NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1519316358|ref|NP_569057|]
View 

collectin-12 [Homo sapiens]

Protein Classification

CCDC158 and CLECT_DC-SIGN_like domain-containing protein( domain architecture ID 13576657)

CCDC158 and CLECT_DC-SIGN_like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
607-732 1.22e-60

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: 199.84  E-value: 1.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGRESHWIGLTDSERENEWKWLDGTSP- 685
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519316358 686 -DYKNWKAGQPDNWGHGhgpGEDCAGLIY-AGQWNDFQCEDVNNFICEK 732
Cdd:cd03590    81 sSKTFWHPGEPNNWGGG---GEDCAELVYdSGGWNDVPCNLEYRWICEK 126
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
108-442 4.18e-08

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


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 57.05  E-value: 4.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  108 LSTFRSDILDLRQQLREITEKTSKNK-----------DTLEKLQASGDALVD---RQSQLKETLENNsfLITTVNKtLQA 173
Cdd:pfam15921   80 LEEYSHQVKDLQRRLNESNELHEKQKfylrqsvidlqTKLQEMQMERDAMADirrRESQSQEDLRNQ--LQNTVHE-LEA 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  174 YNGYVTNLQQDTSVLQGNLQNQMYSHNVVIMNLNNL----------------NLTQVQQRNL---ITNLQRSVDD----- 229
Cdd:pfam15921  157 AKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeasgkkiyehdSMSTMHFRSLgsaISKILRELDTeisyl 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  230 ------TSQAIQRIKNDFQNLQQVFLQAKKDtdwlkekvqSLQTLAANNSALAKANNDTLEDMNSQLNSFTGQMENITti 303
Cdd:pfam15921  237 kgrifpVEDQLEALKSESQNKIELLLQQHQD---------RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ-- 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  304 SQANEQNLKDLQDLhKDAENRTAIKFNQLEERFQLFETDIVNIisnisytAHHLRTLTSNLNEVRTTcTDTLTKHTDDL- 382
Cdd:pfam15921  306 EQARNQNSMYMRQL-SDLESTVSQLRSELREAKRMYEDKIEEL-------EKQLVLANSELTEARTE-RDQFSQESGNLd 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  383 TSLNNTLANI--RLDSVSLRMQQ---------------DLMRSRLD---TEVANLSVIMEEMKlvDSKHGQLIKNFTILQ 442
Cdd:pfam15921  377 DQLQKLLADLhkREKELSLEKEQnkrlwdrdtgnsitiDHLRRELDdrnMEVQRLEALLKAMK--SECQGQMERQMAAIQ 454
 
Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
607-732 1.22e-60

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: 199.84  E-value: 1.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGRESHWIGLTDSERENEWKWLDGTSP- 685
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519316358 686 -DYKNWKAGQPDNWGHGhgpGEDCAGLIY-AGQWNDFQCEDVNNFICEK 732
Cdd:cd03590    81 sSKTFWHPGEPNNWGGG---GEDCAELVYdSGGWNDVPCNLEYRWICEK 126
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
607-731 5.69e-36

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: 131.95  E-value: 5.69e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQM---VGRESHWIGLTDSERENEWKWLDGT 683
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsGSSDYYWIGLSDPDSNGSWQWSDGS 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1519316358  684 SP-DYKNWKAGQPDNwghghgPGEDCAGLIYA-GQWNDFQCEDVNNFICE 731
Cdd:smart00034  81 GPvSYSNWAPGEPNN------SSGDCVVLSTSgGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
625-732 7.93e-25

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 99.47  E-value: 7.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 625 KEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGR-ESHWIGLTDSERENEWKWLDGTSPDYKNWKAgqpdnWGHGHG 703
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-----EPNNNG 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 1519316358 704 PGEDCAGLIYA-GQWNDFQCEDVNNFICEK 732
Cdd:pfam00059  76 ENEDCVELSSSsGKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
607-684 3.51e-09

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 57.43  E-value: 3.51e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519316358 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMvGRESHWIGLTDSERENEWKWLDGTS 684
Cdd:PHA02642   88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYK-DSSDHWIGLNRESSNHPWKWADNSN 164
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
108-442 4.18e-08

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: 57.05  E-value: 4.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  108 LSTFRSDILDLRQQLREITEKTSKNK-----------DTLEKLQASGDALVD---RQSQLKETLENNsfLITTVNKtLQA 173
Cdd:pfam15921   80 LEEYSHQVKDLQRRLNESNELHEKQKfylrqsvidlqTKLQEMQMERDAMADirrRESQSQEDLRNQ--LQNTVHE-LEA 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  174 YNGYVTNLQQDTSVLQGNLQNQMYSHNVVIMNLNNL----------------NLTQVQQRNL---ITNLQRSVDD----- 229
Cdd:pfam15921  157 AKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeasgkkiyehdSMSTMHFRSLgsaISKILRELDTeisyl 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  230 ------TSQAIQRIKNDFQNLQQVFLQAKKDtdwlkekvqSLQTLAANNSALAKANNDTLEDMNSQLNSFTGQMENITti 303
Cdd:pfam15921  237 kgrifpVEDQLEALKSESQNKIELLLQQHQD---------RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ-- 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  304 SQANEQNLKDLQDLhKDAENRTAIKFNQLEERFQLFETDIVNIisnisytAHHLRTLTSNLNEVRTTcTDTLTKHTDDL- 382
Cdd:pfam15921  306 EQARNQNSMYMRQL-SDLESTVSQLRSELREAKRMYEDKIEEL-------EKQLVLANSELTEARTE-RDQFSQESGNLd 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  383 TSLNNTLANI--RLDSVSLRMQQ---------------DLMRSRLD---TEVANLSVIMEEMKlvDSKHGQLIKNFTILQ 442
Cdd:pfam15921  377 DQLQKLLADLhkREKELSLEKEQnkrlwdrdtgnsitiDHLRRELDdrnMEVQRLEALLKAMK--SECQGQMERQMAAIQ 454
PRK11281 PRK11281
mechanosensitive channel MscK;
85-406 2.44e-07

