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Conserved domains on  [gi|73621339|sp|O70156|]
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RecName: Full=Oxidized low-density lipoprotein receptor 1; Short=Ox-LDL receptor 1; AltName: Full=Lectin-like oxidized LDL receptor 1; Short=LOX-1; Short=Lectin-like oxLDL receptor 1; AltName: Full=Lectin-type oxidized LDL receptor 1; Contains: RecName: Full=Oxidized low-density lipoprotein receptor 1, soluble form

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10132518)

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
PubMed:  16336259|10508765
SCOP:  4002453

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
235-356 2.60e-34

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: 122.44  E-value: 2.60e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 235 CPQDWIWHKENCYLFH-GPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHStsPFWMGLHRKNPNHPWLWENGSPL 313
Cdd:cd03593   1 CPKDWICYGNKCYYFSmEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS--SYWIGLSREKSEKPWKWIDGSPL 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 73621339 314 SFQFFRTRgvslqMYSSGTCAYIQGGVVFAENCILTAFSICQK 356
Cdd:cd03593  79 NNLFNIRG-----STKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
55-229 1.78e-10

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: 62.65  E-value: 1.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  55 QQTQLLQVSDLLKQYQA---NLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQE 131
Cdd:COG1196 272 LRLELEELELELEEAQAeeyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 132 ALQRAVNASEESKWELKEQIDilnwKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQ 211
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEA----ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
                       170
                ....*....|....*...
gi 73621339 212 EELLQQNQNLQEALQRAA 229
Cdd:COG1196 428 EALAELEEEEEEEEEALE 445
 
Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
235-356 2.60e-34

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: 122.44  E-value: 2.60e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 235 CPQDWIWHKENCYLFH-GPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHStsPFWMGLHRKNPNHPWLWENGSPL 313
Cdd:cd03593   1 CPKDWICYGNKCYYFSmEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS--SYWIGLSREKSEKPWKWIDGSPL 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 73621339 314 SFQFFRTRgvslqMYSSGTCAYIQGGVVFAENCILTAFSICQK 356
Cdd:cd03593  79 NNLFNIRG-----STKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
235-355 3.29e-23

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: 93.43  E-value: 3.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    235 CPQDWIWHKENCYLFHG-PFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHSTSP--FWMGLHRKNPNHPWLWENGS 311
Cdd:smart00034   1 CPSGWISYGGKCYKFSTeKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 73621339    312 PL-SFQFFRTRGVSlqmYSSGTCAYIQ--GGVVFAENCILTAFSICQ 355
Cdd:smart00034  81 GPvSYSNWAPGEPN---NSSGDCVVLStsGGKWNDVSCTSKLPFVCE 124
PHA02642 PHA02642
C-type lectin-like protein; Provisional
235-336 3.46e-12

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 65.14  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  235 CPQDWIWHKENCYLF-HGPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQatSHSTSPFWMGLHRKNPNHPWLWENGSPL 313
Cdd:PHA02642  88 CPKGWIGFGYKCFYFsEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKR--YKDSSDHWIGLNRESSNHPWKWADNSNY 165
                         90       100
                 ....*....|....*....|...
gi 73621339  314 SFQFFRTrgvslqmySSGTCAYI 336
Cdd:PHA02642 166 NASFVIT--------GTGECAYL 180
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
254-356 3.98e-11

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 59.41  E-value: 3.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   254 NWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHSTSPFWMGLHRKNPNHPWLWENGSPLSFQFFRTRGVSLQmySSGTC 333
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG--ENEDC 80
                          90       100
                  ....*....|....*....|....*
gi 73621339   334 AYIQG--GVVFAENCILTAFSICQK 356
Cdd:pfam00059  81 VELSSssGKWNDENCNSKNPFVCEK 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
55-229 1.78e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 1.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  55 QQTQLLQVSDLLKQYQA---NLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQE 131
Cdd:COG1196 272 LRLELEELELELEEAQAeeyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 132 ALQRAVNASEESKWELKEQIDilnwKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQ 211
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEA----ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
                       170
                ....*....|....*...
gi 73621339 212 EELLQQNQNLQEALQRAA 229
Cdd:COG1196 428 EALAELEEEEEEEEEALE 445
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-230 7.63e-10

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: 60.46  E-value: 7.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     80 LEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEEskweLKEQIDIlnwkln 159
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----LEQQKQI------ 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    160 gISKEQKELLQQNQNLQEALQKAEKYSEESQR----------ELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAA 229
Cdd:TIGR02168  307 -LRERLANLERQLEELEAQLEELESKLDELAEelaeleekleELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                   .
gi 73621339    230 N 230
Cdd:TIGR02168  386 S 386
PRK12704 PRK12704
phosphodiesterase; Provisional
77-211 1.12e-08

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 56.32  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   77 DHILEgqmSAQKKAENASQESKRELKEQIDTLTWKL----NEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQID 152
Cdd:PRK12704  41 KRILE---EAKKEAEAIKKEALLEAKEEIHKLRNEFekelRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 73621339  153 ILNWKLNGISKEQKELlqqNQNLQEALQKAEKYSEESQRELKEQIdtLSwKLNEKSKEQ 211
Cdd:PRK12704 118 ELEQKQQELEKKEEEL---EELIEEQLQELERISGLTAEEAKEIL--LE-KVEEEARHE 170
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
51-219 1.38e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.02  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    51 TLIVQQTQLLQVSDLLKQYQANLT-------QQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLL 123
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQELIfllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   124 QQNQNLqeaLQRAVNASEESKwelKEQIDILNWKlngisKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWK 203
Cdd:pfam05483 499 LENKEL---TQEASDMTLELK---KHQEDIINCK-----KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
                         170       180
                  ....*....|....*....|.
gi 73621339   204 L-----NEKSKEQEELLQQNQ 219
Cdd:pfam05483 568 LdkseeNARSIEYEVLKKEKQ 588
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
112-227 1.24e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.25  E-value: 1.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 112 LNEKSKEQEKLLQQNQNLQEALQRAvnASEESKWELKEQidilnwklngiskEQKELLQQNQNLQEALQKAEKYSEESQR 191
Cdd:cd16269 176 LQSKEAEAEAILQADQALTEKEKEI--EAERAKAEAAEQ-------------ERKLLEEQQRELEQKLEDQERSYEEHLR 240
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 73621339 192 ELKE--------QIDTLSWKLNEKSKEQEELLQQNQNLQ-EALQR 227
Cdd:cd16269 241 QLKEkmeeerenLLKEQERALESKLKEQEALLEEGFKEQaELLQE 285
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
123-231 4.13e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.85  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    123 LQQNQNLQEALQRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSW 202
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQ 218
                           90       100
                   ....*....|....*....|....*....
gi 73621339    203 KLNEKSKEQEELLQQNQNLQEALQRAANS 231
Cdd:smart00787 219 EIMIKVKKLEELEEELQELESKIEDLTNK 247
 
Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
235-356 2.60e-34

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: 122.44  E-value: 2.60e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 235 CPQDWIWHKENCYLFH-GPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHStsPFWMGLHRKNPNHPWLWENGSPL 313
Cdd:cd03593   1 CPKDWICYGNKCYYFSmEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS--SYWIGLSREKSEKPWKWIDGSPL 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 73621339 314 SFQFFRTRgvslqMYSSGTCAYIQGGVVFAENCILTAFSICQK 356
Cdd:cd03593  79 NNLFNIRG-----STKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
235-355 3.29e-23

