|
Name |
Accession |
Description |
Interval |
E-value |
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
17-216 |
1.55e-77 |
|
Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238563 [Multi-domain] Cd Length: 195 Bit Score: 233.32 E-value: 1.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 17 SPYHRIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKKGKKQFDALNLNKEELLKAKPDLILAHESQKATankVLSS 96
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAE---LLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 97 LEKQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAhHKKSKVFIEVSSkPEIYTAGKH 176
Cdd:cd01143 78 LKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKT-IKKSKVYIEVSL-GGPYTAGKN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1390929086 177 TFFNDMLEKLEAQNVYSDINGWNPVTKESIIKKNPDILIS 216
Cdd:cd01143 156 TFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
21-273 |
1.55e-67 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 210.62 E-value: 1.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKYIVGVS--TVDDYPKDVKKGKKQF-DALNLNKEELLKAKPDLILAHESQkaTANKVLSSL 97
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSdwGYCDYPELELKDLPVVgGTGEPNLEAILALKPDLVLASSSG--NDEEDYEQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 98 EKQGIKVVYVkDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKVFIEVSSKPEIYTAGKHT 177
Cdd:COG0614 80 EKIGIPVVVL-DPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 178 FFNDMLEKLEAQNVYSDIN-GWNPVTKESIIKKNPDILI----STEAKTRSDYMDIIKKRGGFNKINAVKNTRIEVVNGD 252
Cdd:COG0614 159 FIGELLELAGGRNVAADLGgGYPEVSLEQVLALDPDVIIlsggGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD 238
|
250 260
....*....|....*....|.
gi 1390929086 253 EVSRPGPRIDEGLKELRDAIY 273
Cdd:COG0614 239 LLSRPGPRLLLALEDLAKALH 259
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
23-246 |
1.70e-28 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 108.61 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 23 VSLMPSNTEILYELGLGKYIVGVS--TVDDYPKDVKKGKKQFDA-LNLNKEELLKAKPDLILAHESQKATANkvlSSLEK 99
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDayTRDPLKADAVAAIVKVGAyGEINVERLAALKPDLVILSTGYLTDEA---EELLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 100 QGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKVFIEVSSKPEIYTAGKHTFF 179
Cdd:pfam01497 78 LIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 180 NDMLEKLEAQNVYSDIN--GWNPVTKESIIKKNPDILI-STEAKTRSDYMDIIKKRGGFNKINAVKNTRI 246
Cdd:pfam01497 158 GDLLRILGIENIAAELSgsEYAPISFEAILSSNPDVIIvSGRDSFTKTGPEFVAANPLWAGLPAVKNGRV 227
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
21-261 |
3.60e-28 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 108.62 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKyiVGVSTVDDYPKDVKKGKKQFDALNLNKEELLKAKPDLILAHesQKATANKVLSSLEKQ 100
Cdd:PRK03379 19 RVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAW--RGGNAERQVDQLASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 101 GIKVVYVkDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKvIDSIPAHHKKSKVFIEVSSKPeIYTAGKHTFFN 180
Cdd:PRK03379 95 GIKVMWV-DATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAA-LKAQYADKPKKRVFLQFGTNP-LFTSGKHSIQS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 181 DMLEKLEAQNVYSDIN-GWNPVTKESIIKKNPDILISTeaktrsdymdiikkrGGFNKINAVKN-----TRIEV--VNGD 252
Cdd:PRK03379 172 QVLSLCGGENIFADSRvPWPQVSREQVLARKPQAIVIT---------------GGPDQIPKIKQfwgpqLKIPVipLNSD 236
|
....*....