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 54.53  E-value: 2.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358   85 AVESDLKKLGDQ----TGKKAISTNSE--LSTF------RSDILDLRQQLREITEKTSKNKDTLEKLQASGDA------- 145
Cdd:PRK11281    40 DVQAQLDALNKQklleAEDKLVQQDLEqtLALLdkidrqKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEetretls 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  146 ----------LVDRQSQLKETLEN----NSFLITTVNKTLQAYNGYVTN---LQQDTSVLQGNLQNQ---------MYSH 199
Cdd:PRK11281   120 tlslrqlesrLAQTLDQLQNAQNDlaeyNSQLVSLQTQPERAQAALYANsqrLQQIRNLLKGGKVGGkalrpsqrvLLQA 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  200 NVVIMNLNNLNLTQVQQRN--LITNLQRSVDDTSQAIQRIKNDFQNLQQVFLQakkdtdwlKEKVQSLQTL--AANNSAL 275
Cdd:PRK11281   200 EQALLNAQNDLQRKSLEGNtqLQDLLQKQRDYLTARIQRLEHQLQLLQEAINS--------KRLTLSEKTVqeAQSQDEA 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  276 AKANNDTL----EDMNSQLNSF-TGQMENITTISQAN-------------EQNLKD----LQ------------------ 315
Cdd:PRK11281   272 ARIQANPLvaqeLEINLQLSQRlLKATEKLNTLTQQNlrvknwldrltqsERNIKEqisvLKgslllsrilyqqqqalps 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  316 -DLHKDAENRTA-IKFNQLE---ERFQLFETDivniisniSYTAHHLRTLTSNLN-EVRTTCTDTLTKHTDDLTSLNNTL 389
Cdd:PRK11281   352 aDLIEGLADRIAdLRLEQFEinqQRDALFQPD--------AYIDKLEAGHKSEVTdEVRDALLQLLDERRELLDQLNKQL 423
                          410
                   ....*....|....*...
gi 1519316358  390 ANIRLDSVSLRM-QQDLM 406
Cdd:PRK11281   424 NNQLNLAINLQLnQQQLL 441
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
60-387 9.65e-06

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 49.28  E-value: 9.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358   60 KVVEKMDNVTG-----GMETSRQTYDDKLTAVESDLKKLgDQTGKKAISTNSELSTFRSDILDLRQQLREITEKTSKNKD 134
Cdd:TIGR01612 2048 KIKEKIDNYEKekekfGIDFDVKAMEEKFDNDIKDIEKF-ENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIK 2126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  135 TLEKLQASGDALVDRQSQLK------------ETLE----NNSFLITTVNKTLQAYNGYVTN----LQQDTSVLQGNLQ- 193
Cdd:TIGR01612 2127 IIEDKIIEKNDLIDKLIEMRkecllfsyatlvETLKskviNHSEFITSAAKFSKDFFEFIEDisdsLNDDIDALQIKYNl 2206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  194 NQMYSHNVVIM-----NLNNLNLTQVQQRNLITNLQRSVDDTSQAIQRIKNDFQNLQQVFLQAKkdtdwLKEKVQSLQTL 268
Cdd:TIGR01612 2207 NQTKKHMISILadatkDHNNLIEKEKEATKIINNLTELFTIDFNNADADILHNNKIQIIYFNSE-----LHKSIESIKKL 2281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  269 AANNSALAKANndtLEDMNSQLNSFTGQMENITTISQ----ANEQNLKDLQDLHKDAENR--------TAIKFNQLEErf 336
Cdd:TIGR01612 2282 YKKINAFKLLN---ISHINEKYFDISKEFDNIIQLQKhkltENLNDLKEIDQYISDKKNIflhalnenTNFNFNALKE-- 2356
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1519316358  337 qlfetdIVNIISNISYTAHHLRTLTSNLNEVRTTCTDTLTKHTDDLTSLNN 387
Cdd:TIGR01612 2357 ------IYDDIINRENKADEIENINNKENENIMQYIDTITKLTEKIQDILI 2401
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
77-354 7.66e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  77 QTYDDKLTAVESDLKKLG---DQTGKKAISTNSELSTFRSDILDLRQQLREITEKTSKNKDTLEKLQASGDALVDRQSQL 153
Cdd:COG4372    55 EQAREELEQLEEELEQARselEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 154 KETLENNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQNQMYSH--NVVIMNLNNLNLTQVQQRNLITNLQRSVDD-T 230
Cdd:COG4372   135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESLpR 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 231 SQAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLNSFTGQMEN-ITTISQANEQ 309
Cdd:COG4372   215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALeLEALEEAALE 294
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1519316358 310 NLKDLQDLHKDAENRTAIKFNQLEERFQLFETDIVNIISNISYTA 354
Cdd:COG4372   295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
205-377 6.90e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 38.93  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 205 NLNNLNLTQVQQRNLITNLQRSVDDTSQAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLE 284
Cdd:cd21116    64 IIGYNNTFQSYYPDLIELADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQ 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 285 DMNSQLNSFTGQMENITTISQANEQNLKDLQDlhkdaenrtaiKFNQLEERFQLFETDIVNIISNISYTAhhlrtLTSNL 364
Cdd:cd21116   144 AQVAVLNALKNQLNSLAEQIDAAIDALEKLSN-----------DWQTLDSDIKELITDLEDAESSIDAAF-----LQADL 207
                         170
                  ....*....|...
gi 1519316358 365 NEVRTTCTDTLTK 377
Cdd:cd21116   208 KAAKADWNQLYEQ 220
 
Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
607-732 1.22e-60

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: 199.84  E-value: 1.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGRESHWIGLTDSERENEWKWLDGTSP- 685
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519316358 686 -DYKNWKAGQPDNWGHGhgpGEDCAGLIY-AGQWNDFQCEDVNNFICEK 732
Cdd:cd03590    81 sSKTFWHPGEPNNWGGG---GEDCAELVYdSGGWNDVPCNLEYRWICEK 126
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
607-731 5.69e-36

