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Conserved domains on  [gi|28872751|ref|NP_787954|]
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dual oxidase 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
32-591 0e+00

Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase like subfamily play vital roles in the innate mucosal immunity of gut epithelia. They provide reactive oxygen species which help control infection.


:

Pssm-ID: 188652 [Multi-domain]  Cd Length: 558  Bit Score: 911.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   32 FDGWYNNLMEHRWGSKGSRLQRLVPASYADGVYQPLGEpHLPNPRDLSNTISRGPAGLASLRNRTVLGVFFGYHVLSDLV 111
Cdd:cd09820    1 YDGWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGE-ERPNPRSLSNLLMKGESGLPSTRNRTALLVFFGQHVVSEIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  112 SVETPGCPAEFLNIRIPPGDPMFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDPANQVTGWLDGSAIYGSSHSWSDALRS 191
Cdd:cd09820   80 DASRPGCPPEYFNIEIPKGDPVFDPECTGNIELPFQRSRYDKNTGYSPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  192 FSRGQLASGPDPAFPRDSQNPLLMWAAPDPAT-GQNGPRGLYAFGAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDW 270
Cdd:cd09820  160 FSGGRLASGDDGGFPRRNTNRLPLANPPPPSYhGTRGPERLFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDW 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  271 EDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPEYTGYRPFLDPSISSEFVAASEQFLSTMVPPGVYMRNASCHFQGV 350
Cdd:cd09820  240 SDEDIFQEARKWVIATYQNIVFYEWLPALLGTNVPPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVYRRNRQCNFREV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  351 INrNSSVSRALRVCNSYWSREHPSLQSaeDVDALLLGMASQIAEREDHVLVEDVRDFWPGPLKFSRTDHLASCLQRGRDL 430
Cdd:cd09820  320 LT-TSGGSPALRLCNTYWNSQEPLLKS--DIDELLLGMASQIAEREDNIIVEDLRDYLFGPLEFSRRDLMALNIQRGRDH 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  431 GLPSYTKARAALGLSPITRWQDINPALSRSNDTVLEATAALYNQDLSWLELLPGGLLESHRD-PGPLFSTIVLEQFVRLR 509
Cdd:cd09820  397 GLPDYNTAREAFGLPPRTTWSDINPDLFKKDPELLERLAELYGNDLSKLDLYVGGMLESKGGgPGELFRAIILDQFQRLR 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  510 DGDRYWFENTRNGLFSKKEIEEIRNTTLQDVLVAVINIDPSALQPNVFVWHKGDPCPQPRQLSTEGLPACAPSVVRDYFE 589
Cdd:cd09820  477 DGDRFWFENVKNGLFTAEEIEEIRNTTLRDVILAVTDIDNTDLQKNVFFWKNGDPCPQPKQLTENMLEPCTPLTVYDYFE 556

                 ..
gi 28872751  590 GS 591
Cdd:cd09820  557 GS 558
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
1277-1551 3.04e-55

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


:

Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 191.36  E-value: 3.04e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1277 VVKAELLP-SGVTHLRFQRPQGFEYKSGQWVRIACLAL-GTTEYHPFTLTSAPHE--DTLSLHIRA-AGPWTTRLREIYS 1351
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAkKGFTTRLLRKALK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1352 APTgdrCARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVSCQvfCKKIYFIWVTRTQRQFEW 1431
Cdd:cd06186   81 SPG---GGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSR--TRRVKLVWVVRDREDLEW 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1432 LADIIRevEENDHQDLVSVHIYITQlaekfdlrttmlyicerhfqkvlnrslftglrsithfgrppfepffnslqevhpq 1511
Cdd:cd06186  156 FLDELR--AAQELEVDGEIEIYVTR------------------------------------------------------- 178
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 28872751 1512 vrkigVFSCGPPGMTKNVEKACqliNRQDRTHFSHHYENF 1551
Cdd:cd06186  179 -----VVVCGPPGLVDDVRNAV---AKKGGTGVEFHEESF 210
PLN02292 super family cl33451
ferric-chelate reductase
1089-1412 2.12e-20

ferric-chelate reductase


The actual alignment was detected with superfamily member PLN02292:

Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 98.02  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1089 TAASISF--MFSYILLTmcrNLITFLRETFLNrYVPFDAAVDFHRLIASTAIVLTV-LHSVGHVVNVYLFSisPLSVLSC 1165
Cdd:PLN02292  120 TVTEVMFlaMFMALLLW---SLANYMYNTFVT-ITPQSAATDGESLWQARLDSIAVrLGLVGNICLAFLFY--PVARGSS 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1166 LFP--GLfhddGSELPQKY---------------------YW-----------WFFQTVPGLTGVVLLLILAIMYVFASH 1211
Cdd:PLN02292  194 LLAavGL----TSESSIKYhiwlghlvmtlftshglcyiiYWismnqvsqmleWDRTGVSNLAGEIALVAGLVMWATTYP 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1212 HFRRRSFRGFWLTHHLYILLYVLLIIHG--SFALIQLPRFHIFFLvpaiiyggDKLVSLSRKKVEISVVKAELLPSGVTH 1289
Cdd:PLN02292  270 KIRRRFFEVFFYTHYLYIVFMLFFVFHVgiSFALISFPGFYIFLV--------DRFLRFLQSRNNVKLVSARVLPCDTVE 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1290 LRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAP--HEDTLSLHIRAAGPWTTRLREIYSAPTG-DRCArypkLYL 1366
Cdd:PLN02292  342 LNFSKNPMLMYSPTSIMFVNIPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLYHMLSSSDQiDRLA----VSV 417
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 28872751  1367 DGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSV-SCQV 1412
Cdd:PLN02292  418 EGPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLIYTSSTeTCKI 464
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
820-881 1.82e-15

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 72.20  E-value: 1.82e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28872751  820 VESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLR 881
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
857-915 9.08e-08

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 50.24  E-value: 9.08e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28872751  857 RLMFRMYDFDGNGLISKDEFIRMLRSfieisnncLSKAQLAEVVESMFRE-----SGFQDKEEL 915
Cdd:cd00051    3 REAFRLFDKDGDGTISADELKAALKS--------LGEGLSEEEIDEMIREvdkdgDGKIDFEEF 58
 
Name Accession Description Interval E-value
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
32-591 0e+00

Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase like subfamily play vital roles in the innate mucosal immunity of gut epithelia. They provide reactive oxygen species which help control infection.


Pssm-ID: 188652 [Multi-domain]  Cd Length: 558  Bit Score: 911.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   32 FDGWYNNLMEHRWGSKGSRLQRLVPASYADGVYQPLGEpHLPNPRDLSNTISRGPAGLASLRNRTVLGVFFGYHVLSDLV 111
Cdd:cd09820    1 YDGWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGE-ERPNPRSLSNLLMKGESGLPSTRNRTALLVFFGQHVVSEIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  112 SVETPGCPAEFLNIRIPPGDPMFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDPANQVTGWLDGSAIYGSSHSWSDALRS 191
Cdd:cd09820   80 DASRPGCPPEYFNIEIPKGDPVFDPECTGNIELPFQRSRYDKNTGYSPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  192 FSRGQLASGPDPAFPRDSQNPLLMWAAPDPAT-GQNGPRGLYAFGAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDW 270
Cdd:cd09820  160 FSGGRLASGDDGGFPRRNTNRLPLANPPPPSYhGTRGPERLFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDW 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  271 EDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPEYTGYRPFLDPSISSEFVAASEQFLSTMVPPGVYMRNASCHFQGV 350
Cdd:cd09820  240 SDEDIFQEARKWVIATYQNIVFYEWLPALLGTNVPPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVYRRNRQCNFREV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  351 INrNSSVSRALRVCNSYWSREHPSLQSaeDVDALLLGMASQIAEREDHVLVEDVRDFWPGPLKFSRTDHLASCLQRGRDL 430
Cdd:cd09820  320 LT-TSGGSPALRLCNTYWNSQEPLLKS--DIDELLLGMASQIAEREDNIIVEDLRDYLFGPLEFSRRDLMALNIQRGRDH 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  431 GLPSYTKARAALGLSPITRWQDINPALSRSNDTVLEATAALYNQDLSWLELLPGGLLESHRD-PGPLFSTIVLEQFVRLR 509
Cdd:cd09820  397 GLPDYNTAREAFGLPPRTTWSDINPDLFKKDPELLERLAELYGNDLSKLDLYVGGMLESKGGgPGELFRAIILDQFQRLR 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  510 DGDRYWFENTRNGLFSKKEIEEIRNTTLQDVLVAVINIDPSALQPNVFVWHKGDPCPQPRQLSTEGLPACAPSVVRDYFE 589
Cdd:cd09820  477 DGDRFWFENVKNGLFTAEEIEEIRNTTLRDVILAVTDIDNTDLQKNVFFWKNGDPCPQPKQLTENMLEPCTPLTVYDYFE 556

                 ..
gi 28872751  590 GS 591
Cdd:cd09820  557 GS 558
An_peroxidase pfam03098
Animal haem peroxidase;
30-557 3.87e-168

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 516.72  E-value: 3.87e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751     30 QRFDGWYNNLMEHRWGSKGSRLQRLVPASYADGVYQPLGEPH---LPNPRDLSNTISRGPAGLASlRNRTVLGVFFGYHV 106
Cdd:pfam03098    2 RTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSSSgspLPSPRLVSNKLFAGDSGIPD-PNLTLLLMQWGQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    107 LSDLVSVETPGCPAEF---------------LNIRIPPGDPMFDPdqRGDVVLPFQRSRWDPETGrspsNPRDPANQVTG 171
Cdd:pfam03098   81 DHDLTLTPESTSPNGSscdcccppenlhppcFPIPIPPDDPFFSP--FGVRCMPFVRSAPGCGLG----NPREQINQVTS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    172 WLDGSAIYGSSHSWSDALRSFSRGQLASGpdpafpRDSQNPLLMWAAPDPATGQNGPRGLYAF--GAERGNREPFLQALG 249
Cdd:pfam03098  155 FLDGSQVYGSSEETARSLRSFSGGLLKVN------RSDDGKELLPFDPDGPCCCNSSGGVPCFlaGDSRANENPGLTALH 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    250 LLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQK--------TLPEYTGYRPFLDPSISSE 321
Cdd:pfam03098  229 TLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEdnmnwfglLPLPYNGYDPNVDPSISNE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    322 FVAASEQFLSTMVPPGVYMRNaschfqgviNRNSSVSRALRVCNSYWSrehPSLQSAEDVDALLLGMASQIAEREDHVLV 401
Cdd:pfam03098  309 FATAAFRFGHSLIPPFLYRLD---------ENNVPEEPSLRLHDSFFN---PDRLYEGGIDPLLRGLATQPAQAVDNNFT 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    402 EDVRDFWPGPL-KFSRTDHLASCLQRGRDLGLPSYTKARAALGLSPITRWQDINPALSrsnDTVLEATAALYNqdlswle 480
Cdd:pfam03098  377 EELTNHLFGPPgEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIP---NEVIAKLRELYG------- 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    481 llpgglleshrDP--------------------GPLFSTIVLEQFVRLRDGDRYWFENTRNGLFSKKEIEEIRNTTLQDV 540
Cdd:pfam03098  447 -----------SVddidlwvgglaekplpgglvGPTFACIIGDQFRRLRDGDRFWYENGNQGSFTPEQLEEIRKTSLARV 515
                          570
                   ....*....|....*..
gi 28872751    541 LVAVINIDPSaLQPNVF 557
Cdd:pfam03098  516 ICDNTDIIET-IQPNVF 531
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
1277-1551 3.04e-55

