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Conserved domains on  [gi|829315329|gb|KLQ08163|]
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hypothetical protein ABF77_00220 [Enterobacter roggenkampii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 465-617 1.63e-12

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


The actual alignment was detected with superfamily member cd01454:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 174  Bit Score: 66.20  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 465 AFTILLDSSGSMSRSVK--EAEAAVVSMLYALDGIqGVTTSAYHFPhaahnsvGLLKGREQTLRTAIGTHQFG------- 535
Cdd:cd01454    2 AVTLLLDLSGSMRSDRRidVAKKAAVLLAEALEAC-GVPHAILGFT-------TDAGGRERVRWIKIKDFDESlherark 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 536 -IGT---QGCTPLCESLWPALADLTSAKADRHVLVIATDGQPDDMA-----------SARAMIQSAKdDDIIVIGIG-FG 599
Cdd:cd01454   74 rLAAlspGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDyyegnvfatedALRAVIEARK-LGIEVFGITiDR 152

                        170       180
                 ....*....|....*....|.
gi 829315329 600 DA---NDSMMKSLFGDTGISV 617
Cdd:cd01454  153 DAttvDKEYLKNIFGEEGYAL 173
PHA03169 super family cl27451
hypothetical protein; Provisional
 218-355 8.89e-05

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 8.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 218 EPPQDDNQGADSDDSKGDDSSSDPAQSSDSSD-KNGDGQNDSAGGNDGSSSSPAGQNEPS---SEPDGNAGGAPDKEHGQ 293
Cdd:PHA03169  47 APPAPTTSGPQVRAVAEQGHRQTESDTETAEEsRHGEKEERGQGGPSGSGSESVGSPTPSpsgSAEELASGLSPENTSGS 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 829315329 294 NDTDDENENSSSTSANRNAPASNSSDSNAaasHPGVNAQGESSVGNLSQNGKDPFEGTTSND 355
Cdd:PHA03169 127 SPESPASHSPPPSPPSHPGPHEPAPPESH---NPSPNQQPSSFLQPSHEDSPEEPEPPTSEP 185
 
Name Accession Description Interval E-value
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 465-617 1.63e-12

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 66.20  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 465 AFTILLDSSGSMSRSVK--EAEAAVVSMLYALDGIqGVTTSAYHFPhaahnsvGLLKGREQTLRTAIGTHQFG------- 535
Cdd:cd01454    2 AVTLLLDLSGSMRSDRRidVAKKAAVLLAEALEAC-GVPHAILGFT-------TDAGGRERVRWIKIKDFDESlherark 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 536 -IGT---QGCTPLCESLWPALADLTSAKADRHVLVIATDGQPDDMA-----------SARAMIQSAKdDDIIVIGIG-FG 599
Cdd:cd01454   74 rLAAlspGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDyyegnvfatedALRAVIEARK-LGIEVFGITiDR 152

                        170       180
                 ....*....|....*....|.
gi 829315329 600 DA---NDSMMKSLFGDTGISV 617
Cdd:cd01454  153 DAttvDKEYLKNIFGEEGYAL 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 466-629 1.16e-09

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 57.85  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329   466 FTILLDSSGSMSRS----VKEAEAAVVSMLYalDGIQGVTTSAYHFPHAAHNSVGLLKGRE-QTLRTAIGTHQFGIGtqG 540
Cdd:smart00327   2 VVFLLDGSGSMGGNrfelAKEFVLKLVEQLD--IGPDGDRVGLVTFSDDARVLFPLNDSRSkDALLEALASLSYKLG--G 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329   541 CTPLCESLWPALADLTSAKAD-----RHVLVIATDGQPDDMAS-ARAMIQSAKDDDIIVIGIGFGDAND-SMMKSLFGDT 613
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGsrrgaPKVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDeEELKKLASAP 157

                          170
                   ....*....|....*.
gi 829315329   614 GISVGSVSALRNKLFE 629
Cdd:smart00327 158 GGVYVFLPELLDLLID 173
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 440-609 2.71e-07