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: 131.95  E-value: 5.69e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQM---VGRESHWIGLTDSERENEWKWLDGT 683
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsGSSDYYWIGLSDPDSNGSWQWSDGS 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1519316358  684 SP-DYKNWKAGQPDNwghghgPGEDCAGLIYA-GQWNDFQCEDVNNFICE 731
Cdd:smart00034  81 GPvSYSNWAPGEPNN------SSGDCVVLSTSgGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
617-732 1.07e-34

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: 127.74  E-value: 1.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 617 KCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMV--GRESHWIGLTDSERENEWKWLDGTSP-DYKNWKAG 693
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKksSSSDVWIGLNDLSSEGTWKWSDGSPLvDYTNWAPG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1519316358 694 QPDNwghghGPGEDCAGLIY--AGQWNDFQCEDVNNFICEK 732
Cdd:cd00037    81 EPNP-----GGSEDCVVLSSssDGKWNDVSCSSKLPFICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
607-730 1.90e-26

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: 105.13  E-value: 1.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 607 CPPHWKNFTDKCY-YFSVEKEiFEDAKLFCED-----KSSHLVFINTREEQQWI----KKQMVGRES--HWIGLTDSERE 674
Cdd:cd03589     1 CPTFWTAFGGYCYrFFGDRLT-WEEAELRCRSfsipgLIAHLVSIHSQEENDFVydlfESSRGPDTPygLWIGLHDRTSE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 675 NEWKWLDGTSPDYKNWKAGQPDNWGHghgpGEDCAGLIY----AGQWNDFQCEDVNNFIC 730
Cdd:cd03589    80 GPFEWTDGSPVDFTKWAGGQPDNYGG----NEDCVQMWRrgdaGQSWNDMPCDAVFPYIC 135
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
607-732 2.13e-26

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: 104.34  E-value: 2.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQmVGRESHWIGLTDSERENEWKWLDGTSpd 686
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQ-IGSSSYWIGLSREKSEKPWKWIDGSP-- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1519316358 687 yknwkagqPDNWGH--GHGPGEDCAgLIYAGQWNDFQCEDVNNFICEK 732
Cdd:cd03593    78 --------LNNLFNirGSTKSGNCA-YLSSTGIYSEDCSTKKRWICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
625-732 7.93e-25

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 99.47  E-value: 7.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 625 KEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGR-ESHWIGLTDSERENEWKWLDGTSPDYKNWKAgqpdnWGHGHG 703
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-----EPNNNG 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 1519316358 704 PGEDCAGLIYA-GQWNDFQCEDVNNFICEK 732
Cdd:pfam00059  76 ENEDCVELSSSsGKWNDENCNSKNPFVCEK 105
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
607-732 2.81e-23

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: 95.72  E-value: 2.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQmvGRESHWIGLTDSERENEWKWLDGTSPD 686
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN--AQDYQWIGLNDRTIEGDFRWSDGHPLQ 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1519316358 687 YKNWKAGQPDNWghgHGPGEDCAGLIY--AGQWNDFQCEDVNNFICEK 732
Cdd:cd03588    79 FENWRPNQPDNF---FATGEDCVVMIWheEGEWNDVPCNYHLPFTCKK 123
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
619-728 2.82e-23

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: 95.57  E-value: 2.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 619 YYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGRESHWIGLTDSERENEWKWLDGTSPDYKNWKAGQPDNW 698
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNN 82
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1519316358 699 GhghGPGEDCAGLIYA----GQWNDFQCEDVNNF 728
Cdd:cd03603    83 G---GGNEDYAAINHFpgisGKWNDLANSYNTLG 113
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
616-731 1.07e-21

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 90.82  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 616 DKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREE----QQWIKKqmvGRESHWIGLTDSERENEWKWLDGTSPDYKNWK 691
Cdd:cd03591     1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAEnaaiASYVKK---GNTYAFIGITDLETEGQFVYLDGGPLTYTNWK 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1519316358 692 AGQPDNwghgHGPGEDCAGLIYAGQWNDFQCEDVNNFICE 731
Cdd:cd03591    78 PGEPNN----AGGGEDCVEMYTSGKWNDVACNLTRLFVCE 113
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
607-731 3.99e-20

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: 86.66  E-value: 3.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 607 CPPHWKNFTDKCY-YFSVEKEiFEDAKLFCED--KSSHLVFINTREEQQ----WIKKQMVGRESHWIGLTDSERENEWKW 679
Cdd:cd03594     1 CPKGWLPYKGNCYgYFRQPLS-WSDAELFCQKygPGAHLASIHSPAEAAaiasLISSYQKAYQPVWIGLHDPQQSRGWEW 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1519316358 680 LDGTSPDYKNWKAGQPdnwghgHGPGEDCAGLI----YAgQWNDFQCEDVNNFICE 731
Cdd:cd03594    80 SDGSKLDYRSWDRNPP------YARGGYCAELSrstgFL-KWNDANCEERNPFICK 128
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
619-732 1.87e-15

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 72.79  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 619 YYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGRES--HWIGLTDseRENEWKWLD--GTSPDYKNWKAGQ 694
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLgyYWIDGND--INNEGTWVDtdKKELEYKNWAPGE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1519316358 695 PDNWGhghgpGEDCA-GLIYA-GQWNDFQCEDVNNFICEK 732
Cdd:cd03592    81 PNNGR-----NENCLeIYIKDnGKWNDEPCSKKKSAICYT 115
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
619-730 1.44e-13

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: 67.40  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 619 YYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGRESH-WIGLTDSEreNEWKWLDGTSPDYKNWKAGQPDN 697
Cdd:cd03602     3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAaWIGLYRDV--DSWRWSDGSESSFRNWNTFQPFG 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1519316358 698 wghghgpGEDCAGLIYAGQWNDFQCEDVNNFIC 730
Cdd:cd03602    81 -------QGDCATMYSSGRWYAALCSALKPFIC 106
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
620-732 2.46e-12

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.