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 191.36  E-value: 3.04e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1277 VVKAELLP-SGVTHLRFQRPQGFEYKSGQWVRIACLAL-GTTEYHPFTLTSAPHE--DTLSLHIRA-AGPWTTRLREIYS 1351
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAkKGFTTRLLRKALK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1352 APTgdrCARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVSCQvfCKKIYFIWVTRTQRQFEW 1431
Cdd:cd06186   81 SPG---GGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSR--TRRVKLVWVVRDREDLEW 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1432 LADIIRevEENDHQDLVSVHIYITQlaekfdlrttmlyicerhfqkvlnrslftglrsithfgrppfepffnslqevhpq 1511
Cdd:cd06186  156 FLDELR--AAQELEVDGEIEIYVTR------------------------------------------------------- 178
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 28872751 1512 vrkigVFSCGPPGMTKNVEKACqliNRQDRTHFSHHYENF 1551
Cdd:cd06186  179 -----VVVCGPPGLVDDVRNAV---AKKGGTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
1380-1533 5.08e-29

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 113.97  E-value: 5.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   1380 FEVSVLVGGGIGVTPFASILKDLVFKSSVSCQvfcKKIYFIWVTRTQRQFEWLADIIREVEENDHQDlVSVHIYITQLAE 1459
Cdd:pfam08030    1 YENVLLVAGGIGITPFISILKDLGNKSKKLKT---KKIKFYWVVRDLSSLEWFKDVLNELEELKELN-IEIHIYLTGEYE 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28872751   1460 KFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRkIGVFSCGPPGMTKNVEKAC 1533
Cdd:pfam08030   77 AEDASDQSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGS-IGVFSCGPPSLVDELRNLV 149
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
1124-1551 1.25e-20

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 96.89  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1124 DAAVDFHRLIASTAIVLTVLHsvghvvnvYLFSISPLSVLSclfpglfhddGSELPQKYYWWF-FQTVPGLT----GVVL 1198
Cdd:COG4097   75 DRLYRLHKWLGILALVLALAH--------PLLLLGPKWLVG----------WGGLPARLAALLtLLRGLAELlgewAFYL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1199 LLILAIMYVFashhfrRRSFR-GFW-LTHHLyillyvlliihgSFALIQLPRFHIFFLVP-------------------- 1256
Cdd:COG4097  137 LLALVVLSLL------RRRLPyELWrLTHRL------------LAVAYLLLAFHHLLLGGpfywsppagvlwaalaaagl 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1257 -AIIYGgdKLVS-LSRKKVEISVVKAELLPSGVT--HLRFQRPQGFEYKSGQ--WVRIAClALGTTEYHPFTLTSAPHED 1330
Cdd:COG4097  199 aAAVYS--RLGRpLRSRRHPYRVESVEPEAGDVVelTLRPEGGRWLGHRAGQfaFLRFDG-SPFWEEAHPFSISSAPGGD 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1331 -TLSLHIRAAGPWTTRLREIysaPTGDRcarypkLYLDGPFG---------EGHQewhkfevsVLVGGGIGVTPFASILK 1400
Cdd:COG4097  276 gRLRFTIKALGDFTRRLGRL---KPGTR------VYVEGPYGrftfdrrdtAPRQ--------VWIAGGIGITPFLALLR 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1401 DLVFKSSVscqvfCKKIYFIWVTRTQRQFEWLADIIREVEENDHqdlVSVHIYITQLAEKFDLRTtmlyicerhfqkvln 1480
Cdd:COG4097  339 ALAARPGD-----QRPVDLFYCVRDEEDAPFLEELRALAARLAG---LRLHLVVSDEDGRLTAER--------------- 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28872751 1481 rslftglrsithfgrppfepffnsLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLiNRQDRTHFshHYENF 1551
Cdd:COG4097  396 ------------------------LRRLVPDLAEADVFFCGPPGMMDALRRDLRA-LGVPARRI--HQERF 439
PLN02292 PLN02292
ferric-chelate reductase
1089-1412 2.12e-20

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 98.02  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1089 TAASISF--MFSYILLTmcrNLITFLRETFLNrYVPFDAAVDFHRLIASTAIVLTV-LHSVGHVVNVYLFSisPLSVLSC 1165
Cdd:PLN02292  120 TVTEVMFlaMFMALLLW---SLANYMYNTFVT-ITPQSAATDGESLWQARLDSIAVrLGLVGNICLAFLFY--PVARGSS 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1166 LFP--GLfhddGSELPQKY---------------------YW-----------WFFQTVPGLTGVVLLLILAIMYVFASH 1211
Cdd:PLN02292  194 LLAavGL----TSESSIKYhiwlghlvmtlftshglcyiiYWismnqvsqmleWDRTGVSNLAGEIALVAGLVMWATTYP 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1212 HFRRRSFRGFWLTHHLYILLYVLLIIHG--SFALIQLPRFHIFFLvpaiiyggDKLVSLSRKKVEISVVKAELLPSGVTH 1289
Cdd:PLN02292  270 KIRRRFFEVFFYTHYLYIVFMLFFVFHVgiSFALISFPGFYIFLV--------DRFLRFLQSRNNVKLVSARVLPCDTVE 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1290 LRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAP--HEDTLSLHIRAAGPWTTRLREIYSAPTG-DRCArypkLYL 1366
Cdd:PLN02292  342 LNFSKNPMLMYSPTSIMFVNIPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLYHMLSSSDQiDRLA----VSV 417
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 28872751  1367 DGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSV-SCQV 1412
Cdd:PLN02292  418 EGPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLIYTSSTeTCKI 464
PLN02631 PLN02631
ferric-chelate reductase
1183-1406 3.66e-19

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 93.95  E-value: 3.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1183 YWWFFQTVPGLTGVVLLLILAIMYVFASHHFRRRSFRGFWLTHHLYILLYVLLIIH--GSFALIQLPRFHIFFLvpaiiy 1260
Cdd:PLN02631  224 FAWNPTYVPNLAGTIAMVIGIAMWVTSLPSFRRKKFELFFYTHHLYGLYIVFYVIHvgDSWFCMILPNIFLFFI------ 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1261 ggDKLVSLSRKKVEISVVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPH--EDTLSLHIRA 1338
Cdd:PLN02631  298 --DRYLRFLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNleKDTLSVVIRR 375
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28872751  1339 AGPWTTRLREIYSAPTGDRcarypKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKS 1406
Cdd:PLN02631  376 QGSWTQKLYTHLSSSIDSL-----EVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELIFQS 438
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
820-881 1.82e-15

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 72.20  E-value: 1.82e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28872751  820 VESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLR 881
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
1087-1226 2.82e-12

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 64.98  E-value: 2.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   1087 RGTAASISFMFSYiLLTMCRNLITFLRetflnrYVPFDAAVDFHRLIASTAIVLTVLHSVGHVVNVYLFSISPlsvlscl 1166
Cdd:pfam01794    1 LGILALALLPLLL-LLALRNNPLEWLT------GLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLEG------- 66
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   1167 fpglfhddgselpqkYYWWFFQTVPGLTGVVLLLILAIMYVFASHHFRRRSFRGFWLTHH 1226
Cdd:pfam01794   67 ---------------ILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHI 111
PTZ00184 PTZ00184
calmodulin; Provisional
810-924 6.03e-12

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 65.17  E-value: 6.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   810 SLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGS-PEEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEISN 888
Cdd:PTZ00184   39 SLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLT 118
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 28872751   889 NclskaqlaEVVESMFRESGFQDKEELTWEDFHFML 924
Cdd:PTZ00184  119 D--------EEVDEMIREADVDGDGQINYEEFVKMM 146
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
802-922 1.70e-11

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 63.27  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  802 LSRAEFAESLglkpqDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLR 881
Cdd:COG5126   22 LERDDFEALF-----RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 28872751  882 SFieisnnCLSKAQLAEVVESMFR-ESGFQDKEELT--WEDFHF 922
Cdd:COG5126   97 AL------GVSEEEADELFARLDTdGDGKISFEEFVaaVRDYYT 134
EF-hand_7 pfam13499
EF-hand domain pair;
823-881 9.59e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 58.80  E-value: 9.59e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28872751    823 MFSLADKDGNGYLSFREFLDILVVFMKGSP--EEKSRLMFRMYDFDGNGLISKDEFIRMLR 881
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEPlsDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PLN02283 PLN02283
alpha-dioxygenase
146-304 5.36e-10

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 64.01  E-value: 5.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   146 FQRSRWDPeTGrSPSNPRDPANQVTGWLDGSAIYGSSHSWSDALRSFSRGQLASGPDPAFPRDSQNPllmwaapdPATG- 224
Cdd:PLN02283  189 FYKTKEVP-TG-SPDIKTGSLNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKISEDGLLLHDEDGI--------PISGd 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   225 -QNGPRGLYAfgaergnrepfLQALgllWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQ-K 302
Cdd:PLN02283  259 vRNSWAGVSL-----------LQAL---FVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVELLKtD 324

                  ..
gi 28872751   303 TL 304
Cdd:PLN02283  325 TL 326
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
857-915 9.08e-08

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 50.24  E-value: 9.08e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28872751  857 RLMFRMYDFDGNGLISKDEFIRMLRSfieisnncLSKAQLAEVVESMFRE-----SGFQDKEEL 915
Cdd:cd00051    3 REAFRLFDKDGDGTISADELKAALKS--------LGEGLSEEEIDEMIREvdkdgDGKIDFEEF 58
EF-hand_7 pfam13499
EF-hand domain pair;
853-925 4.64e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.40  E-value: 4.64e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28872751    853 EEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEisNNCLSKaqlaEVVESMFRESGFQDKEELTWEDFHFMLR 925
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEE--GEPLSD----EEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
859-883 4.89e-06

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 44.29  E-value: 4.89e-06
                            10        20
                    ....*....|....*....|....*
gi 28872751     859 MFRMYDFDGNGLISKDEFIRMLRSF 883
Cdd:smart00054    5 AFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
32-591 0e+00

Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase like subfamily play vital roles in the innate mucosal immunity of gut epithelia. They provide reactive oxygen species which help control infection.