gi 1390929086 253 EVSRPGPRI 261
Cdd:PRK03379 237 WFERASPRI 245
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
17-216 |
1.55e-77 |
|
Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238563 [Multi-domain] Cd Length: 195 Bit Score: 233.32 E-value: 1.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 17 SPYHRIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKKGKKQFDALNLNKEELLKAKPDLILAHESQKATankVLSS 96
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAE---LLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 97 LEKQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAhHKKSKVFIEVSSkPEIYTAGKH 176
Cdd:cd01143 78 LKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKT-IKKSKVYIEVSL-GGPYTAGKN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1390929086 177 TFFNDMLEKLEAQNVYSDINGWNPVTKESIIKKNPDILIS 216
Cdd:cd01143 156 TFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
21-273 |
1.55e-67 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 210.62 E-value: 1.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKYIVGVS--TVDDYPKDVKKGKKQF-DALNLNKEELLKAKPDLILAHESQkaTANKVLSSL 97
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSdwGYCDYPELELKDLPVVgGTGEPNLEAILALKPDLVLASSSG--NDEEDYEQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 98 EKQGIKVVYVkDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKVFIEVSSKPEIYTAGKHT 177
Cdd:COG0614 80 EKIGIPVVVL-DPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 178 FFNDMLEKLEAQNVYSDIN-GWNPVTKESIIKKNPDILI----STEAKTRSDYMDIIKKRGGFNKINAVKNTRIEVVNGD 252
Cdd:COG0614 159 FIGELLELAGGRNVAADLGgGYPEVSLEQVLALDPDVIIlsggGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD 238
|
250 260
....*....|....*....|.
gi 1390929086 253 EVSRPGPRIDEGLKELRDAIY 273
Cdd:COG0614 239 LLSRPGPRLLLALEDLAKALH 259
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
21-273 |
2.28e-58 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 187.71 E-value: 2.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKKGKKQFDALNLNKEELLKAKPDLILAHESqkATANKVLSSLEKQ 100
Cdd:COG4558 29 RIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGILSLKPTLVLASEG--AGPPEVLDQLRAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 101 GIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKV-FIEVSSKPEIYTAGKHTFF 179
Cdd:COG4558 107 GVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKPPRVlFLLSRGGGRPMVAGRGTAA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 180 NDMLEKLEAQNVYSDINGWNPVTKESIIKKNPD-ILISTEAKTRSDYMDIIKKRGGFNKINAVKNTRIEVVNGDEVSRPG 258
Cdd:COG4558 187 DALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDvILVMTRGLESLGGVDGLLALPGLAQTPAGKNKRIVAMDDLLLLGFG 266
|
250
....*....|....*
gi 1390929086 259 PRIDEGLKELRDAIY 273
Cdd:COG4558 267 PRTPQAALALAQALY 281
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
21-268 |
1.57e-49 |
|
Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238564 [Multi-domain] Cd Length: 245 Bit Score: 163.62 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKKGKKQFDALNLNKEELLKAKPDLILAHESQKATAnkVLSSLEKQ 100
Cdd:cd01144 2 RIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCA--VVDQLRAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 101 GIKvVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKvIDSIPAHHKKSKVFIEVSSKPeIYTAGkHTFFN 180
Cdd:cd01144 80 GIP-VLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAA-LRKQYASKPPPRVFYQEWIDP-LMTAG-GDWVP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 181 DMLEKLEAQNVYSDI-NGWNPVTKESIIKKNPD-ILISTEAKTRsdYMDIIKKRGGFNKINAVKNTRIEVVNGDEVSRPG 258
Cdd:cd01144 156 ELIALAGGVNVFADAgERSPQVSWEDVLAANPDvIVLSPCGFGF--TPAILRKEPAWQALPAVRNGRVYAVDGNWYFRPS 233
|
250
....*....|
gi 1390929086 259 PRIDEGLKEL 268
Cdd:cd01144 234 PRLVDGLEQL 243
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