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 52.41  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 440 RLVTSAMLGNTRLF------KHKSKAVDVSSAFTILLDSSGSMS----RSVKEAEAAVVSMLYALDgiqgvTTSAYHFPH 509
Cdd:COG2304   62 RLAQSPWNPQTRLLlvglqpPKAAAEERPPLNLVFVIDVSGSMSgdklELAKEAAKLLVDQLRPGD-----RVSIVTFAG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 510 AAHNSVGLLKGRE-QTLRTAIGthqfGIGTQGCTPLCESLWPALADLTSAKADRHV--LVIATDGQPD----DMASARAM 582
Cdd:COG2304  137 DARVLLPPTPATDrAKILAAID----RLQAGGGTALGAGLELAYELARKHFIPGRVnrVILLTDGDANvgitDPEELLKL 212

                        170       180
                 ....*....|....*....|....*...
gi 829315329 583 IQSAKDDDIIVIGIGFG-DANDSMMKSL 609
Cdd:COG2304  213 AEEAREEGITLTTLGVGsDYNEDLLERL 240
Copine pfam07002
Copine; This family represents a conserved region approximately 220 residues long within ...
 563-612 8.90e-06

Copine; This family represents a conserved region approximately 220 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth.


Pssm-ID: 462064  Cd Length: 214  Bit Score: 47.33  E-value: 8.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 829315329  563 HVLVIATDGQPDDMASARAMIQSAKDDDIIVIGIGFGDANDSMMKSLFGD 612
Cdd:pfam07002 110 HVLLIITDGVVTDMKATIDAIVNASHLPLSIIIVGVGDGDFSDMRELDDD 159
PHA03169 PHA03169
hypothetical protein; Provisional
 218-355 8.89e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 8.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 218 EPPQDDNQGADSDDSKGDDSSSDPAQSSDSSD-KNGDGQNDSAGGNDGSSSSPAGQNEPS---SEPDGNAGGAPDKEHGQ 293
Cdd:PHA03169  47 APPAPTTSGPQVRAVAEQGHRQTESDTETAEEsRHGEKEERGQGGPSGSGSESVGSPTPSpsgSAEELASGLSPENTSGS 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 829315329 294 NDTDDENENSSSTSANRNAPASNSSDSNAaasHPGVNAQGESSVGNLSQNGKDPFEGTTSND 355
Cdd:PHA03169 127 SPESPASHSPPPSPPSHPGPHEPAPPESH---NPSPNQQPSSFLQPSHEDSPEEPEPPTSEP 185
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 212-368 1.44e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 41.52  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 212 ETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDSSDKNGDGQNDSAGGNDGSSSSPAGQNEPSSEPDGNAGGAPDKEH 291
Cdd:cd21118  178 GTNSQGAVAQPGYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSS 257

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 829315329 292 GQNDTDDENENSSSTSANRNAPASNSSDSNAAAShPGVNAQGESSVGNlsqngkDPFEGTTSNDLGRTGQNTSDKLN 368
Cdd:cd21118  258 NSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGS-SSSGGSGGSGGGN------KPECNNPGNDVRMAGGGGSQGSK 327
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 204-355 2.89e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 204 DLAVDAFNETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDS-SDKNGDGQNDSAGGNDGSSSSPAGqNEPSSEPDGN 282
Cdd:NF033609 735 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSD 813

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 829315329 283 AGGAPDKEHGQNDTDDENENSSSTSANRNAPASNSSDSNAAASHPGVNAQGESSVGNLSQNGKDPFEGTTSND 355
Cdd:NF033609 814 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASN 886
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 204-359 4.79e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.28  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 204 DLAVDAFNETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDS---SDKNGDGQNDSAGGNDGSSSSPAGQNEPS---- 276
Cdd:NF033609 757 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsds 836

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 277 -SEPDGNAGGAPDKEHGQNDTDDENENSSSTSANRNAPASNSSDsnaaashpGVNAQGEssvgNLSQNGKDPFEGTTSND 355
Cdd:NF033609 837 dSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKN--------GTNASNK----NEAKDSKEPLPDTGSED 904