Pssm-ID: 188652 [Multi-domain]  Cd Length: 558  Bit Score: 911.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   32 FDGWYNNLMEHRWGSKGSRLQRLVPASYADGVYQPLGEpHLPNPRDLSNTISRGPAGLASLRNRTVLGVFFGYHVLSDLV 111
Cdd:cd09820    1 YDGWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGE-ERPNPRSLSNLLMKGESGLPSTRNRTALLVFFGQHVVSEIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  112 SVETPGCPAEFLNIRIPPGDPMFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDPANQVTGWLDGSAIYGSSHSWSDALRS 191
Cdd:cd09820   80 DASRPGCPPEYFNIEIPKGDPVFDPECTGNIELPFQRSRYDKNTGYSPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  192 FSRGQLASGPDPAFPRDSQNPLLMWAAPDPAT-GQNGPRGLYAFGAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDW 270
Cdd:cd09820  160 FSGGRLASGDDGGFPRRNTNRLPLANPPPPSYhGTRGPERLFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDW 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  271 EDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPEYTGYRPFLDPSISSEFVAASEQFLSTMVPPGVYMRNASCHFQGV 350
Cdd:cd09820  240 SDEDIFQEARKWVIATYQNIVFYEWLPALLGTNVPPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVYRRNRQCNFREV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  351 INrNSSVSRALRVCNSYWSREHPSLQSaeDVDALLLGMASQIAEREDHVLVEDVRDFWPGPLKFSRTDHLASCLQRGRDL 430
Cdd:cd09820  320 LT-TSGGSPALRLCNTYWNSQEPLLKS--DIDELLLGMASQIAEREDNIIVEDLRDYLFGPLEFSRRDLMALNIQRGRDH 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  431 GLPSYTKARAALGLSPITRWQDINPALSRSNDTVLEATAALYNQDLSWLELLPGGLLESHRD-PGPLFSTIVLEQFVRLR 509
Cdd:cd09820  397 GLPDYNTAREAFGLPPRTTWSDINPDLFKKDPELLERLAELYGNDLSKLDLYVGGMLESKGGgPGELFRAIILDQFQRLR 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  510 DGDRYWFENTRNGLFSKKEIEEIRNTTLQDVLVAVINIDPSALQPNVFVWHKGDPCPQPRQLSTEGLPACAPSVVRDYFE 589
Cdd:cd09820  477 DGDRFWFENVKNGLFTAEEIEEIRNTTLRDVILAVTDIDNTDLQKNVFFWKNGDPCPQPKQLTENMLEPCTPLTVYDYFE 556

                 ..
gi 28872751  590 GS 591
Cdd:cd09820  557 GS 558
An_peroxidase pfam03098
Animal haem peroxidase;
30-557 3.87e-168

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 516.72  E-value: 3.87e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751     30 QRFDGWYNNLMEHRWGSKGSRLQRLVPASYADGVYQPLGEPH---LPNPRDLSNTISRGPAGLASlRNRTVLGVFFGYHV 106
Cdd:pfam03098    2 RTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSSSgspLPSPRLVSNKLFAGDSGIPD-PNLTLLLMQWGQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    107 LSDLVSVETPGCPAEF---------------LNIRIPPGDPMFDPdqRGDVVLPFQRSRWDPETGrspsNPRDPANQVTG 171
Cdd:pfam03098   81 DHDLTLTPESTSPNGSscdcccppenlhppcFPIPIPPDDPFFSP--FGVRCMPFVRSAPGCGLG----NPREQINQVTS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    172 WLDGSAIYGSSHSWSDALRSFSRGQLASGpdpafpRDSQNPLLMWAAPDPATGQNGPRGLYAF--GAERGNREPFLQALG 249
Cdd:pfam03098  155 FLDGSQVYGSSEETARSLRSFSGGLLKVN------RSDDGKELLPFDPDGPCCCNSSGGVPCFlaGDSRANENPGLTALH 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    250 LLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQK--------TLPEYTGYRPFLDPSISSE 321
Cdd:pfam03098  229 TLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEdnmnwfglLPLPYNGYDPNVDPSISNE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    322 FVAASEQFLSTMVPPGVYMRNaschfqgviNRNSSVSRALRVCNSYWSrehPSLQSAEDVDALLLGMASQIAEREDHVLV 401
Cdd:pfam03098  309 FATAAFRFGHSLIPPFLYRLD---------ENNVPEEPSLRLHDSFFN---PDRLYEGGIDPLLRGLATQPAQAVDNNFT 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    402 EDVRDFWPGPL-KFSRTDHLASCLQRGRDLGLPSYTKARAALGLSPITRWQDINPALSrsnDTVLEATAALYNqdlswle 480
Cdd:pfam03098  377 EELTNHLFGPPgEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIP---NEVIAKLRELYG------- 446
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751    481 llpgglleshrDP--------------------GPLFSTIVLEQFVRLRDGDRYWFENTRNGLFSKKEIEEIRNTTLQDV 540
Cdd:pfam03098  447 -----------SVddidlwvgglaekplpgglvGPTFACIIGDQFRRLRDGDRFWYENGNQGSFTPEQLEEIRKTSLARV 515
                          570
                   ....*....|....*..
gi 28872751    541 LVAVINIDPSaLQPNVF 557
Cdd:pfam03098  516 ICDNTDIIET-IQPNVF 531
peroxinectin_like_bacterial cd09822
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ...
72-558 8.19e-87

Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are diverse family of enzymes which are not restricted to animals. Members are also found in metazoans, fungi, and plants, and also in bacteria - like most members of this family of uncharacterized proteins.


Pssm-ID: 188654 [Multi-domain]  Cd Length: 420  Bit Score: 290.37  E-value: 8.19e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   72 LPNPRDLSNTISRGPAGLASLRNrtvlgvffgyhvLSDLVSVEtpgcpAEFLnirippgdpmfdpdqrgdvvlpfqrsrw 151
Cdd:cd09822    2 RPSPREISNAVADQTESIPNSRG------------LSDWFWVW-----GQFL---------------------------- 36
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  152 DPETGRSPSNPRDPANQVTGWLDGSAIYGSSHSWSDALRSFSRGQLASGPDPA---FPRDSQNPllmwaapDPATGQNGP 228
Cdd:cd09822   37 DHDIDLTPDNPREQINAITAYIDGSNVYGSDEERADALRSFGGGKLKTSVANAgdlLPFNEAGL-------PNDNGGVPA 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  229 RGLYAFGAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFL-QKTLPEY 307
Cdd:cd09822  110 DDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLgENALPAY 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  308 TGYRPFLDPSISSEFVAASEQFLSTMVPPgvymrnaschFQGVINRNSSVSRALRVCNSYWsreHPSLQSAEDVDALLLG 387
Cdd:cd09822  190 SGYDETVNPGISNEFSTAAYRFGHSMLSS----------ELLRGDEDGTEATSLALRDAFF---NPDELEENGIDPLLRG 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  388 MASQIAEREDHVLVEDVRDFWPGPLKFSRTDhLASC-LQRGRDLGLPSYTKARAALGLSPITRWQDINpalsrSNDTVLE 466
Cdd:cd09822  257 LASQVAQEIDTFIVDDVRNFLFGPPGAGGFD-LAALnIQRGRDHGLPSYNQLREALGLPAVTSFSDIT-----SDPDLAA 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  467 ATAALY----NQDLsWLELLPgglleshRDP------GPLFSTIVLEQFVRLRDGDRYWFENTRnglFSKKEIEEIRNTT 536
Cdd:cd09822  331 RLASVYgdvdQIDL-WVGGLA-------EDHvngglvGETFSTIIADQFTRLRDGDRFFYENDD---LLLDEIADIENTT 399
                        490       500
                 ....*....|....*....|..
gi 28872751  537 LQDVLVAviNIDPSALQPNVFV 558
Cdd:cd09822  400 LADVIRR--NTDVDDIQDNVFL 419
An_peroxidase_like cd05396
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ...
167-543 2.39e-69

Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes prostaglandin G/H synthase, thyroid peroxidase, myeloperoxidase, linoleate diol synthase, lactoperoxidase, peroxinectin, peroxidasin, and others. Despite its name, this family is not restricted to metazoans: members are found in fungi, plants, and bacteria as well.


Pssm-ID: 188647 [Multi-domain]  Cd Length: 370  Bit Score: 238.10  E-value: 2.39e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  167 NQVTGWLDGSAIYGSSHSWSDALRSFSRGQLASGPDPAFPRDSQNPLLMWAAPDPATGQNGPRGLYAFGAERGNREPFLQ 246
Cdd:cd05396    3 NARTPYLDGSSIYGSNPDVARALRTFKGGLLKTNEVKGPSYGTELLPFNNPNPSMGTIGLPPTRCFIAGDPRVNENLLLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  247 ALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPEYTG-----YRPFLDPSISSE 321
Cdd:cd05396   83 AVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDlvllfPDPDVVPYVLSE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  322 FVAASEQFLSTMVPPGVYMRNAscHFQGVINRNSSVSRALrvcNSYWSrehpSLQSAEDVDALLLGMASQIAEREDHVLV 401
Cdd:cd05396  163 FFTAAYRFGHSLVPEGVDRIDE--NGQPKEIPDVPLKDFF---FNTSR----SILSDTGLDPLLRGFLRQPAGLIDQNVD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  402 EDVRDFwpGPLKFSRTDHLASCLQRGRDLGLPSYTKARAALGLSPITRWQDINpalsrSNDTVLEATAALY----NQDLS 477
Cdd:cd05396  234 DVMFLF--GPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDIL-----TDPELAKKLAELYgdpdDVDLW 306
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28872751  478 WLELLPGGLLESHrdPGPLFSTIVLEQFVRLRDGDRYWFENTRN-GLFSKKEIEEIrnTTLQDVLVA 543
Cdd:cd05396  307 VGGLLEKKVPPAR--LGELLATIILEQFKRLVDGDRFYYVNYNPfGKSGKEELEKL--ISLADIICL 369
peroxinectin_like cd09823
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ...
163-537 7.53e-67

peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a role in invertebrate immunity mechanisms. Specifically, peroxinectins are secreted as cell-adhesive and opsonic peroxidases. The immunity mechanism appears to involve an interaction between peroxinectin and a transmembrane receptor of the integrin family. Human myeloperoxidase, which is included in this wider family, has also been reported to interact with integrins.


Pssm-ID: 188655 [Multi-domain]  Cd Length: 378  Bit Score: 231.31  E-value: 7.53e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  163 RDPANQVTGWLDGSAIYGSSHSWSDALRSFSRGQLASGpdpafpRDSQNPLLMWAAPDPATGQNGPRGLYAF--GAERGN 240
Cdd:cd09823    1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQ------RRNGRELLPFSNNPTDDCSLSSAGKPCFlaGDGRVN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  241 REPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPE-----------YTG 309
Cdd:cd09823   75 EQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEkfglylltsgyFNG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  310 YRPFLDPSISSEFVAASEQFLSTMVPPGVYMRNASCHFQGVINRNSSVSRALRvcnsywsrehpsLQSAEDVDALLLGMA 389
Cdd:cd09823  155 YDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENYRPQGSVNLHDLFFNPDR------------LYEEGGLDPLLRGLA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  390 SQIAERED-HVLVEDVRDFWPGPLKFSRTDhLASC-LQRGRDLGLPSYTKARAALGLSPITRWQDINPALSRSNdtvLEA 467
Cdd:cd09823  223 TQPAQKVDrFFTDELTTHFFFRGGNPFGLD-LAALnIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIMSPET---IQK 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  468 TAALYNqdlswlellpgglleSHRD-----------P------GPLFSTIVLEQFVRLRDGDRYWFENT-RNGLFSKKEI 529
Cdd:cd09823  299 LRRLYK---------------SVDDidlyvgglsekPvpgglvGPTFACIIGEQFRRLRRGDRFWYENGgQPSSFTPAQL 363

                 ....*...
gi 28872751  530 EEIRNTTL 537
Cdd:cd09823  364 NEIRKVSL 371
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
1277-1551 3.04e-55

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 191.36  E-value: 3.04e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1277 VVKAELLP-SGVTHLRFQRPQGFEYKSGQWVRIACLAL-GTTEYHPFTLTSAPHE--DTLSLHIRA-AGPWTTRLREIYS 1351
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAkKGFTTRLLRKALK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1352 APTgdrCARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVSCQvfCKKIYFIWVTRTQRQFEW 1431
Cdd:cd06186   81 SPG---GGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSR--TRRVKLVWVVRDREDLEW 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1432 LADIIRevEENDHQDLVSVHIYITQlaekfdlrttmlyicerhfqkvlnrslftglrsithfgrppfepffnslqevhpq 1511
Cdd:cd06186  156 FLDELR--AAQELEVDGEIEIYVTR------------------------------------------------------- 178
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 28872751 1512 vrkigVFSCGPPGMTKNVEKACqliNRQDRTHFSHHYENF 1551
Cdd:cd06186  179 -----VVVCGPPGLVDDVRNAV---AKKGGTGVEFHEESF 210
peroxidasin_like cd09826
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ...
162-564 2.23e-51

Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted heme peroxidase which is involved in hydrogen peroxide metabolism and peroxidative reactions in the cardiovascular system. The domain co-occurs with extracellular matrix domains and may play a role in the formation of the extracellular matrix.


