NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|528512017|ref|XP_005160865|]
View 

beta-taxilin isoform X2 [Danio rerio]

Protein Classification

taxilin( domain architecture ID 12101238)

taxilin is a myosin-like coiled-coil protein involved in intracellular vesicle traffic

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
96-403 8.16e-87

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


:

Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 277.22  E-value: 8.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   96 KEAASLLQSLNKLGSPEEKVEMVLKKYSELVDEHRTEKKQLEQFQQRQGLLVKQRDQLQFEHSRAILARSKLETLCRELQ 175
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  176 RHNRTLKEESLQRLREDEMKRKEITTHFQSTLVDIQSQIEQHSNRNNKLCKENSELAGKLKTIIEQYERREESLEKIFKH 255
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  256 RDLQQKLSDAKLEEANMlltqAEEKHKREKEYllTQAAEWKLQAKELKEQHTIMQAQLVLYSQKFDDFQNTLAKSNEIYV 335
Cdd:pfam09728 161 KELEVQLAEAKLQQATE----EEEKKAQEKEV--AKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528512017  336 TFKQEMDKMTKKMKKLEKESTTWKTRFESCNKALVEMIDERSEKGKEFELFTLKIDRLETLCRALQDE 403
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
PTZ00121 super family cl31754
MAEBL; Provisional
493-788 1.18e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  493 EAQSIKQADQLESTQEQSSTT-----KVIEEKPTA---TKSEMDSKLPEAPQLESIKPVDQLKSTQDESSTIKVTITEKK 564
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKadeakKAAEAKKKAdeaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  565 PTSPATTKPDtESKIPPEPFPKDTKPVDKLESTEEKSITEDLKPEVAVNAVKPliptilEDAKPEMESKLPEETLKlvdk 644
Cdd:PTZ00121 1558 KKAEEKKKAE-EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA------EEAKKAEEAKIKAEELK---- 1626
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  645 pKSTQVKSSTTEKQNTEKPSVPTIPELTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDTFKQESAQPKPVVKEESKDE 724
Cdd:PTZ00121 1627 -KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528512017  725 AVKPEVPEPEPPKQEPLKEEDTQKATAVSEGAKASAIKPKAPKSQDAKAKASKAQPKKQTPAKK 788
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
96-403 8.16e-87