                 ....
gi 829315329 356 LGRT 359
Cdd:NF033609 905 EANT 908
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 204-378 6.79e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 39.51  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 204 DLAVDAFNETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDS---SDKNGDGQNDSAGGNDGSSSSPAGQNEPS-SEP 279
Cdd:NF033609 699 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDS 778

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 280 DGNAGGAPDKEHGQNDTDDENENSSSTSANRNAPASNSSDSNAAASHPGVNAQGESSVGNLSQNGKDPFEGTTSNDLGRT 359
Cdd:NF033609 779 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSES 858

                        170
                 ....*....|....*....
gi 829315329 360 GQNtSDKLNQLIKDKVPPH 378
Cdd:NF033609 859 DSN-SDSESGSNNNVVPPN 876
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 204-346 8.13e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 39.51  E-value: 8.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 204 DLAVDAFNETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDS-SDKNGDGQNDSAGGNDGSSSSPAGQNEPS---SEP 279
Cdd:NF033609 617 DSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdSDS 696

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 829315329 280 DGNAGGAPDKEHGQNDTDDENENSSSTSANRNAPASNSSDSNAAASHPGVNAQGESSVGNLSQNGKD 346
Cdd:NF033609 697 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 763
 
Name Accession Description Interval E-value
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 465-617 1.63e-12

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 66.20  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 465 AFTILLDSSGSMSRSVK--EAEAAVVSMLYALDGIqGVTTSAYHFPhaahnsvGLLKGREQTLRTAIGTHQFG------- 535
Cdd:cd01454    2 AVTLLLDLSGSMRSDRRidVAKKAAVLLAEALEAC-GVPHAILGFT-------TDAGGRERVRWIKIKDFDESlherark 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 536 -IGT---QGCTPLCESLWPALADLTSAKADRHVLVIATDGQPDDMA-----------SARAMIQSAKdDDIIVIGIG-FG 599
Cdd:cd01454   74 rLAAlspGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDyyegnvfatedALRAVIEARK-LGIEVFGITiDR 152

                        170       180
                 ....*....|....*....|.
gi 829315329 600 DA---NDSMMKSLFGDTGISV 617
Cdd:cd01454  153 DAttvDKEYLKNIFGEEGYAL 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 466-629 1.16e-09

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 57.85  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329   466 FTILLDSSGSMSRS----VKEAEAAVVSMLYalDGIQGVTTSAYHFPHAAHNSVGLLKGRE-QTLRTAIGTHQFGIGtqG 540
Cdd:smart00327   2 VVFLLDGSGSMGGNrfelAKEFVLKLVEQLD--IGPDGDRVGLVTFSDDARVLFPLNDSRSkDALLEALASLSYKLG--G 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329   541 CTPLCESLWPALADLTSAKAD-----RHVLVIATDGQPDDMAS-ARAMIQSAKDDDIIVIGIGFGDAND-SMMKSLFGDT 613
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGsrrgaPKVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDeEELKKLASAP 157

                          170
                   ....*....|....*.
gi 829315329   614 GISVGSVSALRNKLFE 629
Cdd:smart00327 158 GGVYVFLPELLDLLID 173
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 468-605 6.58e-08

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 52.57  E-value: 6.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 468 ILLDSSGSMSRSVKE-AEAAVVSMLYALD-GIQGVTTSAYHFPHAAHNSVGLLKGR-EQTLRTAIgtHQFGIGTQGCTPL 544
Cdd:cd00198    5 FLLDVSGSMGGEKLDkAKEALKALVSSLSaSPPGDRVGLVTFGSNARVVLPLTTDTdKADLLEAI--DALKKGLGGGTNI 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 829315329 545 CESLWPALADLTSAKAD--RHVLVIATDGQP-DDMASARAMIQSAKDDDIIVIGIGFGDANDSM 605
Cdd:cd00198   83 GAALRLALELLKSAKRPnaRRVIILLTDGEPnDGPELLAEAARELRKLGITVYTIGIGDDANED 146
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 440-609 2.71e-07