Pssm-ID: 188658  Cd Length: 440  Bit Score: 188.28  E-value: 2.23e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  162 PRDPANQVTGWLDGSAIYGSSHSWSDALR--SFSRGQLASGPdpafPRDSQNPLLMWAAPDPATGQNGPRG----LYAFG 235
Cdd:cd09826   36 PREQINQLTSYIDASNVYGSSDEEALELRdlASDRGLLRVGI----VSEAGKPLLPFERDSPMDCRRDPNEspipCFLAG 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  236 AERGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFL----QKTLPEYTGYR 311
Cdd:cd09826  112 DHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQHITYSHWLPKILgpvgMEMLGEYRGYN 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  312 PFLDPSISSEFVAASEQFLSTMVPPGVYMRNASchFQGVINRNSSVSRAlrvcnsYWSREHpsLQSAEDVDALLLGM--- 388
Cdd:cd09826  192 PNVNPSIANEFATAAFRFGHTLINPILFRLDED--FQPIPEGHLPLHKA------FFAPYR--LVNEGGIDPLLRGLfat 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  389 ------ASQIAEREdhvLVEDVrdfwpgplkFSRTDHLASCL-----QRGRDLGLPSYTKARAALGLSPITRWQDINPAL 457
Cdd:cd09826  262 aakdrvPDQLLNTE---LTEKL---------FEMAHEVALDLaalniQRGRDHGLPGYNDYRKFCNLSVAETFEDLKNEI 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  458 srSNDTVLEATAALY----NQDLsWLELLPGGLLESHRdPGPLFSTIVLEQFVRLRDGDRYWFENtrNGLFSKKEIEEIR 533
Cdd:cd09826  330 --KNDDVREKLKRLYghpgNIDL-FVGGILEDLLPGAR-VGPTLACLLAEQFRRLRDGDRFWYEN--PGVFSPAQLTQIK 403
                        410       420       430
                 ....*....|....*....|....*....|..
gi 28872751  534 NTTLQDVLVAV-INIDpsALQPNVFVWHKGDP 564
Cdd:cd09826  404 KTSLARVLCDNgDNIT--RVQEDVFLVPGNPH 433
thyroid_peroxidase cd09825
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ...
45-558 1.02e-38

Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is expressed in the thyroid and involved in the processing of iodine and iodine compounds. Specifically, TPO oxidizes iodide via hydrogen peroxide to form active iodine, which is then, for example, incorporated into the tyrosine residues of thyroglobulin to yield mono- and di-iodotyrosines.


Pssm-ID: 188657 [Multi-domain]  Cd Length: 565  Bit Score: 153.75  E-value: 1.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   45 GSKGSRLQRLVPASYADGVYQPLG--------EPHLPNPRDLSNTISRGPAGLASL-RNRTVLGVFFGYHVLSDL----- 110
Cdd:cd09825    1 GASNTPLARWLPPIYEDGFSEPVGwnkerlynGFTLPSVREVSNKIMRTSSTAVTPdDLYSHMLTVWGQYIDHDIdftpq 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  111 -VSVETPG----CPA--EFLNIRIPPGDPMFDPDQRGDVVLPFQRSRWDPETGRSPS--------NPRDPANQVTGWLDG 175
Cdd:cd09825   81 sVSRTMFIgstdCKMtcENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTlfgnlslaNPREQINGLTSFIDA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  176 SAIYGSSHSWSDALRSFS--------RGQLASGPDPAFPrdSQNPLLMWAAPDPATGQNGPRGLYafGAERGNREPFLQA 247
Cdd:cd09825  161 STVYGSTLALARSLRDLSsddgllrvNSKFDDSGRDYLP--FQPEEVSSCNPDPNGGERVPCFLA--GDGRASEVLTLTA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  248 LGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFL-----QKTLPEYTGYRPFLDPSISSEF 322
Cdd:cd09825  237 SHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILgpeafDQYGGYYEGYDPTVNPTVSNVF 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  323 VAASEQFLSTMVPPGVYMRNASchFQgvinrNSSVSRALRVCNSYWSREHPSLQSAED--VDALLLGMASQIAEREdhVL 400
Cdd:cd09825  317 STAAFRFGHATIHPTVRRLDEN--FQ-----EHPVLPNLALHDAFFSPWRLVREGGLDpvIRGLIGGPAKLVTPDD--LM 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  401 VEDVRDFWpgpLKFSRTDH--LASC-LQRGRDLGLPSYTKARAALGLSPITRWQDINPALsrSNDTVLEATAALY----N 473
Cdd:cd09825  388 NEELTEKL---FVLSNSSTldLASLnLQRGRDHGLPGYNDWREFCGLPRLATPADLATAI--ADQAVADKILDLYkhpdN 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  474 QDLsWLELLPGGLLESHRdPGPLFSTIVLEQFVRLRDGDRYWFENtrNGLFSKKEIEEIRNTTLQDVLVAviNIDPSALQ 553
Cdd:cd09825  463 IDV-WLGGLAEDFLPGAR-TGPLFACLIGKQMKALRDGDRFWWEN--SNVFTDAQRRELRKHSLSRVICD--NTGLTRVP 536

                 ....*
gi 28872751  554 PNVFV 558
Cdd:cd09825  537 PDAFQ 541
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
155-537 1.03e-34

Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of animal heme peroxidases contains members with somewhat diverse functions. Myeloperoxidases are lysosomal proteins found in azurophilic granules of neutrophils and the lysosomes of monocytes. They are involved in the formation of microbicidal agents upon activation of activated neutrophils (neutrophils undergoing respiratory bursts as a result of phagocytosis), by catalyzing the conversion of hydrogen peroxide to hypochlorous acid. As a heme protein, myeloperoxidase is responsible for the greenish tint of pus, which is rich in neutrophils. Eosinophil peroxidases are haloperoxidases as well, preferring bromide over chloride. Expressed by eosinophil granulocytes, they are involved in attacking multicellular parasites and play roles in various inflammatory diseases such as asthma. The haloperoxidase lactoperoxidase is secreted from mucosal glands and provides antibacterial activity by oxidizing a variety of substrates such as bromide or chloride in the presence of hydrogen peroxide.


Pssm-ID: 188656 [Multi-domain]  Cd Length: 411  Bit Score: 138.71  E-value: 1.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  155 TGRSPSNPRDPANQVTGWLDGSAIYGSSHSWSDALRSFS--RGQLASGPD------PAFPRDSQNPllmwaapDPATGQN 226
Cdd:cd09824    4 ACTSKRNVREQINALTSFVDASMVYGSEPSLAK*LRNLTnqLGLLAVNQRftdnglALLPFENLHN-------DPCALRN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  227 GPRGLYAF--GAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFL---- 300
Cdd:cd09824   77 TSANIPCFlaGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILgeda 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  301 QKTLPEYTGYRPFLDPSISSEFVAASeQFLSTMVPPGVYMRNASCHFQGvinRNSSVSRALRVCNSYwsrehpSLQSAED 380
Cdd:cd09824  157 AARLPPYRGYNESVDPRIANVFTTAF-RRGHTTVQPFVFRLDENYQPHP---PNPQVPLHKAFFASW------RIIREGG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  381 VDALLLGMASQIAE--REDHVLVEDVRDFWPGPLKFSRTDHLASCLQRGRDLGLPSYTKARAALGLSPITRWQDINPALs 458
Cdd:cd09824  227 IDPILRGLMATPAKlnNQNQMLVDELRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVL- 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  459 rSNDTVLEATAALY----NQDLsWLELLPGGLLESHRdPGPLFSTIVLEQFVRLRDGDRYWFENtrNGLFSKKEIEEIRN 534
Cdd:cd09824  306 -NNTVLARKLLDLYgtpdNIDI-WIGGVAEPLVPGGR-VGPLLACLISRQFRRIRDGDRFWWEN--PGVFTEEQRESLRS 380

                 ...
gi 28872751  535 TTL 537
Cdd:cd09824  381 VSL 383
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
1380-1533 5.08e-29

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 113.97  E-value: 5.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   1380 FEVSVLVGGGIGVTPFASILKDLVFKSSVSCQvfcKKIYFIWVTRTQRQFEWLADIIREVEENDHQDlVSVHIYITQLAE 1459
Cdd:pfam08030    1 YENVLLVAGGIGITPFISILKDLGNKSKKLKT---KKIKFYWVVRDLSSLEWFKDVLNELEELKELN-IEIHIYLTGEYE 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28872751   1460 KFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRkIGVFSCGPPGMTKNVEKAC 1533
Cdd:pfam08030   77 AEDASDQSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGS-IGVFSCGPPSLVDELRNLV 149
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
1277-1544 1.79e-21

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 94.82  E-value: 1.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1277 VVKAELLPSgVTHLRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPHE-DTLSLHIRAA--GPWTTRLREIysaP 1353
Cdd:cd00322    1 VATEDVTDD-VRLFRLQLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEeGELELTVKIVpgGPFSAWLHDL---K 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1354 TGDrcarypKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVscqvfcKKIYFIWVTRTQRQFeWLA 1433
Cdd:cd00322   77 PGD------EVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPG------GEITLLYGARTPADL-LFL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1434 DIIREVEENDHqdLVSVHIYITQLAEKFDLRTTMLYICERHFQKVLNRslftglrsithfgrppfepffnslQEVHpqvr 1513
Cdd:cd00322  144 DELEELAKEGP--NFRLVLALSRESEAKLGPGGRIDREAEILALLPDD------------------------SGAL---- 193
                        250       260       270
                 ....*....|....*....|....*....|..
gi 28872751 1514 kigVFSCGPPGMTKNVEKA-CQLINRQDRTHF 1544
Cdd:cd00322  194 ---VYICGPPAMAKAVREAlVSLGVPEERIHT 222
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
1286-1551 1.18e-20

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 91.93  E-value: 1.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1286 GVTHLRFqRPQG--FEYKSGQWVRIACLALGTTEYHPFTLTSAPHED-TLSLHIRAAGPWTTRLREiySAPTGDRcaryp 1362
Cdd:cd06198    8 PTTTLTL-EPRGpaLGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDgRLRFTIKALGDYTRRLAE--RLKPGTR----- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1363 kLYLDGPFG-------EGHQewhkfevsVLVGGGIGVTPFASILKDLVFKSSVscqvfcKKIYFIWVTRTQRQfewlADI 1435
Cdd:cd06198   80 -VTVEGPYGrftfddrRARQ--------IWIAGGIGITPFLALLEALAARGDA------RPVTLFYCVRDPED----AVF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1436 IREVEENDHQDLVSVHIYITqlAEKFDLRTTMLyicerhfqkvlnrslftglrsithfgrppfepffnsLQEVHPQVRKI 1515
Cdd:cd06198  141 LDELRALAAAAGVVLHVIDS--PSDGRLTLEQL------------------------------------VRALVPDLADA 182
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 28872751 1516 GVFSCGPPGMTKNVEKACQLINrQDRTHFshHYENF 1551
Cdd:cd06198  183 DVWFCGPPGMADALEKGLRALG-VPARRF--HYERF 215
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
1124-1551 1.25e-20

