|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
160-726 |
0e+00 |
|
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: 767.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 160 GASNTPFARWLPAQYEDAVSQPKGWDPNKLYNGAALPMVRLVSNRILATADADIESDHDFTFMLTIFGQWVDHDLTFTPF 239
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 240 SPSIRSFSNGIDCENSCERSEPCFPISAPPGDQRLRPNTCLPVFRSAPTCGSGHTAYMFGEV--PNVREQINTLTAYLDA 317
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLslANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 318 GQVYGSEDGLAKELRDLTNDGGLLRVNNRFKDNGRELLPFTSVNTNLCATrqkilNDSTLTEVPCFIAGDARVNENPALN 397
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQPEEVSSCNP-----DPNGGERVPCFLAGDGRASEVLTLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 398 SLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGAFNQILVIKEYLPLIVGPDAYNRHLGPYPGYNENVDPTIANV 477
Cdd:cd09825 236 ASHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 478 FATAAFRFAHLTIQPFIFRLDENYKNHPQFPSVPLYEAFFSPWRVIFEGGIDPVLRGLIGRPAKLNTQDHMLVNALRERL 557
Cdd:cd09825 316 FSTAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 558 FAFTSHIALDLASLNMQRGRDHAIPGYNAWRRFCGLSAPQNEQELAVVMNNTELARKLIELYGTPENIDVWLGGVAEPFA 637
Cdd:cd09825 396 FVLSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 638 PGGRVGSLFACLISRQFQKIRDGDRLWFESNGVFTTKQKTALASVSLARIICDNTGILKVPRDPFRFRS-PANFVNCGNI 716
Cdd:cd09825 476 PGARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKfPEDFVSCDSI 555
|
570
....*....|
gi 1199276932 717 PAFDLEPWKE 726
Cdd:cd09825 556 PGINLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
144-702 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 721.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 144 YRTASGVCNNRKNPLLGASNTPFARWLPAQYEDAVSQPKGWDpnklyNGAALPMVRLVSNRILATaDADIEsDHDFTFML 223
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFAG-DSGIP-DPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 224 TIFGQWVDHDLTFTPFSPSIRSFSngIDCENSCERSEP-CFPISAPPGDQRLRP--NTCLPVFRSAPTCGSGhtaymfge 300
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSS--CDCCCPPENLHPpCFPIPIPPDDPFFSPfgVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 301 vpNVREQINTLTAYLDAGQVYGSEDGLAKELRDLTndGGLLRVNNRfkDNGRELLPFTSVNTNLCATRQkilndstltEV 380
Cdd:pfam03098 144 --NPREQINQVTSFLDGSQVYGSSEETARSLRSFS--GGLLKVNRS--DDGKELLPFDPDGPCCCNSSG---------GV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 381 PCFIAGDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGAFNQILVIKEYLPLIVGPD---AYN 457
Cdd:pfam03098 209 PCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDnmnWFG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 458 RHLGPYPGYNENVDPTIANVFATAAFRFAHLTIQPFIFRLDENykNHPQFPSVPLYEAFFSPWRvIFEGGIDPVLRGLIG 537
Cdd:pfam03098 289 LLPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLDEN--NVPEEPSLRLHDSFFNPDR-LYEGGIDPLLRGLAT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 538 RPAKLNtqDHMLVNALRERLFAFTSH-IALDLASLNMQRGRDHAIPGYNAWRRFCGLSAPQNEQELAVVMNNTELArKLI 616
Cdd:pfam03098 366 QPAQAV--DNNFTEELTNHLFGPPGEfSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEVIA-KLR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 617 ELYGTPENIDVWLGGVAEPFAPGGRVGSLFACLISRQFQKIRDGDRLWFES--NGVFTTKQKTALASVSLARIICDNTGI 694
Cdd:pfam03098 443 ELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENgnQGSFTPEQLEEIRKTSLARVICDNTDI 522
|
....*....
gi 1199276932 695 L-KVPRDPF 702
Cdd:pfam03098 523 IeTIQPNVF 531
|
|
| C1q |
pfam00386 |
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ... |
772-890 |
2.84e-34 |
|
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.