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: 93.43  E-value: 3.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    235 CPQDWIWHKENCYLFHG-PFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHSTSP--FWMGLHRKNPNHPWLWENGS 311
Cdd:smart00034   1 CPSGWISYGGKCYKFSTeKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 73621339    312 PL-SFQFFRTRGVSlqmYSSGTCAYIQ--GGVVFAENCILTAFSICQ 355
Cdd:smart00034  81 GPvSYSNWAPGEPN---NSSGDCVVLStsGGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
245-356 7.78e-17

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: 75.73  E-value: 7.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 245 NCYLFH-GPFNWEKSRENCLSLDAQLLQISTTDDLNFVL-QATSHSTSPFWMGLHRKNPNHPWLWENGSPLsFQFFRTRG 322
Cdd:cd00037   1 SCYKFStEKLTWEEAQEYCRSLGGHLASIHSEEENDFLAsLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPL-VDYTNWAP 79
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 73621339 323 VSLQMYSSGTCAYI---QGGVVFAENCILTAFSICQK 356
Cdd:cd00037  80 GEPNPGGSEDCVVLsssSDGKWNDVSCSSKLPFICEK 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
235-314 6.52e-14

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: 67.71  E-value: 6.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 235 CPQDWIWHKENCYLF-HGPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHSTSpFWMGLHRKNPNHPWLWENGSPL 313
Cdd:cd03590   1 CPTNWKSFQSSCYFFsTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS-YWIGLSDEETEGEWKWVDGTPL 79

                .
gi 73621339 314 S 314
Cdd:cd03590  80 N 80
PHA02642 PHA02642
C-type lectin-like protein; Provisional
235-336 3.46e-12

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 65.14  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  235 CPQDWIWHKENCYLF-HGPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQatSHSTSPFWMGLHRKNPNHPWLWENGSPL 313
Cdd:PHA02642  88 CPKGWIGFGYKCFYFsEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKR--YKDSSDHWIGLNRESSNHPWKWADNSNY 165
                         90       100
                 ....*....|....*....|...
gi 73621339  314 SFQFFRTrgvslqmySSGTCAYI 336
Cdd:PHA02642 166 NASFVIT--------GTGECAYL 180
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
254-356 3.98e-11

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 59.41  E-value: 3.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   254 NWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHSTSPFWMGLHRKNPNHPWLWENGSPLSFQFFRTRGVSLQmySSGTC 333
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG--ENEDC 80
                          90       100
                  ....*....|....*....|....*
gi 73621339   334 AYIQG--GVVFAENCILTAFSICQK 356
Cdd:pfam00059  81 VELSSssGKWNDENCNSKNPFVCEK 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
55-229 1.78e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 1.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  55 QQTQLLQVSDLLKQYQA---NLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQE 131
Cdd:COG1196 272 LRLELEELELELEEAQAeeyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 132 ALQRAVNASEESKWELKEQIDilnwKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQ 211
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEA----ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
                       170
                ....*....|....*...
gi 73621339 212 EELLQQNQNLQEALQRAA 229
Cdd:COG1196 428 EALAELEEEEEEEEEALE 445
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-230 7.63e-10

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: 60.46  E-value: 7.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     80 LEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEEskweLKEQIDIlnwkln 159
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----LEQQKQI------ 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    160 gISKEQKELLQQNQNLQEALQKAEKYSEESQR----------ELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAA 229
Cdd:TIGR02168  307 -LRERLANLERQLEELEAQLEELESKLDELAEelaeleekleELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                   .
gi 73621339    230 N 230
Cdd:TIGR02168  386 S 386
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
41-231 1.61e-09

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: 58.62  E-value: 1.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  41 LAILCLVLSVTLIVQQTQLLQVSDLLKQYQANLTQqdhiLEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQE 120
Cdd:COG4942   4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 121 KLLQQNQNLQEALQRAVNASEESKWELKEQI---------DILNWKLNGISKEQ--------KELLQQNQNLQEALQKAE 183
Cdd:COG4942  80 ALEAELAELEKEIAELRAELEAQKEELAELLralyrlgrqPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADL 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 73621339 184 KYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAANS 231
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-230 9.28e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 9.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  64 DLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAV---NAS 140
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrREL 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 141 EESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTL-----SWK---------LNE 206
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeaeeELEelaeelleaLRA 394
                       170       180
                ....*....|....*....|....
gi 73621339 207 KSKEQEELLQQNQNLQEALQRAAN 230
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLER 418
PRK12704 PRK12704
phosphodiesterase; Provisional
77-211 1.12e-08

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 56.32  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   77 DHILEgqmSAQKKAENASQESKRELKEQIDTLTWKL----NEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQID 152
Cdd:PRK12704  41 KRILE---EAKKEAEAIKKEALLEAKEEIHKLRNEFekelRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 73621339  153 ILNWKLNGISKEQKELlqqNQNLQEALQKAEKYSEESQRELKEQIdtLSwKLNEKSKEQ 211
Cdd:PRK12704 118 ELEQKQQELEKKEEEL---EELIEEQLQELERISGLTAEEAKEIL--LE-KVEEEARHE 170
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
66-231 1.69e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  66 LKQYQANLTQ-QDHI--LEGQMSA-QKKAENAsqESKRELKEQIDT-------LTWK-LNEKSKEQEKLLQQNQNLQEAL 133
Cdd:COG1196 181 LEATEENLERlEDILgeLERQLEPlERQAEKA--ERYRELKEELKEleaelllLKLReLEAELEELEAELEELEAELEEL 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 134 QRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAE---KYSEESQRELKEQIDTLSWKLNEKSKE 210
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEE 338
                       170       180
                ....*....|....*....|.
gi 73621339 211 QEELLQQNQNLQEALQRAANS 231
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAE 359
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
235-315 2.71e-08

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: 51.99  E-value: 2.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 235 CPQDWIWHKENCY-LFHGPFNWEKSRENCLSL--DAQLLQISTTDDLNFV---LQATSHSTSPFWMGLHRKNPNHPWLWE 308
Cdd:cd03594   1 CPKGWLPYKGNCYgYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIaslISSYQKAYQPVWIGLHDPQQSRGWEWS 80

                ....*..
gi 73621339 309 NGSPLSF 315
Cdd:cd03594  81 DGSKLDY 87
PRK09039 PRK09039
peptidoglycan -binding protein;
41-222 4.65e-08

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 54.20  E-value: 4.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   41 LAILCLVLSVTLIVQQtqllqvsdLLKQyqaNLTQQDHILE---GQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSK 117
Cdd:PRK09039  27 LLVIMFLLTVFVVAQF--------FLSR---EISGKDSALDrlnSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  118 EQEKLlqqnQNLQEALQRAVNASEESKWELKEQIDilnwKLNGISKE---QKELLQQN--------QNLQEALQKAEKYS 186
Cdd:PRK09039  96 ERSRL----QALLAELAGAGAAAEGRAGELAQELD----SEKQVSARalaQVELLNQQiaalrrqlAALEAALDASEKRD 167
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 73621339  187 EESQRelkeQIDTLSWKLNEKskeqeeLLQQNQNLQ 222
Cdd:PRK09039 168 RESQA----KIADLGRRLNVA------LAQRVQELN 193
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
55-229 8.41e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 8.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  55 QQTQLLQVSDLLKQYQANLTQQDHILEG---QMSAQKKAENASQESKRELKEQIDTLTwklNEKSKEQEKLLQQNQNLQE 131
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEElrlELEELELELEEAQAEEYELLAELARLE---QDIARLEERRRELEERLEE 320
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 132 ALQRAVNASEESKwELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDtlswKLNEKSKEQ 211
Cdd:COG1196 321 LEEELAELEEELE-ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE----ELLEALRAA 395
                       170
                ....*....|....*...
gi 73621339 212 EELLQQNQNLQEALQRAA 229
Cdd:COG1196 396 AELAAQLEELEEAEEALL 413
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
64-228 8.58e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 8.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   64 DLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQIDtltwklNEKSKEQEKLLQQNQNLQEALQRAVNASEEs 143
Cdd:COG4913  291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR------GNGGDRLEQLEREIERLERELEERERRRAR- 363
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  144 kweLKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQE 223
Cdd:COG4913  364 ---LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440