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 96.89  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1124 DAAVDFHRLIASTAIVLTVLHsvghvvnvYLFSISPLSVLSclfpglfhddGSELPQKYYWWF-FQTVPGLT----GVVL 1198
Cdd:COG4097   75 DRLYRLHKWLGILALVLALAH--------PLLLLGPKWLVG----------WGGLPARLAALLtLLRGLAELlgewAFYL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1199 LLILAIMYVFashhfrRRSFR-GFW-LTHHLyillyvlliihgSFALIQLPRFHIFFLVP-------------------- 1256
Cdd:COG4097  137 LLALVVLSLL------RRRLPyELWrLTHRL------------LAVAYLLLAFHHLLLGGpfywsppagvlwaalaaagl 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1257 -AIIYGgdKLVS-LSRKKVEISVVKAELLPSGVT--HLRFQRPQGFEYKSGQ--WVRIAClALGTTEYHPFTLTSAPHED 1330
Cdd:COG4097  199 aAAVYS--RLGRpLRSRRHPYRVESVEPEAGDVVelTLRPEGGRWLGHRAGQfaFLRFDG-SPFWEEAHPFSISSAPGGD 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1331 -TLSLHIRAAGPWTTRLREIysaPTGDRcarypkLYLDGPFG---------EGHQewhkfevsVLVGGGIGVTPFASILK 1400
Cdd:COG4097  276 gRLRFTIKALGDFTRRLGRL---KPGTR------VYVEGPYGrftfdrrdtAPRQ--------VWIAGGIGITPFLALLR 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1401 DLVFKSSVscqvfCKKIYFIWVTRTQRQFEWLADIIREVEENDHqdlVSVHIYITQLAEKFDLRTtmlyicerhfqkvln 1480
Cdd:COG4097  339 ALAARPGD-----QRPVDLFYCVRDEEDAPFLEELRALAARLAG---LRLHLVVSDEDGRLTAER--------------- 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28872751 1481 rslftglrsithfgrppfepffnsLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLiNRQDRTHFshHYENF 1551
Cdd:COG4097  396 ------------------------LRRLVPDLAEADVFFCGPPGMMDALRRDLRA-LGVPARRI--HQERF 439
PLN02292 PLN02292
ferric-chelate reductase
1089-1412 2.12e-20

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 98.02  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1089 TAASISF--MFSYILLTmcrNLITFLRETFLNrYVPFDAAVDFHRLIASTAIVLTV-LHSVGHVVNVYLFSisPLSVLSC 1165
Cdd:PLN02292  120 TVTEVMFlaMFMALLLW---SLANYMYNTFVT-ITPQSAATDGESLWQARLDSIAVrLGLVGNICLAFLFY--PVARGSS 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1166 LFP--GLfhddGSELPQKY---------------------YW-----------WFFQTVPGLTGVVLLLILAIMYVFASH 1211
Cdd:PLN02292  194 LLAavGL----TSESSIKYhiwlghlvmtlftshglcyiiYWismnqvsqmleWDRTGVSNLAGEIALVAGLVMWATTYP 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1212 HFRRRSFRGFWLTHHLYILLYVLLIIHG--SFALIQLPRFHIFFLvpaiiyggDKLVSLSRKKVEISVVKAELLPSGVTH 1289
Cdd:PLN02292  270 KIRRRFFEVFFYTHYLYIVFMLFFVFHVgiSFALISFPGFYIFLV--------DRFLRFLQSRNNVKLVSARVLPCDTVE 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1290 LRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAP--HEDTLSLHIRAAGPWTTRLREIYSAPTG-DRCArypkLYL 1366
Cdd:PLN02292  342 LNFSKNPMLMYSPTSIMFVNIPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLYHMLSSSDQiDRLA----VSV 417
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 28872751  1367 DGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSV-SCQV 1412
Cdd:PLN02292  418 EGPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLIYTSSTeTCKI 464
FAD_binding_8 pfam08022
FAD-binding domain;
1275-1372 2.97e-19

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 84.69  E-value: 2.97e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   1275 ISVVKAELLPSGVTHLRFQRPQG-FEYKSGQWVRIACL-ALGTTEYHPFTLTSAPHEDTLSLHIRAAGPWTTRLREIYS- 1351
Cdd:pfam08022    4 VPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFLpPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYLSs 83
                           90       100
                   ....*....|....*....|....*
gi 28872751   1352 ----APTGDrcARYPKLYLDGPFGE 1372
Cdd:pfam08022   84 scpkSPENG--KDKPRVLIEGPYGP 106
PLN02631 PLN02631
ferric-chelate reductase
1183-1406 3.66e-19

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 93.95  E-value: 3.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1183 YWWFFQTVPGLTGVVLLLILAIMYVFASHHFRRRSFRGFWLTHHLYILLYVLLIIH--GSFALIQLPRFHIFFLvpaiiy 1260
Cdd:PLN02631  224 FAWNPTYVPNLAGTIAMVIGIAMWVTSLPSFRRKKFELFFYTHHLYGLYIVFYVIHvgDSWFCMILPNIFLFFI------ 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1261 ggDKLVSLSRKKVEISVVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPH--EDTLSLHIRA 1338
Cdd:PLN02631  298 --DRYLRFLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNleKDTLSVVIRR 375
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28872751  1339 AGPWTTRLREIYSAPTGDRcarypKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKS 1406
Cdd:PLN02631  376 QGSWTQKLYTHLSSSIDSL-----EVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELIFQS 438
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
1098-1456 1.09e-17

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 89.14  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1098 SYILLTMCRNLITFlreTFLNryVPFDAAVDFHRLIASTAIVLTVLHSVghvvnvylfsisplsvlSCLFP-GLFHDDGS 1176
Cdd:PLN02844  168 ALLLLPVLRGLALF---RLLG--IQFEASVRYHVWLGTSMIFFATVHGA-----------------STLFIwGISHHIQD 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1177 ELpqkyywWFFQTVPG--LTGVVLLLILAIMYVFASHHFRRRSFRGFWLTHHLYILLYVLLIIHGSfaliqlpRFHIFFL 1254
Cdd:PLN02844  226 EI------WKWQKTGRiyLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG-------DRHFYMV 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1255 VPAI-IYGGDKLVSLSRKKVEISVVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPHED--T 1331
Cdd:PLN02844  293 FPGIfLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDdhT 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1332 LSLHIRAAGPWTTRLREIYSAP--TGDRCARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVS 1409
Cdd:PLN02844  373 MSVIIKCEGGWTNSLYNKIQAEldSETNQMNCIPVAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSR 452
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 28872751  1410 CQvFCKKIYFIWVTRTQRQFEWLADIIREVEENDHQDL-VSVHIYITQ 1456
Cdd:PLN02844  453 YR-FPKRVQLIYVVKKSQDICLLNPISSLLLNQSSNQLnLKLKVFVTQ 499
PIOX_like cd09818
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ...
33-301 6.99e-17

Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family of oxygenases related to the animal heme peroxidases, with members from plants, animals, and bacteria. The plant pathogen-inducible oxygenases (PIOX) oxygenate fatty acids into 2R-hydroperoxides. They may be involved in the hypersensitive reaction, rapid and localized cell death induced by infection with pathogens, and the rapidly induced expression of PIOX may be caused by the oxidative burst that occurs in the process of cell death.


Pssm-ID: 188650 [Multi-domain]  Cd Length: 484  Bit Score: 85.41  E-value: 6.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   33 DGWYNNLMEHRWGSKGSRLQRLVPASYAdgvyQPLGEPHL--PNPRDLSNTisrgpagLASLRNRTvlgvffgyhvlsdl 110
Cdd:cd09818    4 DGSYNDLDNPSMGSVGTRFGRNVPLDAT----FPEDKDELltPNPRVISRR-------LLARTEFK-------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  111 vsvetpgcPAEFLNirippgdpMFDPDQrgdvvLPFQRSRWdpetgrspSNPRDPA--NQVTGWLDGSAIYGSSHSWSDA 188
Cdd:cd09818   59 --------PATSLN--------LLAAAW-----IQFMVHDW--------FSHGPPTyiNTNTHWWDGSQIYGSTEEAQKR 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  189 LRSFSR-GQLASGPDPAFPRDSQNPLlmwaapdPATG--QNGPRGLyafgaergnrepflQALGLLWFRYHNLWAQRLAR 265
Cdd:cd09818  110 LRTFPPdGKLKLDADGLLPVDEHTGL-------PLTGfnDNWWVGL--------------SLLHTLFVREHNAICDALRK 168
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 28872751  266 QHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQ 301
Cdd:cd09818  169 EYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILA 204
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
1277-1545 8.45e-17

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 81.83  E-value: 8.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1277 VVKAELLPSGVTHLRFQRP-QGFEYKSGQWVRIACLalGTTEYHPFTLTSAPHED-TLSLHIRAAGPWTTRLREIysaPT 1354
Cdd:COG0543    2 VVSVERLAPDVYLLRLEAPlIALKFKPGQFVMLRVP--GDGLRRPFSIASAPREDgTIELHIRVVGKGTRALAEL---KP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1355 GDRcarypkLYLDGPFGEGhqewhkFEVS------VLVGGGIGVTPFASILKDLVFKSsvscqvfcKKIYFIWVTRTQRQ 1428
Cdd:COG0543   77 GDE------LDVRGPLGNG------FPLEdsgrpvLLVAGGTGLAPLRSLAEALLARG--------RRVTLYLGARTPED 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1429 FEWLADIireveendhQDLVSVHIYITqlaekfdlrttmlyiCERHFQKvlnrslFTGLrsITHFgrppfepffnsLQEV 1508
Cdd:COG0543  137 LYLLDEL---------EALADFRVVVT---------------TDDGWYG------RKGF--VTDA-----------LKEL 173
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 28872751 1509 HPQVRKIGVFSCGPPGMTKNVEKACQLIN-RQDRTHFS 1545
Cdd:COG0543  174 LAEDSGDDVYACGPPPMMKAVAELLLERGvPPERIYVS 211
An_peroxidase_bacterial_2 cd09821
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ...
86-557 2.38e-16

Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.