Pssm-ID: 395310 [Multi-domain] Cd Length: 126 Bit Score: 127.40 E-value: 2.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 772 AFFASVNSILPATA-KVVVFGQVLYNGQNHYNQTSGMFLCQIPGVYEFEFSCI-GTRSLGFVTLKKNNRVELTPETVALN 849
Cdd:pfam00386 1 AFSAGRTTGLTAPNeQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1199276932 850 T-RSLAEGKAVLSLQRGDRVYVEVSRS----ANGIGFSSYFSGHIL 890
Cdd:pfam00386 81 GsLDVASGSVVLELQRGDEVWLQLTGYnglyYDGSDTDSTFSGFLL 126
|
|
| C1Q |
smart00110 |
Complement component C1q domain; Globular domain found in many collagens and eponymously in ... |
769-892 |
5.92e-26 |
|
Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.
Pssm-ID: 128420 Cd Length: 135 Bit Score: 103.92 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 769 QQSAFFASVNSILPATAKVVVFGQVLYNGQNHYNQTSGMFLCQIPGVYEFEFSCIGTRSLGFVTLKKNN-RVELTPETVA 847
Cdd:smart00110 6 PRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGiQVMSTYDEYQ 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1199276932 848 LNTRSLAEGKAVLSLQRGDRVYVEVSRSANGI----GFSSYFSGHILFP 892
Cdd:smart00110 86 KGLYDVASGGALLQLRQGDQVWLELPDEKNGLyageYVDSTFSGFLLFP 134
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
144-436 |
1.69e-06 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 51.69 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 144 YRTASGVCNNRKNPLLGASNTPFAR-WLPAQYEDAVSQPKgwdpnklyngaalPMVrlVSNRILATADAdIESDHDFT-- 220
Cdd:PLN02283 85 YRTADGKCNDPFNEGAGSQGTFFGRnMPPVDQKDKLLDPH-------------PSV--VATKLLARKKF-IDTGKQFNmi 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 221 ------FMLTifgQWVDHdltftpfspsirsfsngidCENSCErsepcFPISAPPGdqrlRPNTC-LPVFRSAPTcgsgh 293
Cdd:PLN02283 149 aaswiqFMIH---DWIDH-------------------LEDTQQ-----IELTAPKE----VASQCpLKSFKFYKT----- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 294 taymfGEVPNVREQI-----NTLTAYLDAGQVYGSedglakelrdltNDGGLLRVNNrFKDNgrellpftsvntnlcatR 368
Cdd:PLN02283 193 -----KEVPTGSPDIktgslNIRTPWWDGSVIYGS------------NEKGLRRVRT-FKDG-----------------K 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199276932 369 QKILNDSTLTE----VPcfIAGDARvNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGA 436
Cdd:PLN02283 238 LKISEDGLLLHdedgIP--ISGDVR-NSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSA 306
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
160-726 |
0e+00 |
|
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: 767.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 160 GASNTPFARWLPAQYEDAVSQPKGWDPNKLYNGAALPMVRLVSNRILATADADIESDHDFTFMLTIFGQWVDHDLTFTPF 239
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 240 SPSIRSFSNGIDCENSCERSEPCFPISAPPGDQRLRPNTCLPVFRSAPTCGSGHTAYMFGEV--PNVREQINTLTAYLDA 317
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLslANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 318 GQVYGSEDGLAKELRDLTNDGGLLRVNNRFKDNGRELLPFTSVNTNLCATrqkilNDSTLTEVPCFIAGDARVNENPALN 397
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQPEEVSSCNP-----DPNGGERVPCFLAGDGRASEVLTLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 398 SLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGAFNQILVIKEYLPLIVGPDAYNRHLGPYPGYNENVDPTIANV 477
Cdd:cd09825 236 ASHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 478 FATAAFRFAHLTIQPFIFRLDENYKNHPQFPSVPLYEAFFSPWRVIFEGGIDPVLRGLIGRPAKLNTQDHMLVNALRERL 557
Cdd:cd09825 316 FSTAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 558 FAFTSHIALDLASLNMQRGRDHAIPGYNAWRRFCGLSAPQNEQELAVVMNNTELARKLIELYGTPENIDVWLGGVAEPFA 637