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 277.22  E-value: 8.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   96 KEAASLLQSLNKLGSPEEKVEMVLKKYSELVDEHRTEKKQLEQFQQRQGLLVKQRDQLQFEHSRAILARSKLETLCRELQ 175
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  176 RHNRTLKEESLQRLREDEMKRKEITTHFQSTLVDIQSQIEQHSNRNNKLCKENSELAGKLKTIIEQYERREESLEKIFKH 255
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  256 RDLQQKLSDAKLEEANMlltqAEEKHKREKEYllTQAAEWKLQAKELKEQHTIMQAQLVLYSQKFDDFQNTLAKSNEIYV 335
Cdd:pfam09728 161 KELEVQLAEAKLQQATE----EEEKKAQEKEV--AKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528512017  336 TFKQEMDKMTKKMKKLEKESTTWKTRFESCNKALVEMIDERSEKGKEFELFTLKIDRLETLCRALQDE 403
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
PTZ00121 PTZ00121
MAEBL; Provisional
493-788 1.18e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  493 EAQSIKQADQLESTQEQSSTT-----KVIEEKPTA---TKSEMDSKLPEAPQLESIKPVDQLKSTQDESSTIKVTITEKK 564
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKadeakKAAEAKKKAdeaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  565 PTSPATTKPDtESKIPPEPFPKDTKPVDKLESTEEKSITEDLKPEVAVNAVKPliptilEDAKPEMESKLPEETLKlvdk 644
Cdd:PTZ00121 1558 KKAEEKKKAE-EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA------EEAKKAEEAKIKAEELK---- 1626
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  645 pKSTQVKSSTTEKQNTEKPSVPTIPELTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDTFKQESAQPKPVVKEESKDE 724
Cdd:PTZ00121 1627 -KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528512017  725 AVKPEVPEPEPPKQEPLKEEDTQKATAVSEGAKASAIKPKAPKSQDAKAKASKAQPKKQTPAKK 788
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
61-319 3.46e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  61 KDEEAKADEESESKEVAAGADKEQNTEKKLLKgLGKEAASLLQSLNKLgspEEKVEMVLKKYSELVDEHRTEKKQLEQFQ 140
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEEL---ELELEEAQAEEYELLAELARLEQDIARLE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 141 QRQGLLVKQRDQLQFEH----SRAILARSKLETLCRELQRHNRTLKE------ESLQRLREDEMKRKEITTHFQSTLVDI 210
Cdd:COG1196  309 ERRRELEERLEELEEELaeleEELEELEEELEELEEELEEAEEELEEaeaelaEAEEALLEAEAELAEAEEELEELAEEL 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 211 QSQIEQHSNRNNKLCKENSELAGKLKTIIEQYERREESLEKIFKHRDLQQKLSDAKLEEANMLLTQAEEKHKREKEYLLT 290
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
                        250       260
                 ....*....|....*....|....*....
gi 528512017 291 QAAEWKLQAKELKEQHTIMQAQLVLYSQK 319
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
14-254 2.72e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017    14 EQVNESEEQQVDPM-EDFSRQLEDIINTYGSASSLMQEQISILES--EEGKDEEAKADEE-SESKEVAAGADKEQNTEKK 89
Cdd:TIGR02169  271 EQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERelEDAEERLAKLEAEiDKLLAEIEELEREIEEERK 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017    90 LLKGLGKEAASLLQSLNKLgspEEKVEMVLKKYSELVDEHRTEKKQLEQFQQRQGLLVKQRDQLQFEHSRAILARSKLET 169
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDL---RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   170 -LCRELQRHNR--TLKEESLQRLREDEMKRKEItthfQSTLVDIQSQIEQHSNRNNKLCKENSELAGKL------KTIIE 240
Cdd:TIGR02169  428 aIAGIEAKINEleEEKEDKALEIKKQEWKLEQL----AADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaeaqARASE 503
                          250
                   ....*....|....
gi 528512017   241 QYERREESLEKIFK 254
Cdd:TIGR02169  504 ERVRGGRAVEEVLK 517
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
503-720 8.25e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 8.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 503 LESTQEQSSTTKVIEEKPTATKSEMDSKLPEAPQLESIKPVDQLKSTQDESSTIKVTITEKKPTSPATTKPDTESKIPPE 582
Cdd:NF033839 214 LDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPS 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 583 PFPKDTKPVDKLESTEEKSITEDLKPEVAVNAVKPLIPTILEDAKPEMESKLPEETLKLVDKPKSTQVKSSTTEKQNTEK 662
Cdd:NF033839 294 APKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPK 373
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528512017 663 PSVPTIPELTKPEVESKL--PQEAGKPESAKEEPR-QEEVKKAEDTFKQESAQPKPVVKEE 720
Cdd:NF033839 374 PEVKPQPETPKPEVKPQPekPKPEVKPQPEKPKPEvKPQPEKPKPEVKPQPEKPKPEVKPQ 434
PRK12704 PRK12704
phosphodiesterase; Provisional
182-285 1.28e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 182 KEESLQRLREDEMKRKEITTHFQSTLVDIQSQIEQHSNRNNKLCKENSELAGKLKTI---IEQYERREESLEK-IFKHRD 257
Cdd:PRK12704  63 KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELeqkQQELEKKEEELEElIEEQLQ 142
                         90       100
                 ....*....|....*....|....*....
gi 528512017 258 LQQKLSDAKLEEA-NMLLTQAEEKHKREK 285
Cdd:PRK12704 143 ELERISGLTAEEAkEILLEKVEEEARHEA 171
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
582-705 4.72e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 40.26  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  582 EPFPKDTKPVDKLESTEEKSITEDLKPEVAVNAVKpLIPT--ILEDAKPEMESKLPEE--TLKLVDKPKSTQVKSSTTEK 657
Cdd:TIGR00601  11 QKFKIDMEPDETVKELKEKIEAEQGKDAYPVAQQK-LIYSgkILSDDKTVKEYKIKEKdfVVVMVSKPKTGTGKVAPPAA 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 528512017  658 QNTEKPSVPTIPELTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDT 705
Cdd:TIGR00601  90 TPTSAPTPTPSPPASPASGMSAAPASAVEEKSPSEESATATAPESPST 137
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
571-789 4.77e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 40.46  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  571 TKPDTESKIPPEPFPKDTKPVDKLESTEEKSITEDLKPEvavnavkpliPTILEDAKPemESKLPEETLKLVDKPKSTQV 650
Cdd:NF033875   48 TQPGTTTVQPDNPDPQSGSETPKTAVSEEATVQKDTTSQ----------PTKVEEVAS--EKNGAEQSSATPNDTTNAQQ 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  651 KSSTTEKQNTEKPSVP---TIPELTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDTFKQEsaqPKPVVKEESKDEAVK 727
Cdd:NF033875  116 PTVGAEKSAQEQPVVSpetTNEPLGQPTEVAPAENEANKSTSIPKEFETPDVDKAVDEAKKD---PNITVVEKPAEDLGN 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528512017  728 PEVPEPEPPKQEPLKEEDTQKATAVSEGAKASAIKPKAPKSQ---DAKAKASKAQPKKQTPAKKK 789
Cdd:NF033875  193 VSSKDLAAKEKEVDQLQKEQAKKIAQQAAELKAKNEKIAKENaeiAAKNKAEKERYEKEVAEYNK 257
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
96-403 8.16e-87