                 ....*
gi 73621339  224 ALQRA 228
Cdd:COG4913  441 RLLAL 445
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
48-227 1.62e-07

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: 53.14  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     48 LSVTLIVQQTQLLQVSDLLKQYQANLTQqdhiLEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQ 127
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEE----LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    128 NLQEALQ---RAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKY-----SEESQRELKEQIDT 199
Cdd:TIGR02168  376 ELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeLEELEEELEELQEE 455
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 73621339    200 LSWKLNEKSKEQEEL-------------LQQNQNLQEALQR 227
Cdd:TIGR02168  456 LERLEEALEELREELeeaeqaldaaereLAQLQARLDSLER 496
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
56-227 4.95e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 4.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  56 QTQLLQVSDLLKQYQA-----NLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQ--QNQN 128
Cdd:COG3206 188 RKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQ 267
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 129 LQEALQRAVN--ASEESKW--------ELKEQIDILNwklNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQID 198
Cdd:COG3206 268 LRAQLAELEAelAELSARYtpnhpdviALRAQIAALR---AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344
                       170       180       190
                ....*....|....*....|....*....|...
gi 73621339 199 TlswkLNEKSKEQEELLQQ----NQNLQEALQR 227
Cdd:COG3206 345 E----LPELEAELRRLEREvevaRELYESLLQR 373
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
235-337 5.03e-07

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 48.51  E-value: 5.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 235 CPQDWIWHKENCYLFhgpFN----WEKSRENCLSLD-----AQLLQISTTDDLNFVLQ-----ATSHSTSPFWMGLHRKN 300
Cdd:cd03589   1 CPTFWTAFGGYCYRF---FGdrltWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDlfessRGPDTPYGLWIGLHDRT 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 73621339 301 PNHPWLWENGSPLSFQ-----------------FFRTRGVSLQMYSSGTCAYIQ 337
Cdd:cd03589  78 SEGPFEWTDGSPVDFTkwaggqpdnyggnedcvQMWRRGDAGQSWNDMPCDAVF 131
PRK11281 PRK11281
mechanosensitive channel MscK;
56-231 5.09e-07

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 51.84  E-value: 5.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    56 QTQLLQVSDLLKQYQANLTQQDHILEGQMSAQKKAENA-SQESKRelKEQIDTLtwkLNEKSKEQEKLLQQNQNLQEALQ 134
Cdd:PRK11281  127 ESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAAlYANSQR--LQQIRNL---LKGGKVGGKALRPSQRVLLQAEQ 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   135 RAVNAseeskwelkeQIDIlnwklngiskeQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQ-EE 213
Cdd:PRK11281  202 ALLNA----------QNDL-----------QRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLsEK 260
                         170
                  ....*....|....*...
gi 73621339   214 LLQQNQNLQEALQRAANS 231
Cdd:PRK11281  261 TVQEAQSQDEAARIQANP 278
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
89-230 5.31e-07

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: 51.60  E-value: 5.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     89 KAENASQESKRELKE---QIDTLTWKLNEKSKEQEKLLQQNQNLQEAL----------QRAVNASEESKWELKEQIDILN 155
Cdd:TIGR02168  667 KTNSSILERRREIEEleeKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleelSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73621339    156 WKLNGISKEQKELLQQNQNLQEALQKAE---KYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAAN 230
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEeelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
PHA02867 PHA02867
C-type lectin protein; Provisional
230-362 5.31e-07

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 48.91  E-value: 5.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  230 NSSGPCPQDWIWHKENCYLFH-GPFNWEKSRENCLSLDAQLLQISTTDDLNFVlqaTSHSTSPFWmgLHRKNpnhpwlWE 308
Cdd:PHA02867  44 YFSKVCPDEWIGYNSKCYYFTiNETNWNDSKKLCDVMDSSLIRFDNIETLNFV---SRYGKGSYW--IDINQ------NR 112
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 73621339  309 NGSPLSFQFFrtrgvsLQMYSSGTCAYIQGGVVFAENCILTAFSICQKKANLLL 362
Cdd:PHA02867 113 KIPGINFSLY------YEQGVNDICLLFDTSNIIEMSCIFHERTICVKEDRYTH 160
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
83-228 6.62e-07

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 50.29  E-value: 6.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  83 QMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLqealqravNASEESKWELKEQIDILNWKL--NG 160
Cdd:COG1340  58 EAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAEL--------NKAGGSIDKLRKEIERLEWRQqtEV 129
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73621339 161 ISKEQ-KELLQQNQNLQEALQKAEKyseesQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRA 228
Cdd:COG1340 130 LSPEEeKELVEKIKELEKELEKAKK-----ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL 193
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
100-226 9.32e-07

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.60  E-value: 9.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  100 ELKEQIDTLTWKLNEKSKEQEkllQQNQNLQEALQRAvnasEESKWELKEQIDILNwklngiSKEQKELLQQNQNLQEAL 179
Cdd:PRK00409 513 EDKEKLNELIASLEELERELE---QKAEEAEALLKEA----EKLKEELEEKKEKLQ------EEEDKLLEEAEKEAQQAI 579
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 73621339  180 QKAEKYSEESQRELKEQIDTLSWKLNEK--SKEQEELLQQNQNLQEALQ 226
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKAHelIEARKRLNKANEKKEKKKK 628
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
43-231 1.26e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 1.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  43 ILCLVLSVTLIVQ-QTQLLQVSDLLKQYQAnltQQDHILEGQMSAQKKAENASQEsKRELKEQIDTLTWKLNEKSKEQEK 121
Cdd:COG3883   1 ALALALAAPTPAFaDPQIQAKQKELSELQA---ELEAAQAELDALQAELEELNEE-YNELQAELEALQAEIDKLQAEIAE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 122 LLQQNQNLQEALQRAVNASEESKW---------------ELKEQIDILNWklngISKEQKELLQQNQNLQEALQKAEKYS 186
Cdd:COG3883  77 AEAEIEERREELGERARALYRSGGsvsyldvllgsesfsDFLDRLSALSK----IADADADLLEELKADKAELEAKKAEL 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 73621339 187 EESQRELKEQIDTLSWK---LNEKSKEQEELLQQNQNLQEALQRAANS 231
Cdd:COG3883 153 EAKLAELEALKAELEAAkaeLEAQQAEQEALLAQLSAEEAAAEAQLAE 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
48-230 1.39e-06