Pssm-ID: 188653 [Multi-domain]  Cd Length: 570  Bit Score: 84.39  E-value: 2.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   86 PAGLASLRNR--TVLGVFFGyHVLsDLVsvetPGCPAEFLNIRIPPGDPMFDPDQR--GDVVLPFQRSRWDPETGRSPSN 161
Cdd:cd09821    6 DAGLSAPYNSwmTFFGQFFD-HGL-DFI----PKGGNGTVLIPLPPDDPLYDLGRGtnGMALDRGTNNAGPDGILGTADG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  162 PRDPANQVTGWLDGSAIYGSSHSWSDALRSF-----SRGQLASGPDP-------AFPRD-------SQNPLLMWAAPDPA 222
Cdd:cd09821   80 EGEHTNVTTPFVDQNQTYGSHASHQVFLREYdgdgvATGRLLEGATGgsartghAFLDDiahnaapKGGLGSLRDNPTED 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  223 TGQNGPRGLYAF---------GAERGNREPFLQALGLLWFRYHNLWAQRLARQHPD----------------WEDEELFQ 277
Cdd:cd09821  160 PPGPGAPGSYDNelldahfvaGDGRVNENIGLTAVHTVFHREHNRLVDQIKDTLLQsadlafaneaggnnlaWDGERLFQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  278 HARKRVIATYQNIaVYEWLPSFLQKTLPEY---TGYRPFLDPSISSEFVAASEQFLSTMVPPGVyMRNASCHFQGVINRN 354
Cdd:cd09821  240 AARFANEMQYQHL-VFEEFARRIQPGIDGFgsfNGYNPEINPSISAEFAHAVYRFGHSMLTETV-TRIGPDADEGLDNQV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  355 SSVSRALRVCNSYwsreHPSLQSAEDVDALLLGMASQIAEREDHVLVEDVRDFWPG-PLkfsrtDHLASCLQRGRDLGLP 433
Cdd:cd09821  318 GLIDAFLNPVAFL----PATLYAEEGAGAILRGMTRQVGNEIDEFVTDALRNNLVGlPL-----DLAALNIARGRDTGLP 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  434 SYTKAR----AALG----LSPITRWQD-----------IN------PALSRSNDTVLEAT--AALYNQDLSWLELLPGGL 486
Cdd:cd09821  389 TLNEARaqlfAATGdtilKAPYESWNDfgarlknpeslINfiaaygTHLTITGATTLAAKraAAQDLVDGGDGAPADRAD 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  487 LESHRDP-----------------------------GPLFSTIVLEQFVRLRDGDRYWFENTRNGLFSKKEIEeirNTTL 537
Cdd:cd09821  469 FMNAAGAgagtvkgldnvdlwvgglaekqvpfggmlGSTFNFVFEEQMDRLQDGDRFYYLSRTAGLDLLNQLE---NNTF 545
                        570       580
                 ....*....|....*....|
gi 28872751  538 QDVLVAviNIDPSALQPNVF 557
Cdd:cd09821  546 ADMIMR--NTGATHLPQDIF 563
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
820-881 1.82e-15

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 72.20  E-value: 1.82e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28872751  820 VESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLR 881
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
1277-1534 3.03e-15

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 76.75  E-value: 3.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1277 VVKAELLPSGVTHLRFQRPQG---FEYKSGQWVRIACLALGTTEYHPFTLTSAPHEDTLSLHIR--AAGPWTTRLREiyS 1351
Cdd:COG1018    8 VVEVRRETPDVVSFTLEPPDGaplPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKrvPGGGGSNWLHD--H 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1352 APTGDRcarypkLYLDGPFG----EGHQEWHkfevSVLVGGGIGVTPFASILKDLVFKSSVScqvfckKIYFIWVTRTQR 1427
Cdd:COG1018   86 LKVGDT------LEVSGPRGdfvlDPEPARP----LLLIAGGIGITPFLSMLRTLLARGPFR------PVTLVYGARSPA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1428 QFEWLADIIREVEENDHqdlVSVHIYITQLAEKFDLRttmlyicerhfqkvLNRSLFTGLrsithfgrppfepfFNSLQE 1507
Cdd:COG1018  150 DLAFRDELEALAARHPR---LRLHPVLSREPAGLQGR--------------LDAELLAAL--------------LPDPAD 198
                        250       260
                 ....*....|....*....|....*..
gi 28872751 1508 VHpqvrkigVFSCGPPGMTKNVEKACQ 1534
Cdd:COG1018  199 AH-------VYLCGPPPMMEAVRAALA 218
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
174-285 1.39e-14

Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal prostaglandin endoperoxide synthases, including prostaglandin H2 synthase and a set of similar bacterial proteins which may function as cyclooxygenases. Prostaglandin H2 synthase catalyzes the synthesis of prostaglandin H2 from arachidonic acid. In two reaction steps, arachidonic acid is converted to Prostaglandin G2, a peroxide (cyclooxygenase activity) and subsequently converted to the end product via the enzyme's peroxidase activity. Prostaglandin H2 synthase is the target of aspirin and other non-steroid anti-inflammatory drugs such as ibuprofen, which block the substrate's access to the active site and may acetylate a conserved serine residue. In humans and other mammals, prostaglandin H2 synthase (PGHS), also called cyclooxygenase (COX) is present as at least two isozymes, PGHS-1 (or COX-1) and PGHS-2 (or COX-2), respectively. PGHS-1 is expressed constitutively in most mammalian cells, while the expression of PGHS-2 is induced via inflammation response in endothelial cells, activated macrophages, and others. COX-3 is a splice variant of COX-1.


Pssm-ID: 188648 [Multi-domain]  Cd Length: 490  Bit Score: 78.46  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  174 DGSAIYGSSHSWSDALRSFSRGQLAS----------------GPDPAFPRDSqnPLLMWAAPDPAtgqngPRGLYAFGAE 237
Cdd:cd09816  132 DLSQIYGLTEARTHALRLFKDGKLKSqmingeeyppylfedgGVKMEFPPLV--PPLGDELTPER-----EAKLFAVGHE 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 28872751  238 RGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIA 285
Cdd:cd09816  205 RFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIG 252
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
1087-1226 2.82e-12

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 64.98  E-value: 2.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   1087 RGTAASISFMFSYiLLTMCRNLITFLRetflnrYVPFDAAVDFHRLIASTAIVLTVLHSVGHVVNVYLFSISPlsvlscl 1166
Cdd:pfam01794    1 LGILALALLPLLL-LLALRNNPLEWLT------GLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLEG------- 66
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   1167 fpglfhddgselpqkYYWWFFQTVPGLTGVVLLLILAIMYVFASHHFRRRSFRGFWLTHH 1226
Cdd:pfam01794   67 ---------------ILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHI 111
PTZ00184 PTZ00184
calmodulin; Provisional
810-924 6.03e-12

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 65.17  E-value: 6.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   810 SLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGS-PEEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEISN 888
Cdd:PTZ00184   39 SLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLT 118
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 28872751   889 NclskaqlaEVVESMFRESGFQDKEELTWEDFHFML 924
Cdd:PTZ00184  119 D--------EEVDEMIREADVDGDGQINYEEFVKMM 146
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
802-922 1.70e-11

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 63.27  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  802 LSRAEFAESLglkpqDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLR 881
Cdd:COG5126   22 LERDDFEALF-----RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 28872751  882 SFieisnnCLSKAQLAEVVESMFR-ESGFQDKEELT--WEDFHF 922
Cdd:COG5126   97 AL------GVSEEEADELFARLDTdGDGKISFEEFVaaVRDYYT 134
EF-hand_7 pfam13499
EF-hand domain pair;
823-881 9.59e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 58.80  E-value: 9.59e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28872751    823 MFSLADKDGNGYLSFREFLDILVVFMKGSP--EEKSRLMFRMYDFDGNGLISKDEFIRMLR 881
Cdd:pfam13499    7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEPlsDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
819-920 3.26e-10

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 59.60  E-value: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  819 FVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEisnnclskaqlAE 898
Cdd:cd15898    1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTE-----------RP 69
                         90       100
                 ....*....|....*....|..
gi 28872751  899 VVESMFRESGFQDKEELTWEDF 920
Cdd:cd15898   70 ELEPIFKKYAGTNRDYMTLEEF 91
PLN02283 PLN02283
alpha-dioxygenase
146-304 5.36e-10

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 64.01  E-value: 5.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   146 FQRSRWDPeTGrSPSNPRDPANQVTGWLDGSAIYGSSHSWSDALRSFSRGQLASGPDPAFPRDSQNPllmwaapdPATG- 224
Cdd:PLN02283  189 FYKTKEVP-TG-SPDIKTGSLNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKISEDGLLLHDEDGI--------PISGd 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   225 -QNGPRGLYAfgaergnrepfLQALgllWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQ-K 302
Cdd:PLN02283  259 vRNSWAGVSL-----------LQAL---FVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVELLKtD 324

                  ..
gi 28872751   303 TL 304
Cdd:PLN02283  325 TL 326
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
1287-1402 1.52e-09

Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 59.56  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1287 VTH----LRFQRPQGFEYKSGQWVRIACLALG-TTEYHPFTLTSAPHEDTLSLHIRaagpwttrlreIYSAPTG--DRCA 1359
Cdd:cd06196   11 VTHdvkrLRFDKPEGYDFTPGQATEVAIDKPGwRDEKRPFTFTSLPEDDVLEFVIK-----------SYPDHDGvtEQLG 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 28872751 1360 RY---PKLYLDGPF------GEGhqewhkfevsVLVGGGIGVTPFASILKDL 1402
Cdd:cd06196   80 RLqpgDTLLIEDPWgaieykGPG----------VFIAGGAGITPFIAILRDL 121
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
1290-1551 2.78e-09

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99811 [Multi-domain]  Cd Length: 231  Bit Score: 59.14  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1290 LRFQRPQG--FEYKSGQWVRIACLALGTTEYHPFTLTSAPHE-DTLSLHIR--AAGP---W-TTRLREiysaptGDRcar 1360
Cdd:cd06215   16 FRFAAPDGslFAYKPGQFLTLELEIDGETVYRAYTLSSSPSRpDSLSITVKrvPGGLvsnWlHDNLKV------GDE--- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1361 ypkLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVfksSVSCQVfckKIYFIWVTRTQrqfewlADII--RE 1438
Cdd:cd06215   87 ---LWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLL---DTRPDA---DIVFIHSARSP------ADIIfaDE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1439 VEENDHQ-DLVSVHIYITQLAEKfdlrttmlyiCERHFQKVLNRSLftglrsithfgrppfepffnsLQEVHPQVRKIGV 1517
Cdd:cd06215  152 LEELARRhPNFRLHLILEQPAPG----------AWGGYRGRLNAEL---------------------LALLVPDLKERTV 200
                        250       260       270
                 ....*....|....*....|....*....|....
gi 28872751 1518 FSCGPPGMTKNVEKACQLINrQDRTHFshHYENF 1551
Cdd:cd06215  201 FVCGPAGFMKAVKSLLAELG-FPMSRF--HQESF 231
PTZ00183 PTZ00183
centrin; Provisional
810-928 6.09e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 56.62  E-value: 6.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751   810 SLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFM-KGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRsfiEISN 888
Cdd:PTZ00183   45 SLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKKLgERDPREEILKAFRLFDDDKTGKISLKNLKRVAK---ELGE 121
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 28872751   889 NcLSKAQLAEVVEsmfresgFQDKE---ELTWEDFHFMLRDHN 928
Cdd:PTZ00183  122 T-ITDEELQEMID-------EADRNgdgEISEEEFYRIMKKTN 156
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
1276-1527 1.36e-08

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 57.17  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1276 SVVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIaclALGTTEYHPFTLTSAPHED-TLSLHIRAAGPWTTRLREIYSAPT 1354
Cdd:cd06189    2 KVESIEPLNDDVYRVRLKPPAPLDFLAGQYLDL---LLDDGDKRPFSIASAPHEDgEIELHIRAVPGGSFSDYVFEELKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1355 GDrcarypKLYLDGPFGEGH-QEWHKFEVsVLVGGGIGVTPFASILKDLVFKSsvscqvFCKKIYFIWVTRTQRQFEWLA 1433
Cdd:cd06189   79 NG------LVRIEGPLGDFFlREDSDRPL-ILIAGGTGFAPIKSILEHLLAQG------SKRPIHLYWGARTEEDLYLDE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1434 DIIREVEENDHQDLVSVhiyITQLAEKFDLRTTMLYicerhfQKVLNRslftglrsithfgrppfepfFNSLQEVHpqvr 1513
Cdd:cd06189  146 LLEAWAEAHPNFTYVPV---LSEPEEGWQGRTGLVH------EAVLED--------------------FPDLSDFD---- 192
                        250
                 ....*....|....
gi 28872751 1514 kigVFSCGPPGMTK 1527
Cdd:cd06189  193 ---VYACGSPEMVY 203
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
1289-1533 3.55e-08