Cdd:cd09825 396 FVLSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 638 PGGRVGSLFACLISRQFQKIRDGDRLWFESNGVFTTKQKTALASVSLARIICDNTGILKVPRDPFRFRS-PANFVNCGNI 716
Cdd:cd09825 476 PGARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKfPEDFVSCDSI 555
|
570
....*....|
gi 1199276932 717 PAFDLEPWKE 726
Cdd:cd09825 556 PGINLEAWRE 565
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
294-711 |
0e+00 |
|
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: 752.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 294 TAYMFGEVPNVREQINTLTAYLDAGQVYGSEDGLAKELRDLTNDGGLLRVNNRFKDNGRELLPFTSVNTNLCATRQkiln 373
Cdd:cd09824 1 SCGACTSKRNVREQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLAVNQRFTDNGLALLPFENLHNDPCALRN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 374 dsTLTEVPCFIAGDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGAFNQILVIKEYLPLIVGP 453
Cdd:cd09824 77 --TSANIPCFLAGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 454 DAYNRhLGPYPGYNENVDPTIANVFATAaFRFAHLTIQPFIFRLDENYKNHPQFPSVPLYEAFFSPWRVIFEGGIDPVLR 533
Cdd:cd09824 155 DAAAR-LPPYRGYNESVDPRIANVFTTA-FRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRIIREGGIDPILR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 534 GLIGRPAKLNTQDHMLVNALRERLFAFTSHIALDLASLNMQRGRDHAIPGYNAWRRFCGLSAPQNEQELAVVMNNTELAR 613
Cdd:cd09824 233 GLMATPAKLNNQNQMLVDELRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLAR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 614 KLIELYGTPENIDVWLGGVAEPFAPGGRVGSLFACLISRQFQKIRDGDRLWFESNGVFTTKQKTALASVSLARIICDNTG 693
Cdd:cd09824 313 KLLDLYGTPDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTG 392
|
410
....*....|....*....
gi 1199276932 694 ILKVPRDPF-RFRSPANFV 711
Cdd:cd09824 393 ITKVPRDPFqPNSYPRDFV 411
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
144-702 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 721.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 144 YRTASGVCNNRKNPLLGASNTPFARWLPAQYEDAVSQPKGWDpnklyNGAALPMVRLVSNRILATaDADIEsDHDFTFML 223
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFAG-DSGIP-DPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 224 TIFGQWVDHDLTFTPFSPSIRSFSngIDCENSCERSEP-CFPISAPPGDQRLRP--NTCLPVFRSAPTCGSGhtaymfge 300
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSS--CDCCCPPENLHPpCFPIPIPPDDPFFSPfgVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 301 vpNVREQINTLTAYLDAGQVYGSEDGLAKELRDLTndGGLLRVNNRfkDNGRELLPFTSVNTNLCATRQkilndstltEV 380
Cdd:pfam03098 144 --NPREQINQVTSFLDGSQVYGSSEETARSLRSFS--GGLLKVNRS--DDGKELLPFDPDGPCCCNSSG---------GV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 381 PCFIAGDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGAFNQILVIKEYLPLIVGPD---AYN 457
Cdd:pfam03098 209 PCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDnmnWFG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 458 RHLGPYPGYNENVDPTIANVFATAAFRFAHLTIQPFIFRLDENykNHPQFPSVPLYEAFFSPWRvIFEGGIDPVLRGLIG 537
Cdd:pfam03098 289 LLPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLDEN--NVPEEPSLRLHDSFFNPDR-LYEGGIDPLLRGLAT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 538 RPAKLNtqDHMLVNALRERLFAFTSH-IALDLASLNMQRGRDHAIPGYNAWRRFCGLSAPQNEQELAVVMNNTELArKLI 616
Cdd:pfam03098 366 QPAQAV--DNNFTEELTNHLFGPPGEfSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEVIA-KLR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 617 ELYGTPENIDVWLGGVAEPFAPGGRVGSLFACLISRQFQKIRDGDRLWFES--NGVFTTKQKTALASVSLARIICDNTGI 694
Cdd:pfam03098 443 ELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENgnQGSFTPEQLEEIRKTSLARVICDNTDI 522
|
....*....
gi 1199276932 695 L-KVPRDPF 702
Cdd:pfam03098 523 IeTIQPNVF 531
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
268-713 |
0e+00 |
|
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: 565.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 268 PPGDQRLRPNTCLPVFRSAPTCGSGHTAYMFGEVpNVREQINTLTAYLDAGQVYGSEDGLAKELRDLTNDGGLLRVNNRF 347
Cdd:cd09826 1 PPDDPRRRGHRCIEFVRSSAVCGSGSTSLLFNSV-TPREQINQLTSYIDASNVYGSSDEEALELRDLASDRGLLRVGIVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 348 KdNGRELLPFtsvNTNLCATRQKILNDSTlteVPCFIAGDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLY 427
Cdd:cd09826 80 E-AGKPLLPF---ERDSPMDCRRDPNESP---IPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 428 QEARKIVGAFNQILVIKEYLPLIVGPDAYNRhLGPYPGYNENVDPTIANVFATAAFRFAHLTIQPFIFRLDENYKNHPQF 507
Cdd:cd09826 153 HETRKIVGAQMQHITYSHWLPKILGPVGMEM-LGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPEG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 508 PsVPLYEAFFSPWRVIFEGGIDPVLRGLIGRPAKLNTQDHMLVNALRERLFAFTSHIALDLASLNMQRGRDHAIPGYNAW 587
Cdd:cd09826 232 H-LPLHKAFFAPYRLVNEGGIDPLLRGLFATAAKDRVPDQLLNTELTEKLFEMAHEVALDLAALNIQRGRDHGLPGYNDY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 588 RRFCGLSAPQNEQELAVVMNNTELARKLIELYGTPENIDVWLGGVAEPFAPGGRVGSLFACLISRQFQKIRDGDRLWFES 667
Cdd:cd09826 311 RKFCNLSVAETFEDLKNEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWYEN 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1199276932 668 NGVFTTKQKTALASVSLARIICDNT-GILKVPRDPFRFRS-PANFVNC 713
Cdd:cd09826 391 PGVFSPAQLTQIKKTSLARVLCDNGdNITRVQEDVFLVPGnPHGYVSC 438
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
305-691 |
8.03e-166 |
|
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: 487.47 E-value: 8.03e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 305 REQINTLTAYLDAGQVYGSEDGLAKELRDLtnDGGLLRVNNRfkdNGRELLPFTSVNTNLCATRQKilndstltEVPCFI 384
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTF--KGGLLKTQRR---NGRELLPFSNNPTDDCSLSSA--------GKPCFL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 385 AGDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGAFNQILVIKEYLPLIVGPDA------YNR 458
Cdd:cd09823 68 AGDGRVNEQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELmekfglYLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 459 HLGPYPGYNENVDPTIANVFATAAFRFAHLTIQPFIFRLDENYknhPQFPSVPLYEAFFSPWRVIFEGGIDPVLRGLIGR 538
Cdd:cd09823 148 TSGYFNGYDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENY---RPQGSVNLHDLFFNPDRLYEEGGLDPLLRGLATQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 539 PAKlNTQDHMLVNALRERLFAFTSHIALDLASLNMQRGRDHAIPGYNAWRRFCGLSAPQNEQELAVVMNNtELARKLIEL 618
Cdd:cd09823 225 PAQ-KVDRFFTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIMSP-ETIQKLRRL 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199276932 619 YGTPENIDVWLGGVAEPFAPGGRVGSLFACLISRQFQKIRDGDRLWFESNGV---FTTKQKTALASVSLARIICDN 691
Cdd:cd09823 303 YKSVDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
195-703 |
1.07e-120 |
|
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: 372.41 E-value: 1.07e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 195 LPMVRLVSNRIlATADADIESDHDFTFMLTIFGQWVDHDLTFTPFSPsirsfsngidcenscersepcfpisappgdqrl 274
Cdd:cd09822 2 RPSPREISNAV-ADQTESIPNSRGLSDWFWVWGQFLDHDIDLTPDNP--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 275 rpntclpvfrsaptcgsghtaymfgevpnvREQINTLTAYLDAGQVYGSEDGLAKELRdlTNDGGLLRVNnrfKDNGREL 354
Cdd:cd09822 48 ------------------------------REQINAITAYIDGSNVYGSDEERADALR--SFGGGKLKTS---VANAGDL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 355 LPFTSVNTNlcatrqkilNDSTL-TEVPCFIAGDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKI 433
Cdd:cd09822 93 LPFNEAGLP---------NDNGGvPADDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAI 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 434 VGAFNQILVIKEYLPLIVGPDAynrhLGPYPGYNENVDPTIANVFATAAFRFAHLTIQPFIFRLDENYKNhpqFPSVPLY 513
Cdd:cd09822 164 VIAEIQAITYNEFLPALLGENA----LPAYSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTE---ATSLALR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 514 EAFFSPWRVIfEGGIDPVLRGLIGRPAK-LNTQdhmLVNALRERLFAFTSHIALDLASLNMQRGRDHAIPGYNAWRRFCG 592
Cdd:cd09822 237 DAFFNPDELE-ENGIDPLLRGLASQVAQeIDTF---IVDDVRNFLFGPPGAGGFDLAALNIQRGRDHGLPSYNQLREALG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 593 LSAPQNEQELAvvmNNTELARKLIELYGTPENIDVWLGGVAEPFAPGGRVGSLFACLISRQFQKIRDGDRLWFEsNGVFT 672
Cdd:cd09822 313 LPAVTSFSDIT---SDPDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYE-NDDLL 388
|
490 500 510
....*....|....*....|....*....|.
gi 1199276932 673 TKQKTALASVSLARIICDNTGILKVPRDPFR 703
Cdd:cd09822 389 LDEIADIENTTLADVIRRNTDVDDIQDNVFL 419
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
307-691 |
1.05e-118 |
|
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: 365.60 E-value: 1.05e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 307 QINTLTAYLDAGQVYGSEDGLAKELRdlTNDGGLLRVNNRFKDN-GRELLPFTSVNTNLCatrqKILNDSTltevPCFIA 385
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALR--TFKGGLLKTNEVKGPSyGTELLPFNNPNPSMG----TIGLPPT----RCFIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 386 GDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGAFNQILVIKEYLPLIVGPDAYNRHLGPYPG 465
Cdd:cd05396 71 GDPRVNENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 466 YNENVDPTIANVFATAAFRFAHLTIQPFIFRLDENYkNHPQFPSVPLYEAFFSPWRVIF-EGGIDPVLRGLIGRPAKLNT 544
Cdd:cd05396 151 PDPDVVPYVLSEFFTAAYRFGHSLVPEGVDRIDENG-QPKEIPDVPLKDFFFNTSRSILsDTGLDPLLRGFLRQPAGLID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 545 QDHMLVNalreRLFAFTSHIALDLASLNMQRGRDHAIPGYNAWRRFCGLSAPQNEQELAvvmNNTELARKLIELYGTPEN 624
Cdd:cd05396 230 QNVDDVM----FLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDIL---TDPELAKKLAELYGDPDD 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199276932 625 IDVWLGGVAEPFAPGGRVGSLFACLISRQFQKIRDGDRLWFESNGVFTTKQKTALASV-SLARIICDN 691
Cdd:cd05396 303 VDLWVGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKLiSLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
152-706 |
7.99e-87 |
|
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: 288.04 E-value: 7.99e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 152 NNRKNPLLGASNTPFARWLPAQYEDAVSQPKGWDpnklyngaaLPMVRLVSNrILATADADIESDHDFTFMLTIFGQWVD 231
Cdd:cd09820 6 NNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEE---------RPNPRSLSN-LLMKGESGLPSTRNRTALLVFFGQHVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 232 HDLtftpfspsirsfsngIDCENS-CERSepCFPISAPPGDQRLRP----NTCLPVFRSAPTCGSGHTaymfgevPNV-R 305
Cdd:cd09820 76 SEI---------------LDASRPgCPPE--YFNIEIPKGDPVFDPectgNIELPFQRSRYDKNTGYS-------PNNpR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 306 EQINTLTAYLDAGQVYGSEDGLAKELRDLTNdgGLLRVN---NRFKDNGRELLPFTSVNtnlcATRQKILNDSTLtevpc 382
Cdd:cd09820 132 EQLNEVTSWIDGSSIYGSSKAWSDALRSFSG--GRLASGddgGFPRRNTNRLPLANPPP----PSYHGTRGPERL----- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 383 FIAGDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGAFNQILVIKEYLPLIVGpdaynRHLGP 462
Cdd:cd09820 201 FKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLG-----TNVPP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 463 YPGYNENVDPTIANVFATAAFRFAHLTIQPFIFRldENYKNHPQ--------FPSVPLYEAFFSPWRVIFEGGIDPVLRG 534
Cdd:cd09820 276 YTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVYR--RNRQCNFRevlttsggSPALRLCNTYWNSQEPLLKSDIDELLLG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 535 LIGRPAKLntQDHMLVNALRERLFA---FTShiaLDLASLNMQRGRDHAIPGYNAWRRFCGLSAPQNEQELAVVMN--NT 609
Cdd:cd09820 354 MASQIAER--EDNIIVEDLRDYLFGpleFSR---RDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDLFkkDP 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 610 ELARKLIELYG-TPENIDVWLGGVAEpfAPGGRVGSLFACLISRQFQKIRDGDRLWFES--NGVFTTKQKTALASVSLAR 686
Cdd:cd09820 429 ELLERLAELYGnDLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENvkNGLFTAEEIEEIRNTTLRD 506
|
570 580
....*....|....*....|..
gi 1199276932 687 IICDNTGILK--VPRDPFRFRS 706
Cdd:cd09820 507 VILAVTDIDNtdLQKNVFFWKN 528
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
222-703 |
1.29e-42 |
|
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: 164.12 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 222 MLTIFGQWVDHDLTFTPfspsiRSFSNGIDcenscersepcfpISAPPGD---QRLRPNTCLPVFRSAPTCGSGHTAymf 298
Cdd:cd09821 16 WMTFFGQFFDHGLDFIP-----KGGNGTVL-------------IPLPPDDplyDLGRGTNGMALDRGTNNAGPDGIL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 299 GEVPNVREQINTLTAYLDAGQVYGSEDGLAKELRDLTNDGGLlrvnnrfkdNGRELlpfTSVNTNLCATRQKILNDSTLT 378
Cdd:cd09821 75 GTADGEGEHTNVTTPFVDQNQTYGSHASHQVFLREYDGDGVA---------TGRLL---EGATGGSARTGHAFLDDIAHN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 379 EVPC-------------------------------FIAGDARVNENPALNSLHTLFVREHNRL----------ARALHVL 417
Cdd:cd09821 143 AAPKgglgslrdnptedppgpgapgsydnelldahFVAGDGRVNENIGLTAVHTVFHREHNRLvdqikdtllqSADLAFA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 418 NP------TWSSETLYQEARKIVGAFNQILVIKEYLPLIVGP-DAYNRHLgpypGYNENVDPTIANVFATAAFRFAHLTI 490
Cdd:cd09821 223 NEaggnnlAWDGERLFQAARFANEMQYQHLVFEEFARRIQPGiDGFGSFN----GYNPEINPSISAEFAHAVYRFGHSML 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 491 QPFIFRLDENYKNhPQFPSVPLYEAFFSPwrVIF-------EGGIDPVLRGLIGRPAklNTQDHMLVNALRERLFAftsh 563
Cdd:cd09821 299 TETVTRIGPDADE-GLDNQVGLIDAFLNP--VAFlpatlyaEEGAGAILRGMTRQVG--NEIDEFVTDALRNNLVG---- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 564 IALDLASLNMQRGRDHAIPGYNAWRRFC-------GLSAP-----------QNEQEL----------AVVMNNTELARK- 614
Cdd:cd09821 370 LPLDLAALNIARGRDTGLPTLNEARAQLfaatgdtILKAPyeswndfgarlKNPESLinfiaaygthLTITGATTLAAKr 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 615 ----LIELYGTP----------------------ENIDVWLGGVAEPFAP-GGRVGSLFACLISRQFQKIRDGDRLWFES 667
Cdd:cd09821 450 aaaqDLVDGGDGapadradfmnaagagagtvkglDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYYLS 529
|
570 580 590
....*....|....*....|....*....|....*...
gi 1199276932 668 --NGVFTTKQktaLASVSLARIICDNTGILKVPRDPFR 703
Cdd:cd09821 530 rtAGLDLLNQ---LENNTFADMIMRNTGATHLPQDIFS 564
|
|
| C1q |
pfam00386 |
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ... |
772-890 |
2.84e-34 |
|
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.
Pssm-ID: 395310 [Multi-domain] Cd Length: 126 Bit Score: 127.40 E-value: 2.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 772 AFFASVNSILPATA-KVVVFGQVLYNGQNHYNQTSGMFLCQIPGVYEFEFSCI-GTRSLGFVTLKKNNRVELTPETVALN 849
Cdd:pfam00386 1 AFSAGRTTGLTAPNeQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1199276932 850 T-RSLAEGKAVLSLQRGDRVYVEVSRS----ANGIGFSSYFSGHIL 890
Cdd:pfam00386 81 GsLDVASGSVVLELQRGDEVWLQLTGYnglyYDGSDTDSTFSGFLL 126
|
|
| C1Q |
smart00110 |
Complement component C1q domain; Globular domain found in many collagens and eponymously in ... |
769-892 |
5.92e-26 |
|
Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.
Pssm-ID: 128420 Cd Length: 135 Bit Score: 103.92 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 769 QQSAFFASVNSILPATAKVVVFGQVLYNGQNHYNQTSGMFLCQIPGVYEFEFSCIGTRSLGFVTLKKNN-RVELTPETVA 847
Cdd:smart00110 6 PRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGiQVMSTYDEYQ 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1199276932 848 LNTRSLAEGKAVLSLQRGDRVYVEVSRSANGI----GFSSYFSGHILFP 892
Cdd:smart00110 86 KGLYDVASGGALLQLRQGDQVWLELPDEKNGLyageYVDSTFSGFLLFP 134
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
145-639 |
1.51e-20 |
|
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: 95.81 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 145 RTASGVCNNRKNPLLGASNTPFARWLPaqyedaVSQPKGWDPNKLYNgaalPMVRLVSNRILAtADADIESDHdftfmLT 224
Cdd:cd09818 1 RTADGSYNDLDNPSMGSVGTRFGRNVP------LDATFPEDKDELLT----PNPRVISRRLLA-RTEFKPATS-----LN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 225 IFG----QWVDHDLtftpFSPsirsfsngidcenscersepcfpisappgdqrlrpntclpvfrsaptcgsGHTAYmfge 300
Cdd:cd09818 65 LLAaawiQFMVHDW----FSH--------------------------------------------------GPPTY---- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 301 vpnvreqINTLTAYLDAGQVYGSEDGLAKELRdLTNDGGLLRVNN-----RFKDNGrelLPFTSVNTNlcatrqkilnds 375
Cdd:cd09818 87 -------INTNTHWWDGSQIYGSTEEAQKRLR-TFPPDGKLKLDAdgllpVDEHTG---LPLTGFNDN------------ 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 376 tltevpcFIAGdarvnenpaLNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGAF------------------ 437
Cdd:cd09818 144 -------WWVG---------LSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALmakihtvewtpailahpt 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 438 -------NQILVIKEYLPLIVGPDAYNRHLGPYPGynenvdpTIANVFA---------TAAFRFAHLTIQPFIFRldeNY 501
Cdd:cd09818 208 leiamraNWWGLLGERLKRVLGRDGTSELLSGIPG-------SPPNHHGvpyslteefVAVYRMHPLIPDDIDFR---SA 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 502 KNHPQFPSVPLYEAFFSPWRVIFEG-GIDPVLRGL-IGRPAKLNTQDHMlvNALRERLFAFTSHIalDLASLNMQRGRDH 579
Cdd:cd09818 278 DDGATGEEISLTDLAGGKARELLRKlGFADLLYSFgITHPGALTLHNYP--RFLRDLHRPDGRVI--DLAAIDILRDRER 353
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199276932 580 AIPGYNAWRRFCGLSAPQNEQELAvvmNNTELARKLIELYG-TPENIDVWLGGVAEPFAPG 639
Cdd:cd09818 354 GVPRYNEFRRLLHLPPAKSFEDLT---GDEEVAAELREVYGgDVEKVDLLVGLLAEPLPPG 411
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
309-645 |
2.86e-19 |
|
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: 91.94 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 309 NTLTAYLDAGQVYGseDGLAKELRDLTNDGGLLRVnnrFKDNGRELLPFTSVNTNLcATRQKILNDSTLTEVPC------ 382
Cdd:cd09816 125 NTSNHGIDLSQIYG--LTEARTHALRLFKDGKLKS---QMINGEEYPPYLFEDGGV-KMEFPPLVPPLGDELTPereakl 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 383 FIAGDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIV-GAFNQIlVIKEYLplivgpdaynRHLG 461
Cdd:cd09816 199 FAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILiGELIKI-VIEDYI----------NHLS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 462 PYPgYNENVDPTIAnvFAT-------AAFRFAHLtiqpfifrldenYKNHPQFPS--------VPLYEAFFSPwRVIFEG 526
Cdd:cd09816 268 PYH-FKLFFDPELA--FNEpwqrqnrIALEFNLL------------YRWHPLVPDtfniggqrYPLSDFLFNN-DLVVDH 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 527 GIDPVL----RGLIGRPAKLNTQDHMLvnalrerlfaftshiALDLASlnMQRGRDHAIPGYNAWRRFCGLSAPQNEQEL 602
Cdd:cd09816 332 GLGALVdaasRQPAGRIGLRNTPPFLL---------------PVEVRS--IEQGRKLRLASFNDYRKRFGLPPYTSFEEL 394
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1199276932 603 AvvmNNTELARKLIELYGTPENIDVWLGGVAEPFAPGGRVGSL 645
Cdd:cd09816 395 T---GDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPL 434
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
219-534 |
5.61e-15 |
|
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: 78.54 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 219 FTFmltiFGQWVDHDLTFTPfspsirsfsngidcenscersepcfpiSAPPGDQRLRPNtclpvfrsaptcgsghtaymf 298
Cdd:cd09819 50 YTY----LGQFIDHDITLDT---------------------------TSSLAPRQIDPA--------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 299 gEVPNVReqintlTAYLDAGQVYGSEDGLAKELRDL--TNDGGLLRVnnrfkdnGRELLPFTSVNTNLCAtrqkilNDst 376
Cdd:cd09819 78 -ELRNFR------TPALDLDSVYGGGPDGSPYLYDQatPNDGAKLRV-------GRESPGGPGGLPGDGA------RD-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 377 lteVPCF-----IAGDARVNENPALNSLHTLFVREHNRLARALHVLNPTWSSetLYQEARKIVGAFNQILVIKEYLPLIV 451
Cdd:cd09819 136 ---LPRNgqgtaLIGDPRNDENLIVAQLHLAFLRFHNAVVDALRAHGTPGDE--LFEEARRLVRWHYQWLVLNDFLPRIC 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 452 GPDAYNRHL----GPYPGYNENVdPTIANVFATAAFRFAHLTIQPFifrldenYKNHPQFPSVPLyEAFFSpwrviFEGG 527
Cdd:cd09819 211 DPDVVDDVLangrRFYRFFREGK-PFMPVEFSVAAYRFGHSMVRAS-------YDYNRNFPDASL-ELLFT-----FTGG 276
|
....*..
gi 1199276932 528 IDPVLRG 534
Cdd:cd09819 277 GEGDLGG 283
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
144-436 |
1.69e-06 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 51.69 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 144 YRTASGVCNNRKNPLLGASNTPFAR-WLPAQYEDAVSQPKgwdpnklyngaalPMVrlVSNRILATADAdIESDHDFT-- 220
Cdd:PLN02283 85 YRTADGKCNDPFNEGAGSQGTFFGRnMPPVDQKDKLLDPH-------------PSV--VATKLLARKKF-IDTGKQFNmi 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 221 ------FMLTifgQWVDHdltftpfspsirsfsngidCENSCErsepcFPISAPPGdqrlRPNTC-LPVFRSAPTcgsgh 293
Cdd:PLN02283 149 aaswiqFMIH---DWIDH-------------------LEDTQQ-----IELTAPKE----VASQCpLKSFKFYKT----- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276932 294 taymfGEVPNVREQI-----NTLTAYLDAGQVYGSedglakelrdltNDGGLLRVNNrFKDNgrellpftsvntnlcatR 368
Cdd:PLN02283 193 -----KEVPTGSPDIktgslNIRTPWWDGSVIYGS------------NEKGLRRVRT-FKDG-----------------K 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199276932 369 QKILNDSTLTE----VPcfIAGDARvNENPALNSLHTLFVREHNRLARALHVLNPTWSSETLYQEARKIVGA 436
Cdd:PLN02283 238 LKISEDGLLLHdedgIP--ISGDVR-NSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSA 306
|
|
| |