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: 50.44  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     48 LSVTLIVQQTQLLQVSDLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQ 127
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    128 NLQEA------LQRAVNASEESKWELKEQIDILNWKLNgiskEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLS 201
Cdd:TIGR02168  776 ELAEAeaeieeLEAQIEQLKEELKALREALDELRAELT----LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
                          170       180
                   ....*....|....*....|....*....
gi 73621339    202 WKLNEKSKEQEELLQQNQNLQEALQRAAN 230
Cdd:TIGR02168  852 EDIESLAAEIEELEELIEELESELEALLN 880
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
25-229 1.46e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 1.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  25 GLHLLSSTWWCPAAVTLAI-LCLVLSVTLIVQQTQLLQVSDLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKE 103
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 104 QIDTLTWKLNEKSKEQEKL-LQQNQNLQEALQRAVNASEESKW-----------ELKEQIDILNWKLNGISKEQKELLQQ 171
Cdd:COG4717 345 RIEELQELLREAEELEEELqLEELEQEIAALLAEAGVEDEEELraaleqaeeyqELKEELEELEEQLEELLGELEELLEA 424
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 73621339 172 NQ--NLQEALQKAE---KYSEESQRELKEQIDTLSWKLN--EKSKEQEELLQQNQNLQEALQRAA 229
Cdd:COG4717 425 LDeeELEEELEELEeelEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELA 489
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
65-229 1.52e-06

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: 50.06  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     65 LLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQnqnlQEALQRAVNASEESK 144
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE----LEALLNERASLEEAL 889
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    145 WELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAekysEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEA 224
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQL----ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965

                   ....*
gi 73621339    225 LQRAA 229
Cdd:TIGR02168  966 DEEEA 970
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
51-225 2.37e-06

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: 49.68  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     51 TLIVQQTQLLQVSDLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQ 130
Cdd:TIGR02169  692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    131 E---ALQRAVNASEESkwELKEQIDILNWKLNGISKEQKEL----------LQQNQNLQEALQKAEKYSEESQRELKEQI 197
Cdd:TIGR02169  772 EdlhKLEEALNDLEAR--LSHSRIPEIQAELSKLEEEVSRIearlreieqkLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
                          170       180
                   ....*....|....*....|....*...
gi 73621339    198 DTLSWKLNEKSKEQEELLQQNQNLQEAL 225
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAAL 877
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
83-227 2.48e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 48.37  E-value: 2.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  83 QMSAQKKAENASQESKRELKEQIDTLTWKLNEK--SKEQEK-LLQQNQNLQEALQRAVNASEESK--WELKEQIDILNWK 157
Cdd:COG1340  96 ELRKELAELNKAGGSIDKLRKEIERLEWRQQTEvlSPEEEKeLVEKIKELEKELEKAKKALEKNEklKELRAELKELRKE 175
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73621339 158 LNGISKEQKELLQQNQNL----QEALQKAEKYSEESqRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQR 227
Cdd:COG1340 176 AEEIHKKIKELAEEAQELheemIELYKEADELRKEA-DELHKEIVEAQEKADELHEEIIELQKELRELRKELKK 248
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-230 2.86e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 2.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  100 ELKEQIDTLTWKLNEKSKEQEKL---LQQNQNLQEALQRAVNASEESK--WELKEQIDILnwklngisKEQKELLQQNQN 174
Cdd:COG4913  614 ALEAELAELEEELAEAEERLEALeaeLDALQERREALQRLAEYSWDEIdvASAEREIAEL--------EAELERLDASSD 685
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 73621339  175 LQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAAN 230
Cdd:COG4913  686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
54-225 3.05e-06

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: 49.28  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     54 VQQTQLLQVSDLLKQYQANLTQqdhiLEGQMSAQKKAENASQESKRELKEQIDTLtwklNEKSKEQEKLLQQNQNLQEAL 133
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKALREALDELRAELTLL----NEEAANLRERLESLERRIAAT 836
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    134 QRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKaekySEESQRELKEQIDTLSWKLNEKSKEQEE 213
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS----LEEALALLRSELEELSEELRELESKRSE 912
                          170
                   ....*....|..
gi 73621339    214 LLQQNQNLQEAL 225
Cdd:TIGR02168  913 LRRELEELREKL 924
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
55-230 4.10e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 4.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   55 QQTQLLQVSDLLKQYQANLTQQDhILEGQMS------AQKKAENASQESkRELKEQIDTLTWKLNEKSKEQEKLLQQNQN 128
Cdd:COG4913  250 QIELLEPIRELAERYAAARERLA-ELEYLRAalrlwfAQRRLELLEAEL-EELRAELARLEAELERLEARLDALREELDE 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  129 LQEALQRAVNASEEskwELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKS 208
Cdd:COG4913  328 LEAQIRGNGGDRLE---QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404
                        170       180
                 ....*....|....*....|..
gi 73621339  209 KEQEELLQQNQNLQEALQRAAN 230
Cdd:COG4913  405 EALAEAEAALRDLRRELRELEA 426
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
51-219 1.38e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.02  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    51 TLIVQQTQLLQVSDLLKQYQANLT-------QQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLL 123
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQELIfllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   124 QQNQNLqeaLQRAVNASEESKwelKEQIDILNWKlngisKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWK 203
Cdd:pfam05483 499 LENKEL---TQEASDMTLELK---KHQEDIINCK-----KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
                         170       180
                  ....*....|....*....|.
gi 73621339   204 L-----NEKSKEQEELLQQNQ 219
Cdd:pfam05483 568 LdkseeNARSIEYEVLKKEKQ 588
DUF4175 pfam13779
Domain of unknown function (DUF4175);
90-226 1.92e-05

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 46.52  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    90 AENASQEskrELKEQIDTLTWKLNEKSKEqekLLQQNQNLQEALQRAV--NASEESKWELKEQID-ILNWKLNGISKEQK 166
Cdd:pfam13779 503 ERGASDE---EIAKLMQELREALDDYMQA---LAEQAQQNPQDLQQPDdpNAQEMTQQDLQRMLDrIEELARSGRRAEAQ 576
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73621339   167 ELLQQNQNLQEALQKA--EKYSEESQRELKEQIDtlswKLNEKSKEQEELLQQNQNLQEALQ 226
Cdd:pfam13779 577 QMLSQLQQMLENLQAGqpQQQQQQGQSEMQQAMD----ELGDLLREQQQLLDETFRQLQQQG 634
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
64-230 2.41e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   64 DLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELK-------EQIDT--LTWKLNEKSKEQEKLLQQNQNLqEALQ 134
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswDEIDVasAEREIAELEAELERLDASSDDL-AALE 691
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  135 RAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRE-LKEQIDTLSWKLNEKsKEQEE 213
Cdd:COG4913  692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDAVER-ELREN 770
                        170
                 ....*....|....*..
gi 73621339  214 LLQQNQNLQEALQRAAN 230
Cdd:COG4913  771 LEERIDALRARLNRAEE 787
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
80-230 2.90e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   80 LEGQMSAQKKAENASQESKRELKE---QIDTLTWKLNEKSKEQEKL------LQQNQNLQEALQRAVNASEESKWELKEQ 150
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEvlrEINEISSELPELREELEKLekevkeLEELKEEIEELEKELESLEGSKRKLEEK 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  151 IDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYseesqRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAAN 230
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEY-----IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
94-214 3.48e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.59  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   94 SQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEEskwELKEQIDILNWKLNGISKEqkelLQQNQ 173
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK---EAQQAIKEAKKEADEIIKE----LRQLQ 597
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 73621339  174 NLQEALQKAEKySEESQRELKEQIDTLSWKLNEKSKEQEEL 214
Cdd:PRK00409 598 KGGYASVKAHE-LIEARKRLNKANEKKEKKKKKQKEKQEEL 637
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
83-231 4.49e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 4.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  83 QMSAQKKAENASQeSKRELKEQIDTLTWKLNEKSKEQEKLLQQN-------------QNLQEaLQRAVNASEESKWELKE 149
Cdd:COG3206 163 EQNLELRREEARK-ALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlseeaklllQQLSE-LESQLAEARAELAEAEA 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 150 QIDILNWKLNGISKEQKELLQ--QNQNLQEALQKAE-KYSEESQR---------ELKEQIDTLswkLNEKSKEQEELLQQ 217
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEaELAELSARytpnhpdviALRAQIAAL---RAQLQQEAQRILAS 317
                       170
                ....*....|....
gi 73621339 218 NQNLQEALQRAANS 231
Cdd:COG3206 318 LEAELEALQAREAS 331
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
91-195 4.68e-05