Pssm-ID: 153071  Cd Length: 119  Bit Score: 64.09  E-value: 2.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 620 YFSVEKEIFEDAKLFCEDKSSHLVFINTR--EEQQWIK-KQMVGRESHWIGLTDSER-ENEWKWLDGTS--PDYKNWKAG 693
Cdd:cd03601     4 LCSDETMNYAKAGAFCRSRGMRLASLAMRdsEMRDAILaFTLVKGHGYWVGADNLQDgEYDFLWNDGVSlpTDSDLWAPN 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1519316358 694 QPDNwghgHGPGEDCAGLIYA-GQWNDFQCEDVNNFICEK 732
Cdd:cd03601    84 EPSN----PQSRQLCVQLWSKyNLLDDEYCGRAKRVICEK 119
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
617-731 8.29e-11

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.


Pssm-ID: 153066  Cd Length: 129  Bit Score: 60.09  E-value: 8.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 617 KCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIK---KQMVGRESH-WIGLTDSERENEWKWLDGTSPDYKNWK- 691
Cdd:cd03596    10 KCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRdyvKASVPGNWEvWLGINDMVAEGKWVDVNGSPISYFNWEr 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1519316358 692 --AGQPDNwghghGPGEDCAGLIYA--GQWNDFQCEDVNNFICE 731
Cdd:cd03596    90 eiTAQPDG-----GKRENCVALSSSaqGKWFDEDCRREKPYVCE 128
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
618-731 1.40e-10

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.


Pssm-ID: 153065  Cd Length: 149  Bit Score: 59.90  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 618 CY---YF--SVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGRESH----WIGLTDSEREN--------EWKWL 680
Cdd:cd03595    12 CYkiaYFqdSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASdgdfWIGLRRSSQYNvtssacssLYYWL 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1519316358 681 DGTSPDYKNWKAGQPDNWGHG-----HGPGEDcAGL--IYAGQWNDFQCEDVNNFICE 731
Cdd:cd03595    92 DGSISTFRNWYVDEPSCGSEVcvvmyHQPSAP-AGQggPYLFQWNDDNCNMKNNFICK 148
PHA02642 PHA02642
C-type lectin-like protein; Provisional
607-684 3.51e-09

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 57.43  E-value: 3.51e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519316358 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMvGRESHWIGLTDSERENEWKWLDGTS 684
Cdd:PHA02642   88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYK-DSSDHWIGLNRESSNHPWKWADNSN 164
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
108-442 4.18e-08

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: 57.05  E-value: 4.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  108 LSTFRSDILDLRQQLREITEKTSKNK-----------DTLEKLQASGDALVD---RQSQLKETLENNsfLITTVNKtLQA 173
Cdd:pfam15921   80 LEEYSHQVKDLQRRLNESNELHEKQKfylrqsvidlqTKLQEMQMERDAMADirrRESQSQEDLRNQ--LQNTVHE-LEA 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  174 YNGYVTNLQQDTSVLQGNLQNQMYSHNVVIMNLNNL----------------NLTQVQQRNL---ITNLQRSVDD----- 229
Cdd:pfam15921  157 AKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeasgkkiyehdSMSTMHFRSLgsaISKILRELDTeisyl 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  230 ------TSQAIQRIKNDFQNLQQVFLQAKKDtdwlkekvqSLQTLAANNSALAKANNDTLEDMNSQLNSFTGQMENITti 303
Cdd:pfam15921  237 kgrifpVEDQLEALKSESQNKIELLLQQHQD---------RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ-- 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  304 SQANEQNLKDLQDLhKDAENRTAIKFNQLEERFQLFETDIVNIisnisytAHHLRTLTSNLNEVRTTcTDTLTKHTDDL- 382
Cdd:pfam15921  306 EQARNQNSMYMRQL-SDLESTVSQLRSELREAKRMYEDKIEEL-------EKQLVLANSELTEARTE-RDQFSQESGNLd 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  383 TSLNNTLANI--RLDSVSLRMQQ---------------DLMRSRLD---TEVANLSVIMEEMKlvDSKHGQLIKNFTILQ 442
Cdd:pfam15921  377 DQLQKLLADLhkREKELSLEKEQnkrlwdrdtgnsitiDHLRRELDdrnMEVQRLEALLKAMK--SECQGQMERQMAAIQ 454
PRK11281 PRK11281
mechanosensitive channel MscK;
85-406 2.44e-07

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 54.53  E-value: 2.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358   85 AVESDLKKLGDQ----TGKKAISTNSE--LSTF------RSDILDLRQQLREITEKTSKNKDTLEKLQASGDA------- 145
Cdd:PRK11281    40 DVQAQLDALNKQklleAEDKLVQQDLEqtLALLdkidrqKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEetretls 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  146 ----------LVDRQSQLKETLEN----NSFLITTVNKTLQAYNGYVTN---LQQDTSVLQGNLQNQ---------MYSH 199
Cdd:PRK11281   120 tlslrqlesrLAQTLDQLQNAQNDlaeyNSQLVSLQTQPERAQAALYANsqrLQQIRNLLKGGKVGGkalrpsqrvLLQA 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  200 NVVIMNLNNLNLTQVQQRN--LITNLQRSVDDTSQAIQRIKNDFQNLQQVFLQakkdtdwlKEKVQSLQTL--AANNSAL 275
Cdd:PRK11281   200 EQALLNAQNDLQRKSLEGNtqLQDLLQKQRDYLTARIQRLEHQLQLLQEAINS--------KRLTLSEKTVqeAQSQDEA 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  276 AKANNDTL----EDMNSQLNSF-TGQMENITTISQAN-------------EQNLKD----LQ------------------ 315
Cdd:PRK11281   272 ARIQANPLvaqeLEINLQLSQRlLKATEKLNTLTQQNlrvknwldrltqsERNIKEqisvLKgslllsrilyqqqqalps 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  316 -DLHKDAENRTA-IKFNQLE---ERFQLFETDivniisniSYTAHHLRTLTSNLN-EVRTTCTDTLTKHTDDLTSLNNTL 389
Cdd:PRK11281   352 aDLIEGLADRIAdLRLEQFEinqQRDALFQPD--------AYIDKLEAGHKSEVTdEVRDALLQLLDERRELLDQLNKQL 423
                          410
                   ....*....|....*...
gi 1519316358  390 ANIRLDSVSLRM-QQDLM 406
Cdd:PRK11281   424 NNQLNLAINLQLnQQQLL 441
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
617-730 2.96e-07

