSLSKE 193
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 150-223 7.28e-03

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: 37.12  E-value: 7.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2496213732 150 YLQVSRQFQEGTRIWEATNSSLQQQLREKISQLGQK-----EVELQKARKELISSQDTLQEKQRtheDAEQQLQACQAE 223
Cdd:COG2825    41 GKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEaatlsEEERQKKERELQKKQQELQRKQQ---EAQQDLQKRQQE 116
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 165-251 7.40e-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: 38.46  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 165 EATNSSLQQQLREKisqlgqkEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 244
Cdd:TIGR04523 355 ESENSEKQRELEEK-------QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427


                  ....*..
gi 2496213732 245 LTSTRET 251
Cdd:TIGR04523 428 IERLKET 434
HIP1_clath_bdg pfam16515
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ...
 148-225 7.97e-03

Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.


Pssm-ID: 465154 [Multi-domain]  Cd Length: 99  Bit Score: 35.76  E-value: 7.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 148 VRYLQVSRQFQEG--------TRIWEATNSSLQQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQA 219
Cdd:pfam16515  12 TKQLTVAQQAQEEverekkqlEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQSGSQLSSQLAA 91


                  ....*.
gi 2496213732 220 CQAERA 225
Cdd:pfam16515  92 LQAEKE 97
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 172-254 8.94e-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: 38.13  E-value: 8.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732  172 QQQLREKISQLGQKEVELQKARKELISSQDTLQEKQRTH----EDAEQQLQACQAER-------AKTKENLKTEEERRRD 240
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnaaiAGIEAKINELEEEKedkaleiKKQEWKLEQLAADLSK 466

                           90
                   ....*....|....
gi 2496213732  241 LDQRLTSTRETLRR 254
Cdd:TIGR02169  467 YEQELYDLKEEYDR 480
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
169-245 9.06e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 169 SSLQQQLREKISQL----GQKEVELQKARKELISSQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRRDLDQR 244
Cdd:COG4717    45 AMLLERLEKEADELfkpqGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124


                  .
gi 2496213732 245 L 245
Cdd:COG4717   125 L 125
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 173-254 9.60e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.21  E-value: 9.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 173 QQLREKISQLGQKEVELQKARKELissQDTLQEKQRTHEDAEQQLQACQAERAKTKENLKTEEERRR--------DLDQR 244
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEEL---EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaereelaaKIPPE 175

                          90
                  ....*....|
gi 2496213732 245 LTSTRETLRR 254
Cdd:COG1579   176 LLALYERIRK 185
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
169-254 9.71e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496213732 169 SSLQQQLRE----------KISQLGQKEVELQKARKELISSQDTLQEKQRTH--------EDAEQQLQACQAERAKTKEN 230
Cdd:COG4717   135 EALEAELAElperleeleeRLEELRELEEELEELEAELAELQEELEELLEQLslateeelQDLAEELEELQQRLAELEEE 214

                          90       100
                  ....*....|....*....|....
gi 2496213732 231 LKTEEERRRDLDQRLTSTRETLRR 254
Cdd:COG4717   215 LEEAQEELEELEEELEQLENELEA 238
 
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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