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: 45.44  E-value: 4.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     91 ENASQESKRELK---EQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQR----------AVNASEESKWELKEQIDILNWK 157
Cdd:TIGR02169  377 DKEFAETRDELKdyrEKLEKLKREINELKRELDRLQEELQRLSEELADlnaaiagieaKINELEEEKEDKALEIKKQEWK 456
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 73621339    158 LNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKE 195
Cdd:TIGR02169  457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
83-231 5.27e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 5.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  83 QMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESkwELKEQIDILNWKLNGIS 162
Cdd:COG4717  75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE--ALEAELAELPERLEELE 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 163 KEQKELLQQNQNLQEALQKAEKYSEESQR--------------ELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRA 228
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEElleqlslateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232

                ...
gi 73621339 229 ANS 231
Cdd:COG4717 233 ENE 235
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
55-225 6.66e-05

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: 43.76  E-value: 6.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  55 QQTQLLQVSDLLKQYQANLTQQDHI------LEGQMSAQKKAENASQESKRELKEQIDtltwKLNEKSKEQEKLLQQNQN 128
Cdd:COG1579   5 DLRALLDLQELDSELDRLEHRLKELpaelaeLEDELAALEARLEAAKTELEDLEKEIK----RLELEIEEVEARIKKYEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 129 LQEAlqraVNASEESKwELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKS 208
Cdd:COG1579  81 QLGN----VRNNKEYE-ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
                       170
                ....*....|....*..
gi 73621339 209 KEQEELLQQNQNLQEAL 225
Cdd:COG1579 156 AELEELEAEREELAAKI 172
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
49-223 7.36e-05

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 44.65  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    49 SVTLIVQQTQLLQVSDLLKQYQANLTQQDHI--LEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQN 126
Cdd:pfam10168 533 CLQLLSRATQVFREEYLKKHDLAREEIQKRVklLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRRC 612
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   127 ----QNLQEALQRAVNASEESKWEL---KEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIdt 199
Cdd:pfam10168 613 kkvlQRLNSQLPVLSDAEREMKKELetiNEQLKHLANAIKQAKKKMNYQRYQIAKSQSIRKKSSLSLSEKQRKTIKEI-- 690
                         170       180
                  ....*....|....*....|....
gi 73621339   200 lswkLNEKSKEQEELLQQNQNLQE 223
Cdd:pfam10168 691 ----LKQLGSEIDELIKQVKDINK 710
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
247-318 8.69e-05

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 41.64  E-value: 8.69e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73621339 247 YLF-HGPFNWEKSRENCLSLDAQLLQISTTDDLNFVLQATSHSTsPFWMGLHRKNPNHPWLWENGSPLSFQFF 318
Cdd:cd03603   3 YKFvDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYG-ASWIGASDAATEGTWKWSDGEESTYTNW 74
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
85-231 1.02e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  85 SAQKKAENASQESKRELKEQIDTLTWKLNEKSKE----QEKLLQQNQNLQEA------LQRAVNASEESKWELKEQIDIL 154
Cdd:COG4372  27 AALSEQLRKALFELDKLQEELEQLREELEQAREEleqlEEELEQARSELEQLeeeleeLNEQLQAAQAELAQAQEELESL 106
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73621339 155 NWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAANS 231
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
PRK11281 PRK11281
mechanosensitive channel MscK;
90-231 2.25e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.36  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    90 AENASQESKRELKEQIDTLT-WKLNEkskEQEKLLQQNqnLQEALQRavnaseeskwelkeqidilnwkLNGISKEQKEL 168
Cdd:PRK11281   30 ASNGDLPTEADVQAQLDALNkQKLLE---AEDKLVQQD--LEQTLAL----------------------LDKIDRQKEET 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   169 LQQNQNLQEALQKA-------EKYSEESQRELKEQIDTLSwkLNEKSKEQEELLQQNQNLQEALQrAANS 231
Cdd:PRK11281   83 EQLKQQLAQAPAKLrqaqaelEALKDDNDEETRETLSTLS--LRQLESRLAQTLDQLQNAQNDLA-EYNS 149
RNase_Y_N pfam12072
RNase Y N-terminal region;
77-201 2.57e-04

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 41.80  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    77 DHILEgqmSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNlqEALQRavnasEESkweLKEQIDILNW 156
Cdd:pfam12072  37 KRIIE---EAKKEAETKKKEALLEAKEEIHKLRAEAERELKERRNELQRQER--RLLQK-----EET---LDRKDESLEK 103
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 73621339   157 KLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELkEQIDTLS 201
Cdd:pfam12072 104 KEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-ERISGLT 147
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
81-235 2.60e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 42.68  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    81 EGQMSAqKKAENASQESKRElKEQIDTLTWKLNEKSKEQEKllqQNQNLQEALQRAVNASEESK-WELKEQIDILNWKLN 159
Cdd:pfam05262 207 ESQEDA-KRAQQLKEELDKK-QIDADKAQQKADFAQDNADK---QRDEVRQKQQEAKNLPKPADtSSPKEDKQVAENQKR 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   160 GISKEQKELLQQNQNLQEAL---------------QKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQnqnlqea 224
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKdhkafdlkqeskaseKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNED------- 354
                         170
                  ....*....|.
gi 73621339   225 lqrAANSSGPC 235
Cdd:pfam05262 355 ---AIDSSNPV 362
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
99-228 3.70e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    99 RELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAvnaseeskwelKEQIDILNWKLNGISKEQKELLQQNQNLqea 178
Cdd:pfam13851  29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKA-----------QEEVEELRKQLENYEKDKQSLKNLKARL--- 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 73621339   179 lqkaeKYSEESQRELKEQIDTLSWKLNEKSKEQEELL-QQNQNLQEALQRA 228
Cdd:pfam13851  95 -----KVLEKELKDLKWEHEVLEQRFEKVERERDELYdKFEAAIQDVQQKT 140
PHA03097 PHA03097
C-type lectin-like protein; Provisional
221-354 4.00e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 40.62  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  221 LQEALQRAANSSGPCPQDWIWHKENCYLFHGPFNWEKSR-ENCLSLDAQLLQISTTDDLNFVL---QATSHstspfWMGL 296
Cdd:PHA03097  32 LSCKLSPGDRSGLNCRSGWVGYNNKCYTFSENITNKHLAiERCADMDGILTLIDDQKEVLFVSrykGGQDL-----WIGI 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 73621339  297 HRKNPnhpwlWENGSPLSFQFFRTRGvslqmysSGTCAYIQGGVVFAENCILTAFSIC 354
Cdd:PHA03097 107 EKKKG-----DDDDREVLDKVVKPPK-------SGKCAYLKDKTIISSNCNATKGWIC 152
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
99-236 4.08e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   99 RELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQIDILNwKLNGIsKEQKELLQQNQNLQEA 178
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK-RLEEL-EERHELYEEAKAKKEE 373
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73621339  179 LQKAEK-YSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQ-------EALQRAANSSGPCP 236
Cdd:PRK03918 374 LERLKKrLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKkeikelkKAIEELKKAKGKCP 439
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
42-220 4.57e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 4.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  42 AILCLVLSVTLIVQQTQLLQVSDLLKQYQANLTQQD---HILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKE 118
Cdd:COG4372  23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAReelEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 119 QEKLLQQNQNLQ---EALQRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEK-YSEESQRELK 194
Cdd:COG4372 103 LESLQEEAEELQeelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQeLQALSEAEAE 182
                       170       180
                ....*....|....*....|....*.
gi 73621339 195 EQIDTLSWKLNEKSKEQEELLQQNQN 220
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKL 208
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
123-218 5.00e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 41.25  E-value: 5.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 123 LQQNQNLQEalqraVNASEESKWELKEQIDIlnwklngISKEQKELLQQNQNLQ---EALQKAEKYSEESQRELKEQIDT 199
Cdd:COG4026 121 LKSLQNIPE-----YNELREELLELKEKIDE-------IAKEKEKLTKENEELEselEELREEYKKLREENSILEEEFDN 188
                        90
                ....*....|....*....
gi 73621339 200 LSWKLNEKSKEQEELLQQN 218
Cdd:COG4026 189 IKSEYSDLKSRFEELLKKR 207
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
60-228 6.47e-04