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 49.76  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 617 KCYYFSVEKEIFEDAKLFCED-KSSHLVFI-NTREEQQWIKkqMVGRESH---WIG--LTDSERENEWKWLDGTSPDYKN 689
Cdd:cd03598     2 RCYRFVKSPRTFRDAQVICRRcYRGNLASIhSFAFNYRVQR--LVSTLNQaqvWIGgiITGKGRCRRFSWVDGSVWNYAY 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1519316358 690 WKAGQPDNwGHGHgpgedCAGL-IYAGQWNDFQCEDVNNFIC 730
Cdd:cd03598    80 WAPGQPGN-RRGH-----CVELcTRGGHWRRAHCKLRRPFIC 115
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
60-387 9.65e-06

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 49.28  E-value: 9.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358   60 KVVEKMDNVTG-----GMETSRQTYDDKLTAVESDLKKLgDQTGKKAISTNSELSTFRSDILDLRQQLREITEKTSKNKD 134
Cdd:TIGR01612 2048 KIKEKIDNYEKekekfGIDFDVKAMEEKFDNDIKDIEKF-ENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIK 2126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  135 TLEKLQASGDALVDRQSQLK------------ETLE----NNSFLITTVNKTLQAYNGYVTN----LQQDTSVLQGNLQ- 193
Cdd:TIGR01612 2127 IIEDKIIEKNDLIDKLIEMRkecllfsyatlvETLKskviNHSEFITSAAKFSKDFFEFIEDisdsLNDDIDALQIKYNl 2206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  194 NQMYSHNVVIM-----NLNNLNLTQVQQRNLITNLQRSVDDTSQAIQRIKNDFQNLQQVFLQAKkdtdwLKEKVQSLQTL 268
Cdd:TIGR01612 2207 NQTKKHMISILadatkDHNNLIEKEKEATKIINNLTELFTIDFNNADADILHNNKIQIIYFNSE-----LHKSIESIKKL 2281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  269 AANNSALAKANndtLEDMNSQLNSFTGQMENITTISQ----ANEQNLKDLQDLHKDAENR--------TAIKFNQLEErf 336
Cdd:TIGR01612 2282 YKKINAFKLLN---ISHINEKYFDISKEFDNIIQLQKhkltENLNDLKEIDQYISDKKNIflhalnenTNFNFNALKE-- 2356
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1519316358  337 qlfetdIVNIISNISYTAHHLRTLTSNLNEVRTTCTDTLTKHTDDLTSLNN 387
Cdd:TIGR01612 2357 ------IYDDIINRENKADEIENINNKENENIMQYIDTITKLTEKIQDILI 2401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
68-336 1.63e-05

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: 48.51  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358   68 VTGG---METSRQTYDDKLTAVESDLKKLGDQT--GKKAIST--------NSELSTFRSDILDLRQQLREITEKTSKNKD 134
Cdd:TIGR02168  661 ITGGsakTNSSILERRREIEELEEKIEELEEKIaeLEKALAElrkeleelEEELEQLRKELEELSRQISALRKDLARLEA 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  135 TLEKLQASGDALVDRQSQLKETLENNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQNQMYSHNVVIMNLNNLNLTQV 214
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  215 QQRNLITNLQRSVDDTSQAIQRIKN-------DFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMN 287
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEqieelseDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1519316358  288 SQLNSFTGQMenittisQANEQNLKDLQDLHKDAENRTA---IKFNQLEERF 336
Cdd:TIGR02168  901 EELRELESKR-------SELRRELEELREKLAQLELRLEgleVRIDNLQERL 945
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
616-731 1.94e-05

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 45.11  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 616 DKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKK---QMVGRESH-----WIGL-------TDSERE-NEWKW 679
Cdd:cd03600     4 DACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLllaAGPGRHGRgslrlWIGLqreprqcSDPSLPlRGFSW 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 680 LDGTSP-DYKNWKAGqpdnwGHGHGPGEDCAGLIYAGQ------WNDFQCE-DVNNFICE 731
Cdd:cd03600    84 VTGDQDtDFSNWLQE-----PAGTCTSPRCVALSAAGStpdnlkWKDGPCSaRADGYLCK 138
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
81-387 4.77e-05