21-251 |
2.52e-34 |
|
Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238569 [Multi-domain] Cd Length: 235 Bit Score: 123.91 E-value: 2.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKKGKKQFDALNLNKEELLKAKPDLILA-HESQKATAnkvLSSLEK 99
Cdd:cd01149 3 RIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIAsDEAGPPEA---LDQLRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 100 QGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKV-FIEVSSKPEIYTAGKHTF 178
Cdd:cd01149 80 AGVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVlFLLSHGGGAAMAAGRNTA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390929086 179 FNDMLEKLEAQNVYSDINGWNPVTKESIIKKNPD-ILISTEAKTRSDYMDIIKKRGGFNKINAVKNTRIEVVNG 251
Cdd:cd01149 160 ADAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDvILVMSRGLDAVGGVDGLLKLPGLAQTPAGRNKRILAMDD 233
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
21-269 |
1.25e-32 |
|
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238568 [Multi-domain] Cd Length: 284 Bit Score: 120.91 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKYIVGVSTVddYPKDVKKGKKQFDALNLN------KEELLKAKPDLILAHESQKATANKVL 94
Cdd:cd01148 20 RVVSNDQNTTEMMLALGLQDRMVGTAGI--DNKDLPELKAKYDKVPELakkypsKETVLAARPDLVFGGWSYGFDKGGLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 95 S--SLEKQGIKV-------VYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKVFIEVS 165
Cdd:cd01148 98 TpdSLAELGIKTyilpescGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKVAVFVYDS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 166 SKPEIYTAGKHTFFNDMLEKLEAQNVYSDIN-GWNPVTKESIIKKNPDILISTEAKTRSDYMDIIKKRGGF---NKINAV 241
Cdd:cd01148 178 GEDKPFTSGRGGIPNAIITAAGGRNVFADVDeSWTTVSWETVIARNPDVIVIIDYGDQNAAEQKIKFLKENpalKNVPAV 257
|
250 260
....*....|....*....|....*...
gi 1390929086 242 KNTRIeVVNGDEVSRPGPRIDEGLKELR 269
Cdd:cd01148 258 KNNRF-IVLPLAEATPGIRNVDAIEKLA 284
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
23-246 |
1.70e-28 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 108.61 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 23 VSLMPSNTEILYELGLGKYIVGVS--TVDDYPKDVKKGKKQFDA-LNLNKEELLKAKPDLILAHESQKATANkvlSSLEK 99
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDayTRDPLKADAVAAIVKVGAyGEINVERLAALKPDLVILSTGYLTDEA---EELLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 100 QGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKVFIEVSSKPEIYTAGKHTFF 179
Cdd:pfam01497 78 LIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 180 NDMLEKLEAQNVYSDIN--GWNPVTKESIIKKNPDILI-STEAKTRSDYMDIIKKRGGFNKINAVKNTRI 246
Cdd:pfam01497 158 GDLLRILGIENIAAELSgsEYAPISFEAILSSNPDVIIvSGRDSFTKTGPEFVAANPLWAGLPAVKNGRV 227
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
21-261 |
3.60e-28 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 108.62 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKyiVGVSTVDDYPKDVKKGKKQFDALNLNKEELLKAKPDLILAHesQKATANKVLSSLEKQ 100
Cdd:PRK03379 19 RVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAW--RGGNAERQVDQLASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 101 GIKVVYVkDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKvIDSIPAHHKKSKVFIEVSSKPeIYTAGKHTFFN 180
Cdd:PRK03379 95 GIKVMWV-DATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAA-LKAQYADKPKKRVFLQFGTNP-LFTSGKHSIQS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 181 DMLEKLEAQNVYSDIN-GWNPVTKESIIKKNPDILISTeaktrsdymdiikkrGGFNKINAVKN-----TRIEV--VNGD 252
Cdd:PRK03379 172 QVLSLCGGENIFADSRvPWPQVSREQVLARKPQAIVIT---------------GGPDQIPKIKQfwgpqLKIPVipLNSD 236
|
....*....
gi 1390929086 253 EVSRPGPRI 261
Cdd:PRK03379 237 WFERASPRI 245
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
21-259 |
2.02e-27 |
|
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.