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: 41.98  E-value: 6.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     60 LQVSDLLKQYQANLTQQDHIlEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKL----------------- 122
Cdd:TIGR02169  223 YEGYELLKEKEALERQKEAI-ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkekigelea 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    123 -LQQNQNLQEALQRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELkEQIDTLS 201
Cdd:TIGR02169  302 eIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL-EEVDKEF 380
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 73621339    202 WKLNEKSK-----------EQEELLQQNQNLQEALQRA 228
Cdd:TIGR02169  381 AETRDELKdyrekleklkrEINELKRELDRLQEELQRL 418
COG5022 COG5022
Myosin heavy chain [General function prediction only];
67-225 7.72e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.60  E-value: 7.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   67 KQYQANLTQQDHILEGQMSAQkkaenASQESKRELKEQIDTLT---WKLNEKSKEQEKLLQQNQNLQEALQRAVNASEES 143
Cdd:COG5022  762 RRYLQALKRIKKIQVIQHGFR-----LRRLVDYELKWRLFIKLqplLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETE 836
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  144 KWELKEQIDILN---WKLNGISKEQKELLQQNQNLQEA--LQKAEKYSEESQRE------LKEQIDTLSWKLNEKSKEQE 212
Cdd:COG5022  837 EVEFSLKAEVLIqkfGRSLKAKKRFSLLKKETIYLQSAqrVELAERQLQELKIDvksissLKLVNLELESEIIELKKSLS 916
                        170
                 ....*....|...
gi 73621339  213 ELLQQNQNLQEAL 225
Cdd:COG5022  917 SDLIENLEFKTEL 929
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
80-237 8.31e-04

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: 8.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     80 LEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQE--------------KLLQQNQNLQEALQRAVNASEESKw 145
Cdd:pfam12128  602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfartalknarldlrRLFDEKQSEKDKKNKALAERKDSA- 680
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    146 elKEQIDILNWKLNGISKEQKELLQQNQ-NLQEALQKAEKYSEESQRELKEQIDTLSwklNEKSKEQEELLQQNQNLQEA 224
Cdd:pfam12128  681 --NERLNSLEAQLKQLDKKHQAWLEEQKeQKREARTEKQAYWQVVEGALDAQLALLK---AAIAARRSGAKAELKALETW 755
                          170
                   ....*....|...
gi 73621339    225 LQRAANSSGPCPQ 237
Cdd:pfam12128  756 YKRDLASLGVDPD 768
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
67-216 8.60e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.95  E-value: 8.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    67 KQYQANLTQQDhiLEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEE---S 143
Cdd:pfam15905 171 KMKEVMAKQEG--MEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDiaqL 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   144 KWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQ-------IDTLSWKLNEKSKEQEELLQ 216
Cdd:pfam15905 249 EELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKeqtlnaeLEELKEKLTLEEQEHQKLQQ 328
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
97-177 8.72e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 40.48  E-value: 8.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  97 SKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQravnASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQ 176
Cdd:COG4026 129 EYNELREELLELKEKIDEIAKEKEKLTKENEELESELE----ELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELL 204