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 56.08  E-value: 3.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1289 HLRFQRPQGFEYKSGQWVRIACLALGTTeyhPFTLTSAPHE-DTLSLHIRAAGPWTtrlREIYSAPTGDrcarypKLYLD 1367
Cdd:cd06221   17 RLEDDDEELFTFKPGQFVMLSLPGVGEA---PISISSDPTRrGPLELTIRRVGRVT---EALHELKPGD------TVGLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1368 GPFGEGH--QEWHKFEVsVLVGGGIGVTPFASILKDLV-----FkssvscqvfcKKIYFIWVTRTQrqfewlADII--RE 1438
Cdd:cd06221   85 GPFGNGFpvEEMKGKDL-LLVAGGLGLAPLRSLINYILdnredY----------GKVTLLYGARTP------EDLLfkEE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1439 VEENDHQDLVSVHIYITQLAEKFDLRTtmlyicerhfqkvlnrslftglrsithfGRPPfepffNSLQEVHPQVRKIGVF 1518
Cdd:cd06221  148 LKEWAKRSDVEVILTVDRAEEGWTGNV----------------------------GLVT-----DLLPELTLDPDNTVAI 194
                        250
                 ....*....|....*
gi 28872751 1519 SCGPPGMTKNVEKAC 1533
Cdd:cd06221  195 VCGPPIMMRFVAKEL 209
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
857-915 9.08e-08

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 50.24  E-value: 9.08e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28872751  857 RLMFRMYDFDGNGLISKDEFIRMLRSfieisnncLSKAQLAEVVESMFRE-----SGFQDKEEL 915
Cdd:cd00051    3 REAFRLFDKDGDGTISADELKAALKS--------LGEGLSEEEIDEMIREvdkdgDGKIDFEEF 58
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
1290-1471 3.97e-07

Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 52.95  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1290 LRFQRPQGFEYKSGQWVRIAcLALGTTEY--HPFTLTSAPHEDTLSLHIRA--AGPWTTRLreiYSAPTGDRcarypkLY 1365
Cdd:cd06195   15 FRVTRDIPFRFQAGQFTKLG-LPNDDGKLvrRAYSIASAPYEENLEFYIILvpDGPLTPRL---FKLKPGDT------IY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1366 LD-GPFG--------EGHQEWhkfevsvLVGGGIGVTPFASILKDLvfksSVSCQvfCKKIYFIWVTRTQ---------- 1426
Cdd:cd06195   85 VGkKPTGfltldevpPGKRLW-------LLATGTGIAPFLSMLRDL----EIWER--FDKIVLVHGVRYAeelayqdeie 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 28872751 1427 -------RQFEWLADIIREVEENDHQDLVSVHIYITQLAEKFDLR----TTMLYIC 1471
Cdd:cd06195  152 alakqynGKFRYVPIVSREKENGALTGRIPDLIESGELEEHAGLPldpeTSHVMLC 207
EF-hand_7 pfam13499
EF-hand domain pair;
853-925 4.64e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.40  E-value: 4.64e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28872751    853 EEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEisNNCLSKaqlaEVVESMFRESGFQDKEELTWEDFHFMLR 925
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEE--GEPLSD----EEVEELFKEFDLDKDGRISFEEFLELYS 67
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
1277-1412 2.40e-06

FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 50.79  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1277 VVKAELLPSGVTHLRFQRPQG-FEYKSGQWVRIACLALGTTEYHPFTLTSA-PHEDTLSLHIRAAGPWTtrlREIYSAPT 1354
Cdd:cd06192    1 IVKKEQLEPNLVLLTIKAPLAaRLFRPGQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRGPKT---KLIAELKP 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 28872751 1355 GDrcarypKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKdlvFKSSVSCQV 1412
Cdd:cd06192   78 GE------KLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAK---KLAANGNKV 126
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
802-844 3.69e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 45.62  E-value: 3.69e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 28872751  802 LSRAEFAE---SLGLKPQDMFVESMFSLADKDGNGYLSFREFLDIL 844
Cdd:cd00051   17 ISADELKAalkSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
859-883 4.89e-06

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 44.29  E-value: 4.89e-06
                            10        20
                    ....*....|....*....|....*
gi 28872751     859 MFRMYDFDGNGLISKDEFIRMLRSF 883
Cdd:smart00054    5 AFRLFDKDGDGKIDFEEFKDLLKAL 29
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
1277-1402 6.41e-06

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99784 [Multi-domain]  Cd Length: 224  Bit Score: 49.13  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1277 VVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIaclalgTTEYHP-----FTLTSAPHED-TLSLHIRAA-GPWTTR-LRE 1348
Cdd:cd06187    1 VVSVERLTHDIAVVRLQLDQPLPFWAGQYVNV------TVPGRPrtwraYSPANPPNEDgEIEFHVRAVpGGRVSNaLHD 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 28872751 1349 iySAPTGDRcarypkLYLDGPFGEGH-QEWHKFEVsVLVGGGIGVTPFASILKDL 1402
Cdd:cd06187   75 --ELKVGDR------VRLSGPYGTFYlRRDHDRPV-LCIAGGTGLAPLRAIVEDA 120
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
859-883 1.08e-05

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 43.54  E-value: 1.08e-05
                           10        20
                   ....*....|....*....|....*
gi 28872751    859 MFRMYDFDGNGLISKDEFIRMLRSF 883
Cdd:pfam00036    5 IFRLFDKDGDGKIDFEEFKELLKKL 29
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
1290-1538 1.55e-05

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 48.65  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1290 LRFQRPQ---GFEYKSGQWVRIACLALGTTeyhPFTLTSAP-HEDTLSLHIRAAGPWTT---RLREiysaptGDrcaryp 1362
Cdd:PRK08345   25 LRFEDPElaeSFTFKPGQFVQVTIPGVGEV---PISICSSPtRKGFFELCIRRAGRVTTvihRLKE------GD------ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1363 KLYLDGPFGEGH--QEWHKFEVsVLVGGGIGVTPFASilkdlVFKSSVSCQVFCKKIYFIWVTRTQRQFEWLADIIREVE 1440
Cdd:PRK08345   90 IVGVRGPYGNGFpvDEMEGMDL-LLIAGGLGMAPLRS-----VLLYAMDNRWKYGNITLIYGAKYYEDLLFYDELIKDLA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1441 endHQDLVSVHIYITqlaekFDLRTTMLYICERHFQKVLNRSLFTGLrsithfgrppfepffnsLQEVHPQVRKIGVFSC 1520
Cdd:PRK08345  164 ---EAENVKIIQSVT-----RDPEWPGCHGLPQGFIERVCKGVVTDL-----------------FREANTDPKNTYAAIC 218
                         250
                  ....*....|....*...
gi 28872751  1521 GPPGMTKNVEKAcqLINR 1538
Cdd:PRK08345  219 GPPVMYKFVFKE--LINR 234
EF-hand_8 pfam13833
EF-hand domain pair;
831-880 1.63e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 43.84  E-value: 1.63e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 28872751    831 GNGYLSFREFLDILVVF-MKGSPEEKSRLMFRMYDFDGNGLISKDEFIRML 880
Cdd:pfam13833    1 EKGVITREELKRALALLgLKDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
1277-1441 1.65e-05

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 48.10  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1277 VVKAELLPSGVTHLRFQ--RPQGFEYKSGQWVRIAclALGTTEYHPFTLTSAPHEDT-LSLHIRA--AGPWTTRLREiyS 1351
Cdd:cd06212    5 VVAVEALTHDIRRLRLRleEPEPIKFFAGQYVDIT--VPGTEETRSFSMANTPADPGrLEFIIKKypGGLFSSFLDD--G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1352 APTGDrcarypKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVscqvfcKKIYFIWVTRTQRQFEW 1431
Cdd:cd06212   81 LAVGD------PVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSD------RPVRFFYGARTARDLFY 148
                        170
                 ....*....|
gi 28872751 1432 LaDIIREVEE 1441
Cdd:cd06212  149 L-EEIAALGE 157
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
819-923 1.77e-05

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 46.07  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  819 FVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRSfieisnncLSKAqlAE 898
Cdd:cd16202    1 WLKDQFRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQFYNR--------LTKR--PE 70
                         90       100
                 ....*....|....*....|....*.
gi 28872751  899 VVESMFRESgfQDKEELTWEDF-HFM 923
Cdd:cd16202   71 IEELFKKYS--GDDEALTVEELrRFL 94
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
820-844 3.83e-05

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 41.98  E-value: 3.83e-05
                            10        20
                    ....*....|....*....|....*
gi 28872751     820 VESMFSLADKDGNGYLSFREFLDIL 844
Cdd:smart00054    2 LKEAFRLFDKDGDGKIDFEEFKDLL 26
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
1268-1402 6.02e-05

Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.


Pssm-ID: 99807  Cd Length: 238  Bit Score: 46.16  E-value: 6.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1268 LSRKKVEISVVKAELLPSGVTHLRFQ--RPQGFEYKSGQWVRIacLALGTTEYHPFTLTSAP-HEDTLSLHIR--AAGPW 1342
Cdd:cd06211    2 LNVKDFEGTVVEIEDLTPTIKGVRLKldEPEEIEFQAGQYVNL--QAPGYEGTRAFSIASSPsDAGEIELHIRlvPGGIA 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1343 TTRLREIYSapTGDRcarypkLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDL 1402
Cdd:cd06211   80 TTYVHKQLK--EGDE------LEISGPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMILDL 131
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
761-951 7.49e-05

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 46.19  E-value: 7.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  761 RHLLETFFRHLFSQVLDINQADAgtlpldssqkvrealtcelsraEFAEslglkpqdmFVESMFSLADKDGNGYLSFREF 840
Cdd:cd15902   18 GKELDSFLRELLKALNGKDKTDD----------------------EVAE---------KKKEFMEKYDENEDGKIEIREL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  841 LDILVV---FMK---GSPEEKSRLMF----RMYDFDGNGLISKDEFIRMLRSFIEISNNCLSKAQLAEVVESMFRE---- 906
Cdd:cd15902   67 ANILPTeenFLLlfrREQPLISSVEFmkiwRKYDTDGSGFIEAKELKGFLKDLLLKNKKHVSPPKLDEYTKLILKEfdan 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28872751  907 -----------------------SGFQDKEELTWEDFH--FML--RDHNSelrftqlCVKGVEVPEVIKDLC 951
Cdd:cd15902  147 kdgkleldemakllpvqenfllkFQILGAMDLTKEDFEkvFEHydKDNNG-------VIEGNELDALLKDLL 211
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
820-844 8.27e-05

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 40.85  E-value: 8.27e-05
                           10        20
                   ....*....|....*....|....*
gi 28872751    820 VESMFSLADKDGNGYLSFREFLDIL 844
Cdd:pfam00036    2 LKEIFRLFDKDGDGKIDFEEFKELL 26
EF-hand_6 pfam13405
EF-hand domain;
857-883 8.54e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 41.01  E-value: 8.54e-05
                           10        20
                   ....*....|....*....|....*..
gi 28872751    857 RLMFRMYDFDGNGLISKDEFIRMLRSF 883
Cdd:pfam13405    3 REAFKLFDKDGDGKISLEELRKALRSL 29
An_peroxidase_bacterial_1 cd09819
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ...
152-448 8.94e-05

Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.