Pssm-ID: 238566 [Multi-domain] Cd Length: 256 Bit Score: 106.22 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILyeLGLGKYIVGVSTVDDYPKDVKKGKKQFD---------ALNLnkEELLKAKPDLILAHESQKATAN 91
Cdd:cd01146 5 RIVALDWGALETL--LALGVKPVGVADTAGYKPWIPEPALPLEgvvdvgtrgQPNL--EAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 92 KVLSSlekqgI-KVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKVFIEVSSKPEI 170
Cdd:cd01146 81 DQLSQ-----IaPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 171 YTAGKHTFFNDMLEKL-----EAQNVYSDiNGWNPVTKESIIKKNPDILISTEAKTRSDYmDIIKKRGGFNKINAVKNTR 245
Cdd:cd01146 156 RLYGPNSFAGSVLEDLglqnpWAQETTND-SGFATISLERLAKADADVLFVFTYEDEELA-QALQANPLWQNLPAVKNGR 233
|
250
....*....|....
gi 1390929086 246 IEVVNGDEVSRPGP 259
Cdd:cd01146 234 VYVVDDVWWFFGGG 247
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
21-162 |
1.09e-23 |
|
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.
Pssm-ID: 238347 [Multi-domain] Cd Length: 148 Bit Score: 93.78 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKKGKKQ----FDALNLNKEELLKAKPDLILAHESQkatANKVLSS 96
Cdd:cd00636 2 RVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKvpdvGHGYEPNLEKIAALKPDLIIANGSG---LEAWLDK 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390929086 97 LEKQGIKVVYVKDAQ--SIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKVFI 162
Cdd:cd00636 79 LSKIAIPVVVVDEASelSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
21-272 |
2.20e-22 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 94.98 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDV--KKGKKQFDALNLNKEELLKAKPDLILAhesQKATANKVLSSLE 98
Cdd:PRK09534 62 RVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAeeRTNVSGGQPFGVNVEAVVGLDPDLVLA---PNAVAGDTVTRLR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 99 KQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKVFIEVSSKpeiYTAGKHTF 178
Cdd:PRK09534 139 EAGITVFHFPAATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLYPLGDG---YTAGGNTF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 179 FNDMLEKLEAQNVYSD--INGWNPVTKESIIKKNPDILISTEAKTrsdymdIIKKRGGFNKINAVKNTRIEVVNGDEVSR 256
Cdd:PRK09534 216 IGALIEAAGGHNVAADatTDGYPQLSEEVIVQQDPDVIVVATASA------LVAETEPYASTTAGETGNVVTVNVNHINQ 289
|
250
....*....|....*.
gi 1390929086 257 PGPRIDEGLKELRDAI 272
Cdd:PRK09534 290 PAPRIVESMATMATAF 305
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
21-249 |
2.26e-22 |
|
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238562 [Multi-domain] Cd Length: 289 Bit Score: 93.57 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKYIVGVSTV----DDYPK---DVKKGKKQFDALNLNKEELLKAKPDLILahesqkatankV 93
Cdd:cd01142 26 RIAALWGAGNAVVAALGGGKLIVATTSTvqqePWLYRlapSLENVATGGTGNDVNIEELLALKPDVVI-----------V 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 94 LSSLEKQ-GIKVVYVKDAQSID----ETYN-TFKQIGKLTHHDKQAEQLVEETKDNIDKVID---SIPAHHKKsKVFIEV 164
Cdd:cd01142 95 WSTDGKEaGKAVLRLLNALSLRdaelEEVKlTIALLGELLGRQEKAEALVAYFDDNLAYVAArtkKLPDSERP-RVYYAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 165 SSKpeIYTAGKHTFFNDMLEKLEAQNVYSDI--NGWNPVTKESIIKKNPDILISTEAKTRsdymDIIKKRGGFNKINAVK 242
Cdd:cd01142 174 PDP--LTTDGTGSITNSWIDLAGGINVASEAtkKGSGEVSLEQLLKWNPDVIIVGNADTK----AAILADPRWQNLRAVK 247
|
....*..
gi 1390929086 243 NTRIEVV 249
Cdd:cd01142 248 NGRVYVN 254
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
18-246 |
2.51e-21 |
|
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238567 [Multi-domain] Cd Length: 262 Bit Score: 90.09 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 18 PYHRIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKD--VKKGKKQFDAL----------NLNKEELLKAKPDLILAHES 85
Cdd:cd01147 4 PVERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEGrpYFLASPELKDLpvigrggrgnTPNYEKIAALKPDVVIDVGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 86 QKATanKVLSSLEKQ-GIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLV---EETKDNIDKVIDSIPAHHKKSkVF 161
Cdd:cd01147 84 DDPT--SIADDLQKKtGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELIsfiESILADVEERTKDIPDEEKPT-VY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 162 IEvsskpEIYTAGKHTFFND------MLEKLEAQNVYSDINGWN--PVTKESIIKKNPDILISTEAKTRSDYMDIIKKRG 233
Cdd:cd01147 161 FG-----RIGTKGAAGLESGlagsieVFELAGGINVADGLGGGGlkEVSPEQILLWNPDVIFLDTGSFYLSLEGYAKNRP 235
|
250
....*....|...