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 52.41  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 440 RLVTSAMLGNTRLF------KHKSKAVDVSSAFTILLDSSGSMS----RSVKEAEAAVVSMLYALDgiqgvTTSAYHFPH 509
Cdd:COG2304   62 RLAQSPWNPQTRLLlvglqpPKAAAEERPPLNLVFVIDVSGSMSgdklELAKEAAKLLVDQLRPGD-----RVSIVTFAG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 510 AAHNSVGLLKGRE-QTLRTAIGthqfGIGTQGCTPLCESLWPALADLTSAKADRHV--LVIATDGQPD----DMASARAM 582
Cdd:COG2304  137 DARVLLPPTPATDrAKILAAID----RLQAGGGTALGAGLELAYELARKHFIPGRVnrVILLTDGDANvgitDPEELLKL 212

                        170       180
                 ....*....|....*....|....*...
gi 829315329 583 IQSAKDDDIIVIGIGFG-DANDSMMKSL 609
Cdd:COG2304  213 AEEAREEGITLTTLGVGsDYNEDLLERL 240
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 412-609 4.99e-07

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 51.60  E-value: 4.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 412 LRQSLHGLLQGVRAVRRTHRETGRKLDSRLVTsamLGNTRLFKHKSKAVDVSSAFTILLDSSGSMSRSVKE-AEAAVVSM 490
Cdd:COG2425   70 LALDALLLAALLAALLDALLLAVLLLALLLLA---ALLLLAAPASAAVPLLEGPVVLCVDTSGSMAGSKEAaAKAAALAL 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 491 LYALdgIQGVTTSAYHFPHAAHNSVGLLKGRE-QTLRTAIGTHQFGIGTQGCTPLCEslwpALADLTSAKADRHVLVIAT 569
Cdd:COG2425  147 LRAL--RPNRRFGVILFDTEVVEDLPLTADDGlEDAIEFLSGLFAGGGTDIAPALRA----ALELLEEPDYRNADIVLIT 220

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 829315329 570 DGQPDDMASA--RAMIQSAKDDDIIVIGIGfGDANDSMMKSL 609
Cdd:COG2425  221 DGEAGVSPEEllREVRAKESGVRLFTVAIG-DAGNPGLLEAL 261
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 468-625 3.91e-06

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 48.78  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 468 ILLDSSGSMS-----RSVKEAEAAVVSMLYALDGIqGVTTsayhFPHAAHNSVGLLKGREqTLRTAIGthqfGIGTQGCT 542
Cdd:COG1240   97 LVVDASGSMAaenrlEAAKGALLDFLDDYRPRDRV-GLVA----FGGEAEVLLPLTRDRE-ALKRALD----ELPPGGGT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 543 PLCESLWPALADLTSA-KADRHVLVIATDGQP-DDMASARAMIQSAKDDDI--IVIGIGFGDANDSMMKSLFGDTG---I 615
Cdd:COG1240  167 PLGDALALALELLKRAdPARRKVIVLLTDGRDnAGRIDPLEAAELAAAAGIriYTIGVGTEAVDEGLLREIAEATGgryF 246

                        170
                 ....*....|
gi 829315329 616 SVGSVSALRN 625
Cdd:COG1240  247 RADDLSELAA 256
Copine pfam07002
Copine; This family represents a conserved region approximately 220 residues long within ...
 563-612 8.90e-06

Copine; This family represents a conserved region approximately 220 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth.


Pssm-ID: 462064  Cd Length: 214  Bit Score: 47.33  E-value: 8.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 829315329  563 HVLVIATDGQPDDMASARAMIQSAKDDDIIVIGIGFGDANDSMMKSLFGD 612
Cdd:pfam07002 110 HVLLIITDGVVTDMKATIDAIVNASHLPLSIIIVGVGDGDFSDMRELDDD 159
vWA_copine_like cd01459
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ...
 563-614 1.77e-05

VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding.