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: 46.94  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  81 DKLTAVESDLKKLGDQTGKKAISTNSELSTFRSDILDLRQQLREITEKTSKNKDTLEklqasgdalvDRQSQlketLENN 160
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS----------EKQKE----LEQN 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 161 SFLITTVNKTLQAYNGYVTNLQQdtsvlqgnlQNQMYSHNVVIMNLNNLNLTQVQQRNLITNLQRSVDDTSQAIQRIKND 240
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNN---------QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 241 FQNLQQVFLQAKKDtdwLKEKVQSLQTLAANNSalakANNDTLEDMNSQLNSFTGQMENITTISQANEQNLKDLQDLHKD 320
Cdd:TIGR04523 351 LTNSESENSEKQRE---LEEKQNEIEKLKKENQ----SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 321 AENR------TAIKFNQ----LEERFQLFETDIVNIISNISYTAHHLRTLTSNLNEVRTTCTDT---LTKHTDDLTSLNN 387
Cdd:TIGR04523 424 LEKEierlkeTIIKNNSeikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkeLKSKEKELKKLNE 503
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
61-367 6.64e-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: 46.60  E-value: 6.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358   61 VVEKMDNVTGGMETSRQTYDDK---------LTAVESDLKKLGDQTGKKAISTNSELSTFRSDILDLRQQLREITEKTSK 131
Cdd:TIGR02169  648 LFEKSGAMTGGSRAPRGGILFSrsepaelqrLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  132 NKDTLEKLQASGDALVDRQSQLKETLENNSFLITTVNKTLQAyngyvtnLQQDTSVLQGNLqNQMYSHnvvimnlnnLNL 211
Cdd:TIGR02169  728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE-------LEEDLHKLEEAL-NDLEAR---------LSH 790
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  212 TQVQQrnlITNLQRSVDDTsqaIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLN 291
Cdd:TIGR02169  791 SRIPE---IQAELSKLEEE---VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519316358  292 SFTGQMENIttisQANEQNL-KDLQDLHKDAENRTAiKFNQLEERFQLFETDIVNIISNISYTAHHLRTLTSNLNEV 367
Cdd:TIGR02169  865 ELEEELEEL----EAALRDLeSRLGDLKKERDELEA-QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
77-354 7.66e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  77 QTYDDKLTAVESDLKKLG---DQTGKKAISTNSELSTFRSDILDLRQQLREITEKTSKNKDTLEKLQASGDALVDRQSQL 153
Cdd:COG4372    55 EQAREELEQLEEELEQARselEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 154 KETLENNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQNQMYSH--NVVIMNLNNLNLTQVQQRNLITNLQRSVDD-T 230
Cdd:COG4372   135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESLpR 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 231 SQAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLNSFTGQMEN-ITTISQANEQ 309
Cdd:COG4372   215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALeLEALEEAALE 294
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1519316358 310 NLKDLQDLHKDAENRTAIKFNQLEERFQLFETDIVNIISNISYTA 354
Cdd:COG4372   295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
88-442 2.42e-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: 44.63  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  88 SDLKKLGDQTGKKAIstNSELSTFRSDILDLRQQLREITEKTSKNKDTLEKLQASGDALVDRQSQLKETLENNSFLITTV 167
Cdd:TIGR04523 298 SDLNNQKEQDWNKEL--KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 168 NKTLQAYNGYVTNLQQDTSVLQGNLQNQMYSHNVVIMNLNNLNLTQVQQRNLITNLQRSVDDTSQAIQRIKNDFQNLQQV 247
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 248 FLQAKKDTDWLKEKVQSLqtlaannSALAKANNDTLEDMNSQLNSFTGQMENITTISQANEQNLKDLQDlhkdaenrtai 327
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVL-------SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK----------- 517
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 328 KFNQLEERFQLFETDIVNIISNISytahhlrTLTSNLNEVRTTCTDTLTKhtDDLTSLNNTLANIRLDSVSLRMQQDLMR 407
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKIS-------DLEDELNKDDFELKKENLE--KEIDEKNKEIEELKQTQKSLKKKQEEKQ 588
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1519316358 408 SRLDTEVANLSVIMEEMKLVDSKHGQLIKNFTILQ 442
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
59-390 2.71e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.65  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358   59 YKVVEKMDNVTGGMETSRQTYDDKLTAVESDLKKL---GDQTGKKAISTNSELSTFRSDILDLRQQLREITEKTSKNKDT 135
Cdd:TIGR00606  687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKekrRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  136 LEK-----------LQASGDALVDRQ--SQLKETLENN----------------SFLITTVNKTLQAYNGYVTNLQQDTS 186
Cdd:TIGR00606  767 IEEqetllgtimpeEESAKVCLTDVTimERFQMELKDVerkiaqqaaklqgsdlDRTVQQVNQEKQEKQHELDTVVSKIE 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  187 VLQGNLQNQMYSHNVVIMNLNNLNLTQVQqrnLITNLQRSVDDTSQAIQRIKnDFQNLQQVFLQAKK----DTDWLKEKV 262
Cdd:TIGR00606  847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQ---IGTNLQRRQQFEEQLVELST-EVQSLIREIKDAKEqdspLETFLEKDQ 922
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  263 QSLQTLAANNSALAKANNDTLEDMNSQLNSFTGQMENITTISQANeqnlKDLQDLHKDAE-NRTAIKFNQLEERFQLFET 341
Cdd:TIGR00606  923 QEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG----KDDYLKQKETElNTVNAQLEECEKHQEKINE 998
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1519316358  342 DIVNIISNISYTAHHLRTLTSNLnevrttctdTLTKHTDDLTSLNNTLA 390
Cdd:TIGR00606  999 DMRLMRQDIDTQKIQERWLQDNL---------TLRKRENELKEVEEELK 1038
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
607-699 3.25e-04

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.