gi 1390929086 234 GFNKINAVKNTRI 246
Cdd:cd01147 236 FWQSLKAVKNGRV 248
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
66-246 |
1.98e-16 |
|
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238559 [Multi-domain] Cd Length: 342 Bit Score: 77.73 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 66 NLNKEELLKAKPDLILAHESQKAT--ANKVLSSLEKQGIKVVYVKDAQSIDEtyNTFKQI---GKLTHHDKQAEQLVEET 140
Cdd:cd01139 81 DFSVEKVLTLKPDLVILNIWAKTTaeESGILEKLEQAGIPVVFVDFRQKPLK--NTTPSMrllGKALGREERAEEFIEFY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 141 KDNIDKVIDSIPA-HHKKSKVFIEVSSK-PEIY--TAGKHTFfNDMLEKLEAQNVYSDING--WNPVTKESIIKKNPDIL 214
Cdd:cd01139 159 QERIDRIRDRLAKiNEPKPKVFIELGAGgPEECcsTYGNGNW-GELVDAAGGDNIADGLIPgtSGELNAEYVIAANPEII 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390929086 215 I------------------STEAKTRSDYMDIIKKRGGFNKINAVKNTRI 246
Cdd:cd01139 238 IatggnwakdpsgvslgpdGTTADAKESLLRALLKRPGWSSLQAVKNGRV 287
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
21-252 |
6.85e-15 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 73.03 E-value: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGKyiVGVSTVDDYPKDVKKGKKQFDAL---------NLnkEELLKAKPDLILA----HESQK 87
Cdd:COG4594 54 RVVVLEWSFADALLALGVTP--VGIADDNDYDRWVPYLRDLIKGVtsvgtrsqpNL--EAIAALKPDLIIAdksrHEAIY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 88 ATANK-----VLSSLEKQgikvvYvkdaqsiDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAHHKKSKVFI 162
Cdd:COG4594 130 DQLSKiaptvLFKSRNGD-----Y-------QENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 163 EVSSKPEIYTAGKHTFFNDMLEKLEAQNVYS----DINGWNPVTKESIIKKNPDILISTEAKTRSDYmDIIKKRGGFNKI 238
Cdd:COG4594 198 GQFRADGLRLYTPNSFAGSVLAALGFENPPKqskdNGYGYSEVSLEQLPALDPDVLFIATYDDPSIL-KEWKNNPLWKNL 276
|
250
....*....|....
gi 1390929086 239 NAVKNTRIEVVNGD 252
Cdd:COG4594 277 KAVKNGRVYEVDGD 290
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
21-246 |
1.95e-11 |
|
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238560 [Multi-domain] Cd Length: 270 Bit Score: 62.66 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEILYELGLGkyIVGVSTVDDYPKDVK--KGKKQFDALNL---NKEELLKAKPDLILaheSQKATANKVLS 95
Cdd:cd01140 14 KVVVFDVGALDTLDALGVK--VVGVPKSSTLPEYLKkyKDDKYANVGTLfepDLEAIAALKPDLII---IGGRLAEKYDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 96 SLEKQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPahhKKSKVFIEVSSKPEIYTAGK 175
Cdd:cd01140 89 LKKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAK---GKKKALVVLVNGGKLSAFGP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 176 HTFFNDMLEKLEAQNVYSDINGWN---PVTKESIIKKNPDIL--------ISTEAKTRSDYM--DIIKkrggfnKINAVK 242
Cdd:cd01140 166 GSRFGWLHDLLGFEPADENIKASShgqPVSFEYILEANPDWLfvidrgaaIGAEGSSAKEVLdnDLVK------NTTAWK 239
|
....