Pssm-ID: 188651  Cd Length: 465  Bit Score: 46.95  E-value: 8.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  152 DPETGRSPSNPRDPANQVTGWLDGSAIYGsshswsdalrsfsRGQLASgPDPAFPRDSQNPLLMW------AAPDPATGQ 225
Cdd:cd09819   66 TSSLAPRQIDPAELRNFRTPALDLDSVYG-------------GGPDGS-PYLYDQATPNDGAKLRvgrespGGPGGLPGD 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  226 NG---PR--GLYAFGAERGNREPFLQA-LGLLWFRYHNLWAQRLARQHPDWEdeELFQHARKRVIATYQNIAVYEWLPSF 299
Cdd:cd09819  132 GArdlPRngQGTALIGDPRNDENLIVAqLHLAFLRFHNAVVDALRAHGTPGD--ELFEEARRLVRWHYQWLVLNDFLPRI 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  300 LQK--------TLPEYTGYRPFLDPSISSEFVAASEQFLSTMVPPGvYMRNASCH---FQGVINRNSSVSRAL----RVC 364
Cdd:cd09819  210 CDPdvvddvlaNGRRFYRFFREGKPFMPVEFSVAAYRFGHSMVRAS-YDYNRNFPdasLELLFTFTGGGEGDLggfsPLP 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  365 NSY---WSREHpslqsaeDVDAlllGMASQIAEREDHVLVEDVRDFWPGPLKFSRTD-HLA-SCLQRGRDLGLPSYTKAR 439
Cdd:cd09819  289 ENWiidWRRFF-------DIDG---SAPPQFARKIDTKLAPPLFDLPNGGVGLAPPMkSLAfRNLLRGYRLGLPSGQAVA 358

                 ....*....
gi 28872751  440 AALGLSPIT 448
Cdd:cd09819  359 RALGIAPLT 367
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
1290-1405 9.21e-05

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 46.02  E-value: 9.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  1290 LRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLtSAPHEDTLSLHIRAAGPWTTRLREIysaPTGDRcarypkLYLDGP 1369
Cdd:PRK00054   22 LVLDGEKVFDMKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVGEGTKKLSKL---KEGDE------LDIRGP 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 28872751  1370 FGEGhqewhkFEVSV------LVGGGIGVTPFASILKDLVFK 1405
Cdd:PRK00054   92 LGNG------FDLEEiggkvlLVGGGIGVAPLYELAKELKKK 127
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
1290-1409 1.64e-04

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 44.93  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1290 LRFQRPqgFEYKSGQ----WVRiaclalGTTEYhPFTLTSAPHEDTLSlhIRAAGPWTTRLreiYSAPTGDrcarypKLY 1365
Cdd:cd06220   16 FVFDWD--FDFKPGQfvmvWVP------GVDEI-PMSLSYIDGPNSIT--VKKVGEATSAL---HDLKEGD------KLG 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 28872751 1366 LDGPFGEGhqewhkFEVS----VLVGGGIGVTPFASILKDLVFKSSVS 1409
Cdd:cd06220   76 IRGPYGNG------FELVggkvLLIGGGIGIAPLAPLAERLKKAADVT 117
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
857-937 2.75e-04

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 42.65  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  857 RLMFRMYDFDGNGLISKDEFIRMLRSFieisNNCLSKAQLAEvvesMFRESGFQDKEELTWEDFHFMLRDHNS--ELR-- 932
Cdd:cd15898    3 RRQWIKADKDGDGKLSLKEIKKLLKRL----NIRVSEKELKK----LFKEVDTNGDGTLTFDEFEELYKSLTErpELEpi 74

                 ....*
gi 28872751  933 FTQLC 937
Cdd:cd15898   75 FKKYA 79
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
1284-1525 2.94e-04

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 44.18  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1284 PSGVThLRFQRPQG--FEYKSGQWVRIACLAL-GTTEYHPFTLTSAPHEDT-LSLHIR--AAGPWTTRLREIYSAptGDR 1357
Cdd:cd06217   14 PTVKT-FRLAVPDGvpPPFLAGQHVDLRLTAIdGYTAQRSYSIASSPTQRGrVELTVKrvPGGEVSPYLHDEVKV--GDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1358 carypkLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVscqvfcKKIYFIWVTRTqrqfewLADIIR 1437
Cdd:cd06217   91 ------LEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWP------VPFRLLYSART------AEDVIF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1438 EVEendhqdlvsvhiyITQLAekfdlrttmlyicERHFqkVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRKIGV 1517
Cdd:cd06217  153 RDE-------------LEQLA-------------RRHP--NLHVTEALTRAAPADWLGPAGRITADLIAELVPPLAGRRV 204

                 ....*...
gi 28872751 1518 FSCGPPGM 1525
Cdd:cd06217  205 YVCGPPAF 212
EF-hand_7 pfam13499
EF-hand domain pair;
800-844 9.78e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 9.78e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 28872751    800 CELSRAEFAESLGLKPQDMFVESMFSLADKDGNGYLSFREFLDIL 844
Cdd:pfam13499   22 EELKKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh_PI-PLCeta2 cd16221
EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also ...
824-876 1.85e-03

EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2, or phosphoinositide phospholipase C-like 4, or phospholipase C-like protein 4 (PLC-L4), or phospholipase C-eta-2 (PLC-eta2), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the pituitary gland, pineal gland, retina, and lung, as well as in neuroendocrine cells. PI-PLC-eta2 has been implicated in the regulation of neuronal differentiation/maturation. It is required for retinoic acid-stimulated neurite growth. It may also in part function downstream of G-protein-coupled receptors and play an important role in the formation and maintenance of the neuronal network in the postnatal brain. Moreover, PI-PLC-eta2 acts as a Ca2+ sensor that shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Its activation can be triggered either by intracellular calcium mobilization or by G beta-gamma signaling. PI-PLC-eta2 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320051 [Multi-domain]  Cd Length: 141  Bit Score: 40.30  E-value: 1.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 28872751  824 FSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGN-GLISKDEF 876
Cdd:cd16221    6 FDEADKNGDGSLSIGEVLQLLHKLNVNLPRQKVKQMFKEADTDDNqGTLGFEEF 59
PLN02964 PLN02964
phosphatidylserine decarboxylase
819-890 2.02e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 2.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28872751   819 FVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIE---ISNNC 890
Cdd:PLN02964  180 FARRILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALLALQQEqepIINNC 254
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
820-885 2.97e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 40.20  E-value: 2.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28872751  820 VESMFSLADKDGNGYLSFREFLDILV--VFMKGSPEeKSRLMFRMYDFDGNGLISKDEFIRmLRSFIE 885
Cdd:cd16180    2 LRRIFQAVDRDRSGRISAKELQRALSngDWTPFSIE-TVRLMINMFDRDRSGTINFDEFVG-LWKYIQ 67
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
828-915 3.03e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 41.18  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  828 DKDGNGYLSFREFLDILVVFMKG----------SPEEKSRLMFRmYDFDGNGLISKDEFIRMLRSFIEISNNCLSKAQLA 897
Cdd:cd15902    9 DADGNGYIEGKELDSFLRELLKAlngkdktddeVAEKKKEFMEK-YDENEDGKIEIRELANILPTEENFLLLFRREQPLI 87
                         90       100
                 ....*....|....*....|....*
gi 28872751  898 EVVESM--FRE-----SGFQDKEEL 915
Cdd:cd15902   88 SSVEFMkiWRKydtdgSGFIEAKEL 112
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
824-880 3.73e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 39.82  E-value: 3.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 28872751  824 FSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRML 880
Cdd:cd16180   73 FRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVEAC 129
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
820-884 4.12e-03

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 39.56  E-value: 4.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28872751  820 VESMFSLADKDGNGYLSFREFLDILVVFmKGS--PEEKSRLMFRMYDFDGNGLISKDEFiRMLRSFI 884
Cdd:cd16184    2 VQQWFQAVDRDRSGKISAKELQQALVNG-NWShfNDETCRLMIGMFDKDKSGTIDIYEF-QALWNYI 66
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
1277-1401 4.49e-03

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 40.33  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1277 VVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIAcLALGTTEyhPFTLTSAPHED-TLSLHIR-----AAGPWTTRLREIy 1350
Cdd:cd06194    1 VVSLQRLSPDVLRVRLEPDRPLPYLPGQYVNLR-RAGGLAR--SYSPTSLPDGDnELEFHIRrkpngAFSGWLGEEARP- 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 28872751 1351 saptGDRcarypkLYLDGPFGEG--HQEWHKFEVsVLVGGGIGVTPFASILKD 1401
Cdd:cd06194   77 ----GHA------LRLQGPFGQAfyRPEYGEGPL-LLVGAGTGLAPLWGIARA 118
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
819-881 6.22e-03

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 38.77  E-value: 6.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28872751  819 FVESMFSLADKDGNGYLSFREFLDiLVVFMKGSPEEKSrlMFRMYDFDGNGLISKDEFIRMLR 881
Cdd:cd16207   39 YLRELFDKADTDKKGYLNFEEFQE-FVKLLKRRKDIKA--IFKQLTKPGSDGLTLEEFLKFLR 98
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
820-876 7.86e-03

EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes represent a class of neuron-specific metazoan PI-PLCs that are most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. They are phosphatidylinositol 4,5-bisphosphate-hydrolyzing enzymes that are more sensitive to Ca2+ than other PI-PLC isozymes. They function as calcium sensors activated by small increases in intracellular calcium concentrations. They are also activated through G-protein-coupled receptor (GPCR) stimulation, and further mediate GPCR signalling pathways. PI-PLC-eta isozymes contain an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. There are two PI-PLC-eta isozymes (1-2). Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family.


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 38.52  E-value: 7.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 28872751  820 VESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGN-GLISKDEF 876
Cdd:cd16205    2 LKQTFEEADKNGDGLLSIGEILQLMHKLNVNLPRRKVRQMFKEADTDDNqGTLDFEEF 59
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
768-946 7.93e-03

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 38.74  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  768 FRHLFSQVLDI-NQADAGTLpldssQKVREALTCElsraefaeslGLKPQDMF----VESMFSLADKDGNGYLSFREFLD 842
Cdd:cd16182    2 VRELFEKLAGEdEEIDAVEL-----QKLLNASLLK----------DMPKFDGFsletCRSLIALMDTNGSGRLDLEEFKT 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751  843 ILvvfmkgSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRSF-IEISNNclskaqlaeVVES-MFResgFQDKEE-LTWED 919
Cdd:cd16182   67 LW------SDLKKWQAIFKKFDTDRSGTLSSYELRKALESAgFHLSNK---------VLQAlVLR---YADSTGrITFED 128
                        170       180
                 ....*....|....*....|....*...
gi 28872751  920 F-HFMLRDHNSELRFTQLCVKGVEVPEV 946
Cdd:cd16182  129 FvSCLVRLKTAFETFSALDKKNEGVIPL 156
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
857-881 7.96e-03

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 38.75  E-value: 7.96e-03
                         10        20
                 ....*....|....*....|....*
gi 28872751  857 RLMFRMYDFDGNGLISKDEFIRMLR 881
Cdd:cd15900    3 EIAFKMFDLDGDGELDKEEFNKVQS 27
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
1384-1544 9.14e-03

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 39.85  E-value: 9.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1384 VLVGGGIGVTPFASILKDLVFKSSVscqvfcKKIYFIWVTRTQRQ--F-EWLADIireVEENDHqdlVSVHIYITQLAEK 1460
Cdd:cd06184  117 VLISAGVGITPMLSMLEALAAEGPG------RPVTFIHAARNSAVhaFrDELEEL---AARLPN---LKLHVFYSEPEAG 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872751 1461 FDLRTTmlyicerHFQKVLNRSLFTGLrsithfgrppfepffNSLQEVHpqvrkigVFSCGPPGMTKNVEKacQLINR-- 1538
Cdd:cd06184  185 DREEDY-------DHAGRIDLALLREL---------------LLPADAD-------FYLCGPVPFMQAVRE--GLKALgv 233

                 ....*..
gi 28872751 1539 -QDRTHF 1544
Cdd:cd06184  234 pAERIHY 240
 
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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