Pssm-ID: 153067  Cd Length: 129  Bit Score: 41.41  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKQMVGRE------SHWIGLtdseRE---NEW 677
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQmtkqklTPWVGL----RKinvSYW 76
                          90       100
                  ....*....|....*....|....*.
gi 1519316358 678 KWLDgTSPdYKN----WKAGQPDNWG 699
Cdd:cd03597    77 CWED-MSP-FTNttlqWLPGEPSDAG 100
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
80-335 3.93e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  80 DDKLTAVESDLKKLGDQ--TGKKAISTNSELSTFRSDIL-----DLRQQLREITEKTSKNKDTLEKLQASGDALVDRQSQ 152
Cdd:COG1196   192 EDILGELERQLEPLERQaeKAERYRELKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAELEE 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 153 LKETLENNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQNQmyshnvvIMNLNNLNLTQVQQRNLITNLQRSVDDTSQ 232
Cdd:COG1196   272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEE 344
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 233 AIQRIKNDFQNLQQVFLQAKkdtdwlKEKVQSLQTLAANNSALAKANNDTLEDMNSQLNsftgQMENITTISQANEQNLK 312
Cdd:COG1196   345 ELEEAEEELEEAEAELAEAE------EALLEAEAELAEAEEELEELAEELLEALRAAAE----LAAQLEELEEAEEALLE 414
                         250       260
                  ....*....|....*....|...
gi 1519316358 313 DLQDLHKDAENRTAIKFNQLEER 335
Cdd:COG1196   415 RLERLEEELEELEEALAELEEEE 437
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
103-435 6.38e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 103 STNSELSTFRSDILDLRQQLREITEKTSKNKDTLEKLQASGDALVDRQSQLKETLENNSFLITTVNKTLQAYNGYVTNLQ 182
Cdd:COG4372    35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 183 QDTSVLQGNLQNQMYSHNVVIMNLNNLNLTQVQQRNLITNLQRSVDDTSQAIQRIKNDFQNLQQVFLQAKKDTdwlkekv 262
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE------- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 263 qslQTLAANNSALAKANNDTLEDMNSQLnsftgqmenITTISQANEQNLKDLQDLHKDAENRTAIKFNQLEERFQLFETD 342
Cdd:COG4372   188 ---LLKEANRNAEKEEELAEAEKLIESL---------PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 343 IVNIISNISYTAHHLRTLTSNLNEVRTTCTDTLTKHTDDLTSLNNTLANIRLDSVslRMQQDLMRSRLDTEVANLSVIME 422
Cdd:COG4372   256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI--GALEDALLAALLELAKKLELALA 333
                         330
                  ....*....|...
gi 1519316358 423 EMKLVDSKHGQLI 435
Cdd:COG4372   334 ILLAELADLLQLL 346
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
107-306 8.38e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 8.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 107 ELSTFR--SDILDLRQQLREITEKTSKNKDTLEKLQASGDALVDRQSQLKETLENNSFLITTV--NKTLQAYNGYVTNLQ 182
Cdd:COG3206   197 ALEEFRqkNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELE 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 183 QDTSVLQGNLQNQmysHNVVImnlnnlnltqvQQRNLITNLQRSVDD-TSQAIQRIKNDFQNLQQ--VFLQAKKDTdwLK 259
Cdd:COG3206   277 AELAELSARYTPN---HPDVI-----------ALRAQIAALRAQLQQeAQRILASLEAELEALQAreASLQAQLAQ--LE 340
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1519316358 260 EKVQSLQTLAANNSAL---AKANNDTLEDMNSQLN----SFTGQMENITTISQA 306
Cdd:COG3206   341 ARLAELPELEAELRRLereVEVARELYESLLQRLEearlAEALTVGNVRVIDPA 394
PHA02867 PHA02867
C-type lectin protein; Provisional
607-666 1.40e-03

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 40.05  E-value: 1.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKKqmVGRESHWI 666
Cdd:PHA02867   49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVSR--YGKGSYWI 106
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
128-417 2.09e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 128 KTSKNKDTLEKLQASGDALVDRQSQLkETLENNSFLITTVNKTlqayngyvtNLQQDTsvlqgnlQNQMYSHNVVIMNL- 206
Cdd:COG3206    62 EPQSSDVLLSGLSSLSASDSPLETQI-EILKSRPVLERVVDKL---------NLDEDP-------LGEEASREAAIERLr 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 207 NNLNLTQVQQRNLITnLqrSVDDTSQA-IQRIKNDF------QNLQQVFLQAKKDTDWLKEKVQSLQT-LAANNSALA-- 276
Cdd:COG3206   125 KNLTVEPVKGSNVIE-I--SYTSPDPElAAAVANALaeayleQNLELRREEARKALEFLEEQLPELRKeLEEAEAALEef 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 277 KANNDTLeDMNSQLNSFTGQMENIttisqanEQNLKDLQDLHKDAENRtaikFNQLEERFQLFETDIVNIISNISYTAhh 356
Cdd:COG3206   202 RQKNGLV-DLSEEAKLLLQQLSEL-------ESQLAEARAELAEAEAR----LAALRAQLGSGPDALPELLQSPVIQQ-- 267
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519316358 357 lrtLTSNLNEVRTTCTDTLTKHTD---DLTSLNNTLANIRldsVSLRMQQDLMRSRLDTEVANL 417
Cdd:COG3206   268 ---LRAQLAELEAELAELSARYTPnhpDVIALRAQIAALR---AQLQQEAQRILASLEAELEAL 325
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-406 2.17e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358   80 DDKLTAVESDLKKLGDQ--TGKKAISTNSELSTFRSDIL-----DLRQQLREITEKTSKNKDTLEKLQAsgdALVDRQSQ 152
Cdd:TIGR02168  192 EDILNELERQLKSLERQaeKAERYKELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTA---ELQELEEK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  153 LKET-LENNSflittVNKTLQAYNGYVTNLQQDTSVLQGNLQnqmyshnvvimnlnnlnLTQVQQRNLITNLQRsvddTS 231
Cdd:TIGR02168  269 LEELrLEVSE-----LEEEIEELQKELYALANEISRLEQQKQ-----------------ILRERLANLERQLEE----LE 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  232 QAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLNSFTG---QMEN-ITTISQAN 307
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELqIASLNNEI 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  308 EQNLKDLQDLhkdAENRTAIKFNQLEERFQLFETDIVNIISNISYTAHHLRTLTSNLNEVRT---TCTDTLTKHTDDLTS 384
Cdd:TIGR02168  403 ERLEARLERL---EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEaleELREELEEAEQALDA 479
                          330       340
                   ....*....|....*....|....
gi 1519316358  385 LNNTLA--NIRLDSVSlRMQQDLM 406
Cdd:TIGR02168  480 AERELAqlQARLDSLE-RLQENLE 502
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
111-343 2.67e-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: 41.16  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 111 FRSDILDLRQQLREITEKTSKNKDTLEKLQASgdaLVDRQSQLKETLENNSFLITTVNKtLQAYNGYVTNLQQDTSVLQG 190
Cdd:TIGR04523  73 SNNKIKILEQQIKDLNDKLKKNKDKINKLNSD---LSKINSEIKNDKEQKNKLEVELNK-LEKQKKENKKNIDKFLTEIK 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 191 NLQNQMYSHNVVIMNLNnlnltqvqqrNLITNLQRSVDDTSQAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAA 270
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLK----------KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLES 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 271 NNSALAKANN---DTLEDMNSQLNSFTGQMEN----ITTISQANEQNLKDLQDLHKDAENrTAIKFNQLEERFQLFETDI 343
Cdd:TIGR04523 219 QISELKKQNNqlkDNIEKKQQEINEKTTEISNtqtqLNQLKDEQNKIKKQLSEKQKELEQ-NNKKIKELEKQLNQLKSEI 297
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
95-298 3.32e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  95 DQTGKKAISTNSELSTFRSDILDLRQQLREITEKTSKNKDTLEKLQASGDALVDRQSQLKETLEnnsflittvnKTLQAY 174
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE----------ERREEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 175 NGYVTNLQQdtsvlQGNLQNQMyshnVVIMNLNNLN--LTQVQQRNLITNLQRS-VDDTSQAIQRIKNDFQNLQQVFLQA 251
Cdd:COG3883    89 GERARALYR-----SGGSVSYL----DVLLGSESFSdfLDRLSALSKIADADADlLEELKADKAELEAKKAELEAKLAEL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1519316358 252 KKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLNSFTGQME 298
Cdd:COG3883   160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
PHA03097 PHA03097
C-type lectin-like protein; Provisional
594-676 4.34e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 38.69  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 594 LQNEPTPAPEDN-GCPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINTREEQQWIKK-QMVGreSHWIGLTDS 671
Cdd:PHA03097   32 LSCKLSPGDRSGlNCRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRyKGGQ--DLWIGIEKK 109