gi 1390929086 243 NTRI 246
Cdd:cd01140 240 NGKV 243
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
16-185 |
6.02e-08 |
|
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238561 [Multi-domain] Cd Length: 186 Bit Score: 51.65 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 16 KSPYHRIVSLMPSNTEILYELGLGKYIVGVS--TVDDYPKDVKKGKKQF--DALNLNKEELLKAKPDLILAheSQKATAN 91
Cdd:cd01141 5 KVPPKRIVVLSPTHVDLLLALDKADKIVGVSasAYDLNTPAVKERIDIQvgPTGSLNVELIVALKPDLVIL--YGGFQAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 92 KVLSSLEKQGIKVVYVKDAQS----IDETYNTFKQIGKLThhdkqaEQLVEETKDNIDKVIDSIPAHHK---KSKVFIEV 164
Cdd:cd01141 83 TILDKLEQLGIPVLYVNEYPSplgrAEWIKFAAAFYGVGK------EDKADEAFAQIAGRYRDLAKKVSnlnKPTVAIGK 156
|
170 180
....*....|....*....|.
gi 1390929086 165 SSKPEIYTAGKHTFFNDMLEK 185
Cdd:cd01141 157 PVKGLWYMPGGNSYVAKMLRD 177
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
21-252 |
1.26e-05 |
|
Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238558 [Multi-domain] Cd Length: 248 Bit Score: 45.40 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 21 RIVSLMPSNTEilyELGLGKYIVGVSTVD----DYPKDVKKGKKQfDALNLNKEELLKAKPDLILAHESQKATANKvlss 96
Cdd:cd01138 11 RIVALSGETEG---LALLGIKPVGAASIGgknpYYKKKTLAKVVG-IVDEPNLEKVLELKPDLIIVSSKQEENYEK---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 97 LEKQGIKVVYVKDAQSIDEtynTFKQIGKLTHHDKQAE-------QLVEETKDNIDKVIDsipahhKKSKVFIEVSSKpE 169
Cdd:cd01138 83 LSKIAPTVPVSYNSSDWEE---QLKEIGKLLNKEDEAEkwladykQKAKEAKEKIKKKLG------NDKSVAVLRGRK-Q 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 170 IYTAGK-HTFFNDMLEK---LEAQNVYSDIN---GWNPVTKESIIKKNPD---ILISTEAKTRSDYMdiikKRGGFNKIN 239
Cdd:cd01138 153 IYVFGEdGRGGGPILYAdlgLKAPEKVKEIEdkpGYAAISLEVLPEFDADyifLLFFTGPEAKADFE----SLPIWKNLP 228
|
250
....*....|...
gi 1390929086 240 AVKNTRIEVVNGD 252
Cdd:cd01138 229 AVKNNHVYIVDAW 241
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
43-256 |
6.02e-05 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 43.51 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 43 VGVSTV---DDYPK-----DVKKGKKQFDALNLNKEELLKA----KPDLILAHESQKATANKVLSSLEkqgiKVVYVKda 110
Cdd:PRK11411 56 VGVSPVgvaDDNDAkrilpEVRAHLKPWQSVGTRSQPSLEAiaalKPDLIIADSSRHAGVYIALQKIA----PTLLLK-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390929086 111 qSIDETY----NTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPahhKKSKVFIEVSSKPEIYTAGKHTFFNDMLEKL 186
Cdd:PRK11411 130 -SRNETYqenlQSAAIIGEVLGKKREMQARIEQHKERMAQFASQLP---KGTRVAFGTSREQQFNLHSPESYTGSVLAAL 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390929086 187 EAQNVYSDING--WNPVTKESIIKKNPDILISTEAKTRSdymdIIK---KRGGFNKINAVKNTRIEVVNGDEVSR 256
Cdd:PRK11411 206 GLNVPKAPMNGaaMPSISLEQLLALNPDWLLVAHYRQES----IVKrwqQDPLWQMLTAAKKQQVASVDSNTWAR 276
|
|
| |