Pssm-ID: 238736  Cd Length: 254  Bit Score: 46.60  E-value: 1.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 829315329 563 HVLVIATDGQPDDMASARAMIQSAKDDDIIVIGIGFGDANDSMMKSLFGDTG 614
Cdd:cd01459  158 HILLIITDGEITDMNETIKAIVEASKYPLSIVIVGVGDGPFDAMERLDDDDG 209
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 467-604 2.41e-05

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 44.98  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 467 TILLDSSGSMSRS----VKEAEAAVVSML-YALDGIQ-GVTTSAY----HFPHAAHNSVGLLKGREQTLRTAIGTHQFgI 536
Cdd:cd01450    4 VFLLDGSESVGPEnfekVKDFIEKLVEKLdIGPDKTRvGLVQYSDdvrvEFSLNDYKSKDDLLKAVKNLKYLGGGGTN-T 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 829315329 537 GtqgctplcESLWPALADLTSAKADR----HVLVIATDGQPDDMASARAMIQSAKDDDIIVIGIGFGDANDS 604
Cdd:cd01450   83 G--------KALQYALEQLFSESNARenvpKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEE 146
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 468-609 4.14e-05

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 44.64  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 468 ILLDSSGSMS-RSVKEAEAAVVSML-------YALDGIQ-GVTTsayhFPHAAHNSVGLlkgreqtlrTAIGTHQFGIGT 538
Cdd:cd01464    8 LLLDTSGSMAgEPIEALNQGLQMLQselrqdpYALESVEiSVIT----FDSAARVIVPL---------TPLESFQPPRLT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 539 -QGCTPLCESLWPALADL------TSA--KAD-RHVLVIATDGQP-DDMASARAMIQSAKDDDIIVIGIGFG-DANDSMM 606
Cdd:cd01464   75 aSGGTSMGAALELALDCIdrrvqrYRAdqKGDwRPWVFLLTDGEPtDDLTAAIERIKEARDSKGRIVACAVGpKADLDTL 154


                 ...
gi 829315329 607 KSL 609
Cdd:cd01464  155 KQI 157
VWA pfam00092
von Willebrand factor type A domain;
468-609 6.87e-05

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 43.80  E-value: 6.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329  468 ILLDSSGSMSRS----VKEAEAAVVSMLYAL-DGIQ-GVTTSAY----HFPHAAHNSVgllkgreQTLRTAIgtHQFGIG 537
Cdd:pfam00092   4 FLLDGSGSIGGDnfekVKEFLKKLVESLDIGpDGTRvGLVQYSSdvrtEFPLNDYSSK-------EELLSAV--DNLRYL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 829315329  538 TQGCTPLCESLWPALADLTSAKA-----DRHVLVIATDGQPDDmASARAMIQSAKDDDIIVIGIGFGDANDSMMKSL 609
Cdd:pfam00092  75 GGGTTNTGKALKYALENLFSSAAgarpgAPKVVVLLTDGRSQD-GDPEEVARELKSAGVTVFAVGVGNADDEELRKI 150
PHA03169 PHA03169
hypothetical protein; Provisional
 218-355 8.89e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 8.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 218 EPPQDDNQGADSDDSKGDDSSSDPAQSSDSSD-KNGDGQNDSAGGNDGSSSSPAGQNEPS---SEPDGNAGGAPDKEHGQ 293
Cdd:PHA03169  47 APPAPTTSGPQVRAVAEQGHRQTESDTETAEEsRHGEKEERGQGGPSGSGSESVGSPTPSpsgSAEELASGLSPENTSGS 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 829315329 294 NDTDDENENSSSTSANRNAPASNSSDSNAaasHPGVNAQGESSVGNLSQNGKDPFEGTTSND 355
Cdd:PHA03169 127 SPESPASHSPPPSPPSHPGPHEPAPPESH---NPSPNQQPSSFLQPSHEDSPEEPEPPTSEP 185
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 464-609 1.19e-04

VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 43.03  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 464 SAFTILLDSSGSMSRS----VKEAEAAVVSMLYALDGIQGVTtsayhFPHAAHNSVGLLKGRE-QTLRTAIGthqfGIGT 538
Cdd:cd01465    1 LNLVFVIDRSGSMDGPklplVKSALKLLVDQLRPDDRLAIVT-----YDGAAETVLPATPVRDkAAILAAID----RLTA 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 829315329 539 QGCTPLCESLWPALADLTSAKADRHV--LVIATDGQP----DDMASARAMIQSAKDDDIIVIGIGFGDA-NDSMMKSL 609
Cdd:cd01465   72 GGSTAGGAGIQLGYQEAQKHFVPGGVnrILLATDGDFnvgeTDPDELARLVAQKRESGITLSTLGFGDNyNEDLMEAI 149
PRK12495 PRK12495
hypothetical protein; Provisional
 246-371 3.32e-04

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 42.55  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 246 DSSDKNGDGQNDSAGGNDGSSSSPAGQNEPSSEPDGNAGGAPdKEHGQNDTDDENENSSSTSANRNAPASNSSDSNAAAS 325
Cdd:PRK12495  73 AAGDDAGDGAEATAPSDAGSQASPDDDAQPAAEAEAADQSAP-PEASSTSATDEAATDPPATAAARDGPTPDPTAQPATP 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 829315329 326 HPGVNAQGESSVgnlsqNGKDPFEGTTSNDLGRTGQNTSDKLNQLI 371
Cdd:PRK12495 152 DERRSPRQRPPV-----SGEPPTPSTPDAHVAGTLQAARESLVETL 192
PHA02664 PHA02664
hypothetical protein; Provisional
 254-344 4.67e-04

hypothetical protein; Provisional


Pssm-ID: 177447  Cd Length: 534  Bit Score: 43.07  E-value: 4.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 254 GQNDSAGGNDGSSSSPAGQN---EPSSEPDGNAGGAPDKEHGQNDTDDENENSSSTSANRNAPASNSSDSNAAASHPGVN 330
Cdd:PHA02664 409 PEEGRAAAAAAAANAPADQDveaEAHDEFDQDPGAPAHADRADSDEDDMDEQESGDERADGEDDSDSSYSYSTTSSEDES 488

                         90
                 ....*....|....
gi 829315329 331 AQGESSVGNLSQNG 344
Cdd:PHA02664 489 DSADDSWGDESDSG 502
PHA03169 PHA03169
hypothetical protein; Provisional
 208-366 1.08e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.88  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 208 DAFNETNEQEEPPQDDnqgADSDDSKGDDSSSDPAQSSDSSDKNGDGQNDSAGGNDGSS-SSPAGQNEPSSEPDGNAGGA 286
Cdd:PHA03169 116 SGLSPENTSGSSPESP---ASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHeDSPEEPEPPTSEPEPDSPGP 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 287 PDKEHG------QNDTDDENENSSSTSanRNAPASNSSDSNAAASHPGVNAQGEssvgnlsqngkDPFEGTTSNDLGRTG 360
Cdd:PHA03169 193 PQSETPtsspppQSPPDEPGEPQSPTP--QQAPSPNTQQAVEHEDEPTEPEREG-----------PPFPGHRSHSYTVVG 259


                 ....*.
gi 829315329 361 QNTSDK 366
Cdd:PHA03169 260 WKPSTR 265
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 212-368 1.44e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 41.52  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 212 ETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDSSDKNGDGQNDSAGGNDGSSSSPAGQNEPSSEPDGNAGGAPDKEH 291
Cdd:cd21118  178 GTNSQGAVAQPGYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSS 257

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 829315329 292 GQNDTDDENENSSSTSANRNAPASNSSDSNAAAShPGVNAQGESSVGNlsqngkDPFEGTTSNDLGRTGQNTSDKLN 368
Cdd:cd21118  258 NSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGS-SSSGGSGGSGGGN------KPECNNPGNDVRMAGGGGSQGSK 327
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 204-355 2.89e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 204 DLAVDAFNETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDS-SDKNGDGQNDSAGGNDGSSSSPAGqNEPSSEPDGN 282
Cdd:NF033609 735 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSD 813

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 829315329 283 AGGAPDKEHGQNDTDDENENSSSTSANRNAPASNSSDSNAAASHPGVNAQGESSVGNLSQNGKDPFEGTTSND 355
Cdd:NF033609 814 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASN 886
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 466-571 3.98e-03

VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have a conserved MIDAS motif, however, their biochemical function is not well characterised.


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 38.48  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 466 FTILLDSSGSMSRSVKEAEAAVVSMLYALDGIQGVTTSAYHFPHAAHNSVGLLK-GREQTLRTAIGThQFGIGTQGCTPL 544
Cdd:cd01462    3 VILLVDQSGSMYGAPEEVAKAVALALLRIALAENRDTYLILFDSEFQTKIVDKTdDLEEPVEFLSGV-QLGGGTDINKAL 81

                         90       100
                 ....*....|....*....|....*..
gi 829315329 545 CEslwpALADLTSAKADRHVLVIATDG 571
Cdd:cd01462   82 RY----ALELIERRDPRKADIVLITDG 104
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 205-368 4.01e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 39.98  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 205 LAVDAFNETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDSSDKNGDGQNDSAGGNDGSSSSPAGQNEPSSEpdGNAG 284
Cdd:cd21118  191 GTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGG--SNGG 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 285 GAPDKEHGQNDTDDENENSSSTSANRNAPASNSSDSNAAASHPGVNAQGESSVGNLSQNGKDPFEGTTSNDLGRTGQNTS 364
Cdd:cd21118  269 SSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGL 348


                 ....
gi 829315329 365 DKLN 368
Cdd:cd21118  349 NTLN 352
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 204-359 4.79e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.28  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 204 DLAVDAFNETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDS---SDKNGDGQNDSAGGNDGSSSSPAGQNEPS---- 276
Cdd:NF033609 757 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsds 836

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 277 -SEPDGNAGGAPDKEHGQNDTDDENENSSSTSANRNAPASNSSDsnaaashpGVNAQGEssvgNLSQNGKDPFEGTTSND 355
Cdd:NF033609 837 dSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKN--------GTNASNK----NEAKDSKEPLPDTGSED 904


                 ....
gi 829315329 356 LGRT 359
Cdd:NF033609 905 EANT 908
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 204-378 6.79e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 39.51  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 204 DLAVDAFNETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDS---SDKNGDGQNDSAGGNDGSSSSPAGQNEPS-SEP 279
Cdd:NF033609 699 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDS 778

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 280 DGNAGGAPDKEHGQNDTDDENENSSSTSANRNAPASNSSDSNAAASHPGVNAQGESSVGNLSQNGKDPFEGTTSNDLGRT 359
Cdd:NF033609 779 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSES 858

                        170
                 ....*....|....*....
gi 829315329 360 GQNtSDKLNQLIKDKVPPH 378
Cdd:NF033609 859 DSN-SDSESGSNNNVVPPN 876
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 564-601 7.46e-03

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 37.72  E-value: 7.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 829315329 564 VLVIATDGQPDDMASARAMIQSAKDDDIIVIGIGFGDA 601
Cdd:cd01469  106 VLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGH 143
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 204-346 8.13e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 39.51  E-value: 8.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829315329 204 DLAVDAFNETNEQEEPPQDDNQGADSDDSKGDDSSSDPAQSSDS-SDKNGDGQNDSAGGNDGSSSSPAGQNEPS---SEP 279
Cdd:NF033609 617 DSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdSDS 696

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 829315329 280 DGNAGGAPDKEHGQNDTDDENENSSSTSANRNAPASNSSDSNAAASHPGVNAQGESSVGNLSQNGKD 346
Cdd:NF033609 697 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 763
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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