                  ....*
gi 1519316358 672 ERENE 676
Cdd:PHA03097  110 KGDDD 114
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
73-278 5.59e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  73 ETSRQTYDDKLTAVESDLKKLGDQTgkkaISTNSELSTFRSDILDLRQQLREITEKTSKNKDTLEKLQAsgdALVDRQSQ 152
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAEL----DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 153 LKETLE---NNSFLITTVNKTLQAYN--GYVTNLQqdtsvlqgnLQNQMYSHNVVImnLNNLNLTQVQQRNLITNLQRSV 227
Cdd:COG3883    88 LGERARalyRSGGSVSYLDVLLGSESfsDFLDRLS---------ALSKIADADADL--LEELKADKAELEAKKAELEAKL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519316358 228 DDTSQAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKA 278
Cdd:COG3883   157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
88-270 6.57e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  88 SDLKKLGDQTGKKAISTNSELSTFRSDILDLRQQLREITEKTSKNKDTLEKLQASGDALVDRQSQLKETLE--------- 158
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAellralyrl 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 159 -NNSFL--------ITTVNKTLQAYNGYVTNLQQDTSVLQGNLQNqmyshnvvimnLNNLNLTQVQQRNLITNLQRSVDD 229
Cdd:COG4942   117 gRQPPLalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAE-----------LAALRAELEAERAELEALLAELEE 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1519316358 230 TSQAIQRIKNDFQ----NLQQVFLQAKKDTDWLKEKVQSLQTLAA 270
Cdd:COG4942   186 ERAALEALKAERQkllaRLEKELAELAAELAELQQEAEELEALIA 230
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
205-377 6.90e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 38.93  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 205 NLNNLNLTQVQQRNLITNLQRSVDDTSQAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLE 284
Cdd:cd21116    64 IIGYNNTFQSYYPDLIELADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQ 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 285 DMNSQLNSFTGQMENITTISQANEQNLKDLQDlhkdaenrtaiKFNQLEERFQLFETDIVNIISNISYTAhhlrtLTSNL 364
Cdd:cd21116   144 AQVAVLNALKNQLNSLAEQIDAAIDALEKLSN-----------DWQTLDSDIKELITDLEDAESSIDAAF-----LQADL 207
                         170
                  ....*....|...
gi 1519316358 365 NEVRTTCTDTLTK 377
Cdd:cd21116   208 KAAKADWNQLYEQ 220
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
87-411 7.95e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.72  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358  87 ESDLKKLGDQTGKKAISTNSELSTFRSDILDLRQQLreiTEKTSKNKDTLEKLQASGDALVDRQSQLKETLENNSFL--- 163
Cdd:pfam05557   8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQL---DRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKkky 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 164 ITTVNK-------TLQAYNGYVTNLQQDTSVLQGNLQNQ---MYSHNVVIMNLNNLNltQVQQRN------LITNLQRSV 227
Cdd:pfam05557  85 LEALNKklnekesQLADAREVISCLKNELSELRRQIQRAeleLQSTNSELEELQERL--DLLKAKaseaeqLRQNLEKQQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 228 DDTSQAIQRIKNDFQNLQQvFLQAKKDTDWLKEKVQS-------LQTLAANNSALAKANNDTL------EDMNSQLNSFT 294
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQS-QEQDSEIVKNSKSELARipelekeLERLREHNKHLNENIENKLllkeevEDLKRKLEREE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519316358 295 GQMENITTISQANEQNLKDLQDLHKDAENR--TAIKFNQLEERF-QLFETDIVNIISNISYTAhHLRTLTSNLNEVRTTC 371
Cdd:pfam05557 242 KYREEAATLELEKEKLEQELQSWVKLAQDTglNLRSPEDLSRRIeQLQQREIVLKEENSSLTS-SARQLEKARRELEQEL 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1519316358 372 TDTLTKHTDDLTSLNNTLANIRldsvslRMQQ---------DLMRSRLD 411
Cdd:pfam05557 321 AQYLKKIEDLNKKLKRHKALVR------RLQRrvllltkerDGYRAILE 363
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH