|
Name |
Accession |
Description |
Interval |
E-value |
| adm_rel |
TIGR01431 |
adenosine deaminase-related growth factor; Members of this family have been described as ... |
1-467 |
0e+00 |
|
adenosine deaminase-related growth factor; Members of this family have been described as secreted proteins with growth factor activity and regions of adenosine deaminase homology in insects, mollusks, and vertebrates.
Pssm-ID: 273620 [Multi-domain] Cd Length: 479 Bit Score: 837.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 1 MMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRT-LIFPPSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTM 79
Cdd:TIGR01431 14 SMRLGGKLVLTTKEKLANERIMTLKIAEMKEAMRTpLIFPPSMHFFQAKHLIERSQVFKILRMMPKGAALHLHDLGIVSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 80 DWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKrVQNVTEFDDSLLRNFTLVTQHPEVIYTNQN 159
Cdd:TIGR01431 94 DWLVRNVTYRPNLHICFTKRNIMVLRFRHPTPRPSECCSKWILLEDYRK-SQNVEEFDDSLLRNFTLVTTHPEVDYTTQN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 160 VVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHP 239
Cdd:TIGR01431 173 VVWSRFETIFFTLSGLLHYAPVFRDYYFRALEEFYEDNVQYMELRSRLFPLYELSGTHHDEEWSVKTYKEVTEKFVEEHP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 240 EFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAkDGVKLPYFFHAGETD 319
Cdd:TIGR01431 253 DFIGIKIIYSDLRSKDVEEIAEYIKMAMGLRIKYPDFVAGFDLVGQEDTGHSLLDYKDALLIPS-IGVKLPYFFHAGETN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 320 WQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSD 399
Cdd:TIGR01431 332 WQGTSVDRNLLDALLLNTTRIGHGFALSKHPAVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVATLMADNYPMVISSD 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 532691759 400 DPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVA 467
Cdd:TIGR01431 412 DPAFWGAKGLSYDFYEAFMGIAGMKADLRTLKQLALNSIKYSALSEEEKNTAMAKWKKQWDKFIDDVL 479
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
40-459 |
0e+00 |
|
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors with sequence similarty to adenosine deaminase.
Pssm-ID: 238646 Cd Length: 345 Bit Score: 563.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 40 PSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRphchicftprgimqfrfahptprpsekcsk 119
Cdd:cd01321 1 PGMHFFKAKDLIENSTLFKIIQKMPKGALLHVHDTAMVSSDWLIKNATYR------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 120 willedyrkrvqnvtefddsllrnftlvtqhpeviytnqnvvwskFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVL 199
Cdd:cd01321 51 ---------------------------------------------FEQIFDIIDGLLTYLPIFRDYYRRLLEELYEDNVQ 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 200 YMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAG 279
Cdd:cd01321 86 YVELRSSFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 280 FDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKK 359
Cdd:cd01321 166 FDLVGQEDAGRPLLDFLPQLLWFPKQCAEIPFFFHAGETNGDGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 360 DIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIK 439
Cdd:cd01321 246 NIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIR 325
|
410 420
....*....|....*....|
gi 532691759 440 YSTLLESEKNTFMEIWKKRW 459
Cdd:cd01321 326 YSALSDQEKDEAVAKWEKKW 345
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
186-464 |
7.13e-32 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 124.43 E-value: 7.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 186 VFRSMQEFY-----------EDNVLYMEIRarLLPVYelsgeHHDEEWSVKTYQE-VAQKFVETHPEF-IGIKIIYSDHR 252
Cdd:COG1816 59 VLQTEEDFRrlayeyledaaADGVRYAEIR--FDPQL-----HTRRGLSLEEVVEaVLDGLREAEREFgISVRLILCALR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 253 SKDVAVIAESIRMAMGLRIKFptvVAGFDLVGHEDtGHSLHDYKEALMIPAKDGVKLpyFFHAGETD-WQgtsidrNILD 331
Cdd:COG1816 132 HLSPEAAFETLELALRYRDRG---VVGFGLAGDER-GFPPEKFAEAFARAREAGLHL--TAHAGEAGgPE------SIWE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 332 AL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAkGLS 410
Cdd:COG1816 200 ALdLLGAERIGHGVRAIEDPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGT-TLT 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 532691759 411 YDfYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEKntfmEIWKKRWDKFIA 464
Cdd:COG1816 279 DE-YELAAEAFGL--SDADLAQLARNAIEASFLPEEEK----AALLAELDAYFA 325
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
182-448 |
5.29e-28 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 113.73 E-value: 5.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 182 FRDYVFRSMQEFYEDNVLYMEIR-------ARLLPVYELsgehhdeewsVKTYQEVAQKFVETHPefIGIKIIYSDHRSK 254
Cdd:PRK09358 79 LRRLAFEYLEDAAADGVVYAEIRfdpqlhtERGLPLEEV----------VEAVLDGLRAAEAEFG--ISVRLILCFMRHF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 255 DVAVIAESIrmAMGLRIKFPTVVAGFDLVGHEDtGHSLHDYKEALMIpAKD-GvkLPYFFHAGETDwqGTSidrNILDAL 333
Cdd:PRK09358 147 GEEAAAREL--EALAARYRDDGVVGFDLAGDEL-GFPPSKFARAFDR-ARDaG--LRLTAHAGEAG--GPE---SIWEAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 334 -MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGaKGLSyD 412
Cdd:PRK09358 216 dELGAERIGHGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFG-TTLT-E 293
|
250 260 270
....*....|....*....|....*....|....*.
gi 532691759 413 FYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEK 448
Cdd:PRK09358 294 EYEALAEAFGL--SDEDLAQLARNALEAAFLSEEEK 327
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
182-449 |
3.49e-19 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 88.26 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 182 FRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHH-----DEEWSVKTyqeVAQKFVETHPEF-IGIKIIYSDHRSKD 255
Cdd:pfam00962 70 IRRLAFEYAEDVAKDGVVYAEVR--------YDPQSHasrglSPDTVVDA---VLDAVDAAEREFgITVRLIVCAMRHEH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 256 VAVIAESIRMAMGLRikfPTVVAGFDLVGHEdTGHSLH---DYKEALMIPAKDGVKLPyfFHAGETDWQGTsidrnILDA 332
Cdd:pfam00962 139 PECSREIAELAPRYR---DQGIVAFGLAGDE-KGFPPSlfrDHVEAFARARDAGLHLT--VHAGEAGGPQS-----VWEA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 333 L-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAK-GLS 410
Cdd:pfam00962 208 LdDLGAERIGHGVRSAEDPRLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDlLDE 287
|
250 260 270
....*....|....*....|....*....|....*....
gi 532691759 411 YDFYEVFMGIggmkaDLRTLKQLAMNSIKYSTLLESEKN 449
Cdd:pfam00962 288 YQVAKRAPGF-----DEEELARLAKNAVKGSFLPADEKR 321
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| adm_rel |
TIGR01431 |
adenosine deaminase-related growth factor; Members of this family have been described as ... |
1-467 |
0e+00 |
|
adenosine deaminase-related growth factor; Members of this family have been described as secreted proteins with growth factor activity and regions of adenosine deaminase homology in insects, mollusks, and vertebrates.
Pssm-ID: 273620 [Multi-domain] Cd Length: 479 Bit Score: 837.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 1 MMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRT-LIFPPSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTM 79
Cdd:TIGR01431 14 SMRLGGKLVLTTKEKLANERIMTLKIAEMKEAMRTpLIFPPSMHFFQAKHLIERSQVFKILRMMPKGAALHLHDLGIVSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 80 DWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKrVQNVTEFDDSLLRNFTLVTQHPEVIYTNQN 159
Cdd:TIGR01431 94 DWLVRNVTYRPNLHICFTKRNIMVLRFRHPTPRPSECCSKWILLEDYRK-SQNVEEFDDSLLRNFTLVTTHPEVDYTTQN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 160 VVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHP 239
Cdd:TIGR01431 173 VVWSRFETIFFTLSGLLHYAPVFRDYYFRALEEFYEDNVQYMELRSRLFPLYELSGTHHDEEWSVKTYKEVTEKFVEEHP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 240 EFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAkDGVKLPYFFHAGETD 319
Cdd:TIGR01431 253 DFIGIKIIYSDLRSKDVEEIAEYIKMAMGLRIKYPDFVAGFDLVGQEDTGHSLLDYKDALLIPS-IGVKLPYFFHAGETN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 320 WQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSD 399
Cdd:TIGR01431 332 WQGTSVDRNLLDALLLNTTRIGHGFALSKHPAVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVATLMADNYPMVISSD 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 532691759 400 DPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVA 467
Cdd:TIGR01431 412 DPAFWGAKGLSYDFYEAFMGIAGMKADLRTLKQLALNSIKYSALSEEEKNTAMAKWKKQWDKFIDDVL 479
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
40-459 |
0e+00 |
|
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors with sequence similarty to adenosine deaminase.
Pssm-ID: 238646 Cd Length: 345 Bit Score: 563.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 40 PSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRphchicftprgimqfrfahptprpsekcsk 119
Cdd:cd01321 1 PGMHFFKAKDLIENSTLFKIIQKMPKGALLHVHDTAMVSSDWLIKNATYR------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 120 willedyrkrvqnvtefddsllrnftlvtqhpeviytnqnvvwskFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVL 199
Cdd:cd01321 51 ---------------------------------------------FEQIFDIIDGLLTYLPIFRDYYRRLLEELYEDNVQ 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 200 YMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAG 279
Cdd:cd01321 86 YVELRSSFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 280 FDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKK 359
Cdd:cd01321 166 FDLVGQEDAGRPLLDFLPQLLWFPKQCAEIPFFFHAGETNGDGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 360 DIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIK 439
Cdd:cd01321 246 NIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIR 325
|
410 420
....*....|....*....|
gi 532691759 440 YSTLLESEKNTFMEIWKKRW 459
Cdd:cd01321 326 YSALSDQEKDEAVAKWEKKW 345
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
151-455 |
8.68e-47 |
|
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase catalyzes a similar reaction leading to the hydrolytic removal of an amino group at the 6 position of the adenine nucleotide ring, a branch point in the adenylate catabolic pathway.
Pssm-ID: 238250 Cd Length: 305 Bit Score: 164.06 E-value: 8.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 151 PEVIYTNqnvVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRarllpvYELSGEHHDEEWSVKTYQ-- 228
Cdd:cd00443 16 PETLLEL---IKKEFFEKFLLVHNLLQKGEALARALKEVIEEFAEDNVQYLELR------TTPRLLETEKGLTKEQYWll 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 229 --EVAQKFVETHPeFIGIKIIYSDHRSKDV---AVIAESIrmaMGLRIKFPTVVAGFDLVGHEDTGHS-LHDYKEALMIp 302
Cdd:cd00443 87 viEGISEAKQWFP-PIKVRLILSVDRRGPYvqnYLVASEI---LELAKFLSNYVVGIDLVGDESKGENpLRDFYSYYEY- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 303 AKDGVKLPYFFHAGETDWQGTsidrnILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNH 382
Cdd:cd00443 162 ARRLGLLGLTLHCGETGNREE-----LLQALLLLPDRIGHGIFLLKHPELIYLVKLRNIPIEVCPTSNVVLGTVQSYEKH 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532691759 383 PVATLMATGHPMVISSDDPAMFGAkGLSYDFYEVFMgigGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIW 455
Cdd:cd00443 237 PFMRFFKAGLPVSLSTDDPGIFGT-SLSEEYSLAAK---TFGLTFEDLCELNRNSVLSSFAKDEEKKSLLEVL 305
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
186-464 |
7.13e-32 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 124.43 E-value: 7.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 186 VFRSMQEFY-----------EDNVLYMEIRarLLPVYelsgeHHDEEWSVKTYQE-VAQKFVETHPEF-IGIKIIYSDHR 252
Cdd:COG1816 59 VLQTEEDFRrlayeyledaaADGVRYAEIR--FDPQL-----HTRRGLSLEEVVEaVLDGLREAEREFgISVRLILCALR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 253 SKDVAVIAESIRMAMGLRIKFptvVAGFDLVGHEDtGHSLHDYKEALMIPAKDGVKLpyFFHAGETD-WQgtsidrNILD 331
Cdd:COG1816 132 HLSPEAAFETLELALRYRDRG---VVGFGLAGDER-GFPPEKFAEAFARAREAGLHL--TAHAGEAGgPE------SIWE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 332 AL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAkGLS 410
Cdd:COG1816 200 ALdLLGAERIGHGVRAIEDPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGT-TLT 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 532691759 411 YDfYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEKntfmEIWKKRWDKFIA 464
Cdd:COG1816 279 DE-YELAAEAFGL--SDADLAQLARNAIEASFLPEEEK----AALLAELDAYFA 325
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
166-449 |
6.21e-29 |
|
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases.
Pssm-ID: 238645 Cd Length: 325 Bit Score: 116.15 E-value: 6.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 166 ETIFFTISGLIHYApVFRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHH-----DEEWSVKTYQEVAQKFVETHPe 240
Cdd:cd01320 56 AKYDFGLSVLQTEE-DFERLAYEYLEDAAADGVVYAEIR--------FSPQLHtrrglSFDEVVEAVLRGLDEAEAEFG- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 241 fIGIKIIYSDHRSKDVAVIAESIRMAmgLRIKFPTVVaGFDLVGHEdTGHSLHDYKEALMIPAKDGVKLPyfFHAGETDw 320
Cdd:cd01320 126 -IKARLILCGLRHLSPESAQETLELA--LKYRDKGVV-GFDLAGDE-VGFPPEKFVRAFQRAREAGLRLT--AHAGEAG- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 321 qGTSidrNILDAL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSD 399
Cdd:cd01320 198 -GPE---SVRDALdLLGAERIGHGIRAIEDPELVKRLAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTD 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 532691759 400 DPAMFGAKgLSYDFYEVFMGIGgmkADLRTLKQLAMNSIKYSTLLESEKN 449
Cdd:cd01320 274 DPTVFGTY-LTDEYELLAEAFG---LTEEELKKLARNAVEASFLSEEEKA 319
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
182-448 |
5.29e-28 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 113.73 E-value: 5.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 182 FRDYVFRSMQEFYEDNVLYMEIR-------ARLLPVYELsgehhdeewsVKTYQEVAQKFVETHPefIGIKIIYSDHRSK 254
Cdd:PRK09358 79 LRRLAFEYLEDAAADGVVYAEIRfdpqlhtERGLPLEEV----------VEAVLDGLRAAEAEFG--ISVRLILCFMRHF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 255 DVAVIAESIrmAMGLRIKFPTVVAGFDLVGHEDtGHSLHDYKEALMIpAKD-GvkLPYFFHAGETDwqGTSidrNILDAL 333
Cdd:PRK09358 147 GEEAAAREL--EALAARYRDDGVVGFDLAGDEL-GFPPSKFARAFDR-ARDaG--LRLTAHAGEAG--GPE---SIWEAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 334 -MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGaKGLSyD 412
Cdd:PRK09358 216 dELGAERIGHGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFG-TTLT-E 293
|
250 260 270
....*....|....*....|....*....|....*.
gi 532691759 413 FYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEK 448
Cdd:PRK09358 294 EYEALAEAFGL--SDEDLAQLARNALEAAFLSEEEK 327
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
162-453 |
1.92e-25 |
|
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of mammals and E. coli. Other members of this family are predicted also to be adenosine deaminase, an enzyme of nucleotide degradation. This family is distantly related to AMP deaminase.
Pssm-ID: 273619 Cd Length: 324 Bit Score: 106.29 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 162 WSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHH-DEEWSVKTYQE-----VAQKFV 235
Cdd:TIGR01430 50 LQDFLAKYDFGVEVLRTEDDFKRLAYEYVEKAAKDGVVYAEVF--------FDPQLHtNRGISPDTVVEavldgLDEAER 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 236 ETHpefIGIKIIYSDHRSKDVAVIAESIRMAmgLRIKFPTVVaGFDLVGHEdTGHSLHDYKEALMIPAKDGVKLPyfFHA 315
Cdd:TIGR01430 122 DFG---IKSRLILCGMRHKQPEAAEETLELA--KPYKEQTIV-GFGLAGDE-RGGPPPDFVRAFAIARELGLHLT--VHA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 316 GETDwqGTSIDRNILDalMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMV 395
Cdd:TIGR01430 193 GELG--GPESVREALD--DLGATRIGHGVRALEDPELLKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVT 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 532691759 396 ISSDDPAMFGakglSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFME 453
Cdd:TIGR01430 269 LNSDDPAYFG----SYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKKELLA 322
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
182-449 |
3.49e-19 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 88.26 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 182 FRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHH-----DEEWSVKTyqeVAQKFVETHPEF-IGIKIIYSDHRSKD 255
Cdd:pfam00962 70 IRRLAFEYAEDVAKDGVVYAEVR--------YDPQSHasrglSPDTVVDA---VLDAVDAAEREFgITVRLIVCAMRHEH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 256 VAVIAESIRMAMGLRikfPTVVAGFDLVGHEdTGHSLH---DYKEALMIPAKDGVKLPyfFHAGETDWQGTsidrnILDA 332
Cdd:pfam00962 139 PECSREIAELAPRYR---DQGIVAFGLAGDE-KGFPPSlfrDHVEAFARARDAGLHLT--VHAGEAGGPQS-----VWEA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 333 L-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAK-GLS 410
Cdd:pfam00962 208 LdDLGAERIGHGVRSAEDPRLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDlLDE 287
|
250 260 270
....*....|....*....|....*....|....*....
gi 532691759 411 YDFYEVFMGIggmkaDLRTLKQLAMNSIKYSTLLESEKN 449
Cdd:pfam00962 288 YQVAKRAPGF-----DEEELARLAKNAVKGSFLPADEKR 321
|
|
| A_deaminase_N |
pfam08451 |
Adenosine/AMP deaminase N-terminal; This domain is found to the N-terminus of the Adenosine ... |
1-60 |
1.53e-17 |
|
Adenosine/AMP deaminase N-terminal; This domain is found to the N-terminus of the Adenosine/AMP deaminase domain (pfam00962) in metazoan proteins such as the Cat eye syndrome critical region protein 1 and its homologs.
Pssm-ID: 462481 Cd Length: 95 Bit Score: 77.73 E-value: 1.53e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532691759 1 MMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRTLI-FPPSMHFFQAKHLIERSQVFNIL 60
Cdd:pfam08451 35 RLRLGGNLELSPLEEKANDILMAIKQVELAEGFRNWEnYPPAPHFFLAKDLINESDLFKFL 95
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
194-435 |
1.08e-14 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 75.29 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 194 YEDNVLYMEIRARllPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKF 273
Cdd:PTZ00124 116 YKEGVVLMEFRYS--PTFVAFKHNLDIDLIHQAIVKGIKEAVELLDHKIEVGLLCIGDTGHDAAPIKESADFCLKHKADF 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 274 ptvvAGFDLVGHEdtgHSLHDYKEALMIPAKDGVKLPyfFHAGEtDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVR 353
Cdd:PTZ00124 194 ----VGFDHAGHE---VDLKPFKDIFDYVREAGVNLT--VHAGE-DVTLPNLNTLYSAIQVLKVKRIGHGIRVAESQELI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 354 TYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFgAKGLSYDFYEVFMGIGGMKADLRTLKQL 433
Cdd:PTZ00124 264 DMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMF-LTNINDDYEELYTHLNFTLADFMKMNEW 342
|
..
gi 532691759 434 AM 435
Cdd:PTZ00124 343 AL 344
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
273-440 |
4.94e-10 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 60.04 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 273 FPTVVAGFDLVGHE-DTGHSLHDYKEALMIPAKDGvkLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHpA 351
Cdd:cd01292 112 LELGAVGLKLAGPYtATGLSDESLRRVLEEARKLG--LPVVIHAGELPDPTRALEDLVALLRLGGRVVIGHVSHLDPE-L 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 352 VRTYSwKKDIPIEVCPISNQVLKLvSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMgIGGMKADLRTLK 431
Cdd:cd01292 189 LELLK-EAGVSLEVCPLSNYLLGR-DGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLK-VLRLGLSLEEAL 265
|
170
....*....|
gi 532691759 432 QLA-MNSIKY 440
Cdd:cd01292 266 RLAtINPARA 275
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
339-404 |
1.53e-03 |
|
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at position 6 of the adenine nucleotide ring. AMPD is a diverse and highly regulated eukaryotic key enzyme of the adenylate catabolic pathway.
Pssm-ID: 238644 Cd Length: 496 Bit Score: 40.81 E-value: 1.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532691759 339 RIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLvsDLRNHPVATLMATGHPMVISSDDPAMF 404
Cdd:cd01319 351 GISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFL--SYEKNPFPEFFKRGLNVSLSTDDPLQF 414
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
314-403 |
3.06e-03 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 39.85 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 314 HAGETDwqgtsiDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLvsDLRNHPVATLMATGHP 393
Cdd:PLN03055 422 HAGEAG------DIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLAMSPLSNNSLFL--DYHRNPFPMFFARGLN 493
|
90
....*....|
gi 532691759 394 MVISSDDPAM 403
Cdd:PLN03055 494 VSLSTDDPLQ 503
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
310-404 |
9.85e-03 |
|
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein involved in energy metabolism. Most members of the family have an additional, poorly alignable region of 150 amino acids or more N-terminal to the region included in the model.
Pssm-ID: 273618 [Multi-domain] Cd Length: 611 Bit Score: 38.29 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691759 310 PYFFHAGETDWQGTSidrnildalMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDlRNhPVATLMA 389
Cdd:TIGR01429 443 PHCGEAGSVDHLVSA---------FLTSHGINHGILLRKVPVLQYLYYLTQIPIAMSPLSNNSLFLEYS-KN-PLPEYLH 511
|
90
....*....|....*
gi 532691759 390 TGHPMVISSDDPAMF 404
Cdd:TIGR01429 512 KGLNVSLSTDDPLQF 526
|
|
| |