                .
gi 73621339 177 E 177
Cdd:COG4026 205 K 205
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
80-222 8.79e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    80 LEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKW----------ELKE 149
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikelekqlnQLKS 295
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73621339   150 QIDILN-WKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQID----TLSWKLNEKSKEQEELLQQNQNLQ 222
Cdd:TIGR04523 296 EISDLNnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkkELTNSESENSEKQRELEEKQNEIE 373
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
66-226 1.11e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.71  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  66 LKQYQANLTQ-QDHILEGQMSAQKKAENASQESKRELKEQidtltwKLNEKSKEQE----KLLQQNQNLQEALQRAVNAS 140
Cdd:COG5185 338 IQNLTAEIEQgQESLTENLEAIKEEIENIVGEVELSKSSE------ELDSFKDTIEstkeSLDEIPQNQRGYAQEILATL 411
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 141 EESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEES-----QRELKEQIDTLSWKLNEKSKEQEELL 215
Cdd:COG5185 412 EDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEEsqsrlEEAYDEINRSVRSKKEDLNEELTQIE 491
                       170
                ....*....|.
gi 73621339 216 QQNQNLQEALQ 226
Cdd:COG5185 492 SRVSTLKATLE 502
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
112-227 1.24e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.25  E-value: 1.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 112 LNEKSKEQEKLLQQNQNLQEALQRAvnASEESKWELKEQidilnwklngiskEQKELLQQNQNLQEALQKAEKYSEESQR 191
Cdd:cd16269 176 LQSKEAEAEAILQADQALTEKEKEI--EAERAKAEAAEQ-------------ERKLLEEQQRELEQKLEDQERSYEEHLR 240
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 73621339 192 ELKE--------QIDTLSWKLNEKSKEQEELLQQNQNLQ-EALQR 227
Cdd:cd16269 241 QLKEkmeeerenLLKEQERALESKLKEQEALLEEGFKEQaELLQE 285
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
101-290 1.51e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 40.55  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   101 LKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESkweLKEQIDILNWkLNGISKEQKELLQQNQNL----- 175
Cdd:PRK10246  549 LRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNIT---LQPQDDIQPW-LDAQEEHERQLRLLSQRHelqgq 624
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   176 ----QEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEEL---------LQQNQNLQEALQRAANSSGPC----PQD 238
Cdd:PRK10246  625 iaahNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLatrqqeaqsWQQRQNELTALQNRIQQLTPLletlPQS 704
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 73621339   239 WIWHKENCYLFhgPFNWEKSRENCLSLDAQL--LQISTTDDLNFVLQATSHSTS 290
Cdd:PRK10246  705 DDLPHSEETVA--LDNWRQVHEQCLSLHSQLqtLQQQDVLEAQRLQKAQAQFDT 756
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
75-244 1.79e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339     75 QQDHILEGQMSAQKKAENASQESK------RELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELK 148
Cdd:pfam15921  654 ERDQLLNEVKTSRNELNSLSEDYEvlkrnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    149 EQIDilnwklngISKEQKELLQQN-QNLQEALQKAEK---YSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQE- 223
Cdd:pfam15921  734 KQIT--------AKRGQIDALQSKiQFLEEAMTNANKekhFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEk 805
                          170       180
                   ....*....|....*....|....*..
gi 73621339    224 ------ALQRAANSSGPCpQDWIWHKE 244
Cdd:pfam15921  806 vanmevALDKASLQFAEC-QDIIQRQE 831
PRK12705 PRK12705
hypothetical protein; Provisional
37-240 1.88e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.08  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   37 AAVTLAILCLVLSVTLIvqqtqllqvsdLLKQYQANLTQQDHIL-EGQMSAQKKAENASQESK----RELKEQIDTLTWK 111
Cdd:PRK12705   7 LVILLLLIGLLLGVLVV-----------LLKKRQRLAKEAERILqEAQKEAEEKLEAALLEAKelllRERNQQRQEARRE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  112 LNEKSKEQEKLLQQNQNLQEalqRAvnaseeskwelkEQIDILNWKLngiSKEQKELLQQNQ-------NLQEALQKAEK 184
Cdd:PRK12705  76 REELQREEERLVQKEEQLDA---RA------------EKLDNLENQL---EEREKALSARELeleelekQLDNELYRVAG 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73621339  185 YSEESQR---------ELKEQIDTLSWKLNEKSKEQEELLQQNqNLQEALQRAAN--------SSGPCPQDWI 240
Cdd:PRK12705 138 LTPEQARklllklldaELEEEKAQRVKKIEEEADLEAERKAQN-ILAQAMQRIASetasdlsvSVVPIPSDAM 209
PRK11281 PRK11281
mechanosensitive channel MscK;
56-223 2.03e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.28  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    56 QTQLLQVSDLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQ----IDTLTWKLNEKSKEQEKLLQQNQNLQE 131
Cdd:PRK11281  169 SQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGntqlQDLLQKQRDYLTARIQRLEHQLQLLQE 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   132 AL-QRAVNASEESKWELKEQIDILNWKLNG-ISKEQ-------KELLQQNQNLQEALQKAEKYSE------ESQRELKEQ 196
Cdd:PRK11281  249 AInSKRLTLSEKTVQEAQSQDEAARIQANPlVAQELeinlqlsQRLLKATEKLNTLTQQNLRVKNwldrltQSERNIKEQ 328
                         170       180
                  ....*....|....*....|....*....
gi 73621339   197 IDTL--SWKLNEKSKEQEELLQQNQNLQE 223
Cdd:PRK11281  329 ISVLkgSLLLSRILYQQQQALPSADLIEG 357
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
105-234 2.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 105 IDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKWE---LKEQIDILNWKLNGISKEQKELLQQNQNLQEALQK 181
Cdd:COG4717  48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQL 127
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73621339 182 AEKYSEESQ-----RELKEQIDTLSWK---LNEKSKEQEELLQQNQNLQEALQRAANSSGP 234
Cdd:COG4717 128 LPLYQELEAleaelAELPERLEELEERleeLRELEEELEELEAELAELQEELEELLEQLSL 188
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
80-229 2.14e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 2.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  80 LEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQE---ALQRAVNASEESKWELKEQIDILNW 156
Cdd:COG1340  13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREkrdELNEKVKELKEERDELNEKLNELRE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 157 KLNGISKEQKELLQQNQN---LQEALQKAEKY------SEESQRELKEQIDtlswKLNEKSKEQEELLQQNQNLQEALQR 227
Cdd:COG1340  93 ELDELRKELAELNKAGGSidkLRKEIERLEWRqqtevlSPEEEKELVEKIK----ELEKELEKAKKALEKNEKLKELRAE 168

                ..
gi 73621339 228 AA 229
Cdd:COG1340 169 LK 170
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
117-234 2.22e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 40.04  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   117 KEQEKLLQQNQNLQEALQRAVNASEESKW----------ELKEQIDILNwKLNGISKEQKEllqqNQNL-QEALQKAEKY 185
Cdd:pfam05911 688 EEFEQLKSEKENLEVELASCTENLESTKSqlqeseqliaELRSELASLK-ESNSLAETQLK----CMAEsYEDLETRLTE 762
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 73621339   186 SEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAANSSGP 234
Cdd:pfam05911 763 LEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESS 811
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
71-221 2.77e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.12  E-value: 2.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  71 ANLTQQDHILEGQMSAQKKAENASQESkRELKEQIDTLTWKLNEKSKEQEKLLQQnqnLQEALQRAVNASEESKwELKEQ 150
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKELRAEL-KELRKEAEEIHKKIKELAEEAQELHEE---MIELYKEADELRKEAD-ELHKE 217
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73621339 151 IDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIdtlswkLNEKSKEQEELLQQNQNL 221
Cdd:COG1340 218 IVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEE------LEEKAEEIFEKLKKGEKL 282
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
72-233 3.00e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 39.45  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   72 NLTQQdhILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLqqnqNLQEALQRAVNASEESKWELKEQI 151
Cdd:PLN03229 440 KLKEQ--ILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAMGLQERLE----NLREEFSKANSQDQLMHPVLMEKI 513
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  152 DILNWKLN-GISKEQKELlqqnqNLQEALQKAEKYSE-ESQRELKEQIDTLSWKLNEKSKE---QEELLQQNQNLQEALQ 226
Cdd:PLN03229 514 EKLKDEFNkRLSRAPNYL-----SLKYKLDMLNEFSRaKALSEKKSKAEKLKAEINKKFKEvmdRPEIKEKMEALKAEVA 588

                 ....*..
gi 73621339  227 RAANSSG 233
Cdd:PLN03229 589 SSGASSG 595
PTZ00121 PTZ00121
MAEBL; Provisional
88-232 3.41e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    88 KKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQIDILNWKLN-GISKEQK 166
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRmEVDKKIK 1801
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   167 ELLQQNQNLQEALQKAEKYSEESQR----ELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAANSS 232
Cdd:PTZ00121 1802 DIFDNFANIIEGGKEGNLVINDSKEmedsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFN 1871
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
96-229 3.55e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   96 ESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQIDILNwKLNGISKEQKELLQQNQNL 175
Cdd:PRK02224 533 EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERL 611
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 73621339  176 QEAL-QKAEKYSEESQR--ELKEQIDTLSWKLNEKSkeQEELLQQNQNLQEALQRAA 229
Cdd:PRK02224 612 REKReALAELNDERRERlaEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQVE 666
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
277-354 3.88e-03

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. 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. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 36.58  E-value: 3.88e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73621339 277 DLNFVLQATSHSTSPFWMGLHRKNPNhpWLWENGSPLSFQFFRTrgvsLQMYSSGTCAYI-QGGVVFAENCILTAFSIC 354
Cdd:cd03602  34 DNALLSNLSRVSNSAAWIGLYRDVDS--WRWSDGSESSFRNWNT----FQPFGQGDCATMySSGRWYAALCSALKPFIC 106
mukB PRK04863
chromosome partition protein MukB;
53-227 3.90e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    53 IVQQTQLLQVS----DLLKQY--QANLTQQDHILEGQMSAQKKAENAsQESKRELKEQIDTLtwklnEKSKEQEKLLQQN 126
Cdd:PRK04863  860 EQQQRSQLEQAkeglSALNRLlpRLNLLADETLADRVEEIREQLDEA-EEAKRFVQQHGNAL-----AQLEPIVSVLQSD 933
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   127 QNLQEALQRAVNASEESKWELKEQIDIL---NWKLNGISKEQ-KELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSW 202
Cdd:PRK04863  934 PEQFEQLKQDYQQAQQTQRDAKQQAFALtevVQRRAHFSYEDaAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQA 1013
                         170       180
                  ....*....|....*....|....*....
gi 73621339   203 KLNEKSKEQEELLQ----QNQNLQEALQR 227
Cdd:PRK04863 1014 QLAQYNQVLASLKSsydaKRQMLQELKQE 1042
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
101-227 4.05e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.33  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    101 LKEQIDTLTwklNEKSKEQEKLLQQNQNLQEALqraVNASEESKWELKEQIDILNWKLNGIsKEQKELLQQ---NQN--- 174
Cdd:pfam15921  243 VEDQLEALK---SESQNKIELLLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSI-QSQLEIIQEqarNQNsmy 315
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73621339    175 -------------LQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQR 227
Cdd:pfam15921  316 mrqlsdlestvsqLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
123-231 4.13e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.85  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    123 LQQNQNLQEALQRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSW 202
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQ 218
                           90       100
                   ....*....|....*....|....*....
gi 73621339    203 KLNEKSKEQEELLQQNQNLQEALQRAANS 231
Cdd:smart00787 219 EIMIKVKKLEELEEELQELESKIEDLTNK 247
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
55-225 4.14e-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: 39.23  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    55 QQTQLLQVSDLLKQYQANLTQQdhilEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKL----LQQNQNLQ 130
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQK----QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLesekKEKESKIS 541
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   131 EALQRAVNASEESKWE-LKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKE---QIDTLSWKLNE 206
Cdd:TIGR04523 542 DLEDELNKDDFELKKEnLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEkekKISSLEKELEK 621
                         170
                  ....*....|....*....
gi 73621339   207 KSKEQEELLQQNQNLQEAL 225
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKSKK 640
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
64-228 4.45e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   64 DLLKQYQANLTQQDHILEGQMSAQKKAENASQesKRELKEQIDTLTW-KLNEKSKEQEKLLQQNQNLqEALQRAVNASEE 142
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKELAEQ--LKELEEKLKKYNLeELEKKAEEYEKLKEKLIKL-KGEIKSLKKELE 549
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  143 SKWELKEQIDILNWKLNGISKEQKELLQQNQN--------LQEALQKAEKYSEESQrELKEQIDTLSWKLNEKSKEQEEL 214
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeLEERLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEEL 628
                        170
                 ....*....|....
gi 73621339  215 LQQNQNLQEALQRA 228
Cdd:PRK03918 629 DKAFEELAETEKRL 642
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
99-228 5.18e-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: 37.98  E-value: 5.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  99 RELKEQIDTLTWKLNEKSKEQEKLLQQNQNLQEA---LQRAVNASEESKWELKEQIDILNWKLNGISKeQKELlqqnQNL 175
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEY----EAL 94
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 73621339 176 Q---EALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRA 228
Cdd:COG1579  95 QkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
235-319 5.78e-03

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 36.40  E-value: 5.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 235 CPQDWIWHKENCYL-FHGPFNWEKSRENCLSLDAQLLQISTTDDLNFVlqaTSHSTSPFWMGLHRKNPNHPWLWENGSPL 313
Cdd:cd03588   1 CEEGWDKFQGHCYRhFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV---NNNAQDYQWIGLNDRTIEGDFRWSDGHPL 77

                ....*.
gi 73621339 314 SFQFFR 319
Cdd:cd03588  78 QFENWR 83
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
58-225 5.80e-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: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    58 QLLQVSDLLKQYQANLTQQDHILEGQMSAQKKAENASQESKRELKEQIDTLTWKLNEKSKEQEKLLQQNQnlQEALQRAV 137
Cdd:pfam07888  91 QSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK--KAGAQRKE 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   138 NASEESKWELKEQidilnwklngisKEQKELLQQNQNLQEALQKAEKYSEESQReLKEQIDTLSWKLNE---KSKEQEEL 214
Cdd:pfam07888 169 EEAERKQLQAKLQ------------QTEEELRSLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTahrKEAENEAL 235
                         170
                  ....*....|.
gi 73621339   215 LQQNQNLQEAL 225
Cdd:pfam07888 236 LEELRSLQERL 246
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
62-195 5.80e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 38.66  E-value: 5.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   62 VSDLLKQYQANLTQQDHILEGQMSAQKKAENAS----------QESKRELKEQIDTL--TWKLNEKSKE-QEKLLQQNQN 128
Cdd:PRK04778 280 AEEKNEEIQERIDQLYDILEREVKARKYVEKNSdtlpdflehaKEQNKELKEEIDRVkqSYTLNESELEsVRQLEKQLES 359
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  129 LQEALQRAVNASEESKW---ELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQRELKE 195
Cdd:PRK04778 360 LEKQYDEITERIAEQEIaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHE 429
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
112-227 5.82e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 38.80  E-value: 5.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339    112 LNEKSKEQEKLLQQNQNLQEALQRAVNASEESKwELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAEKYSEESQR 191
Cdd:TIGR00618  158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKK-SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 73621339    192 ELKEQidtlSWKLNEKSKEQEELLQQNQNLQEALQR 227
Cdd:TIGR00618  237 QTQQS----HAYLTQKREAQEEQLKKQQLLKQLRAR 268
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
121-215 8.02e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 38.13  E-value: 8.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  121 KLLQQNQNL-QEALQR--------AVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEALQKAekyseesqR 191
Cdd:PRK05431   5 KLIRENPEAvKEALAKrgfpldvdELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEV--------K 76
                         90       100
                 ....*....|....*....|....
gi 73621339  192 ELKEQIDTLSWKLNEKSKEQEELL 215
Cdd:PRK05431  77 ELKEEIKALEAELDELEAELEELL 100
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
56-190 8.13e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.07  E-value: 8.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  56 QTQLLQVSDLLKQYQANLTQqdhiLEGQMSAQKKAENASQESK--RELKEQIDTLTWKLNEKSKE--------------- 118
Cdd:COG3206 225 ESQLAEARAELAEAEARLAA----LRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARytpnhpdvialraqi 300
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339 119 ---QEKLLQQNQNLQEALQRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQ-------QNQNLQEALQKAEKYSEE 188
Cdd:COG3206 301 aalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlerevevARELYESLLQRLEEARLA 380

                ..
gi 73621339 189 SQ 190
Cdd:COG3206 381 EA 382
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
83-229 8.25e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 38.10  E-value: 8.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339  83 QMSAQKKAENASQESKRELKEqidtltwKLNEKSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQIdilnwklngIS 162
Cdd:COG3064  46 ELEAKRQAEEEAREAKAEAEQ-------RAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAA---------AA 109
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73621339 163 KEQKELLQQNQNLQEALQKAEKYSEESQRELKEQIDTLSWKLNEKSKEQEELLQQNQNLQEALQRAA 229
Cdd:COG3064 110 AEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAA 176
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
102-217 8.55e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 37.65  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73621339   102 KEQIDTLTWKLNE---KSKEQEKLLQQNQNLQEALQRAVNASEESKWELKEQIDILNWKLNGISKEQKELLQQNQNLQEA 178
Cdd:pfam02841 154 LEERDKLEAKYNQvprKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQM 233
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 73621339   179 LQKAEKYSEESQRELKE--------QIDTLSWKLNEKSKEQEELLQQ 217
Cdd:pfam02841 234 MEAQERSYQEHVKQLIEkmeaereqLLAEQERMLEHKLQEQEELLKE 280
 
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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