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 277.22  E-value: 8.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   96 KEAASLLQSLNKLGSPEEKVEMVLKKYSELVDEHRTEKKQLEQFQQRQGLLVKQRDQLQFEHSRAILARSKLETLCRELQ 175
Cdd:pfam09728   1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  176 RHNRTLKEESLQRLREDEMKRKEITTHFQSTLVDIQSQIEQHSNRNNKLCKENSELAGKLKTIIEQYERREESLEKIFKH 255
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  256 RDLQQKLSDAKLEEANMlltqAEEKHKREKEYllTQAAEWKLQAKELKEQHTIMQAQLVLYSQKFDDFQNTLAKSNEIYV 335
Cdd:pfam09728 161 KELEVQLAEAKLQQATE----EEEKKAQEKEV--AKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFT 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528512017  336 TFKQEMDKMTKKMKKLEKESTTWKTRFESCNKALVEMIDERSEKGKEFELFTLKIDRLETLCRALQDE 403
Cdd:pfam09728 235 TFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLCRALQAE 302
PTZ00121 PTZ00121
MAEBL; Provisional
493-788 1.18e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  493 EAQSIKQADQLESTQEQSSTT-----KVIEEKPTA---TKSEMDSKLPEAPQLESIKPVDQLKSTQDESSTIKVTITEKK 564
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKadeakKAAEAKKKAdeaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  565 PTSPATTKPDtESKIPPEPFPKDTKPVDKLESTEEKSITEDLKPEVAVNAVKPliptilEDAKPEMESKLPEETLKlvdk 644
Cdd:PTZ00121 1558 KKAEEKKKAE-EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA------EEAKKAEEAKIKAEELK---- 1626
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  645 pKSTQVKSSTTEKQNTEKPSVPTIPELTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDTFKQESAQPKPVVKEESKDE 724
Cdd:PTZ00121 1627 -KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528512017  725 AVKPEVPEPEPPKQEPLKEEDTQKATAVSEGAKASAIKPKAPKSQDAKAKASKAQPKKQTPAKK 788
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
61-319 3.46e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  61 KDEEAKADEESESKEVAAGADKEQNTEKKLLKgLGKEAASLLQSLNKLgspEEKVEMVLKKYSELVDEHRTEKKQLEQFQ 140
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEEL---ELELEEAQAEEYELLAELARLEQDIARLE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 141 QRQGLLVKQRDQLQFEH----SRAILARSKLETLCRELQRHNRTLKE------ESLQRLREDEMKRKEITTHFQSTLVDI 210
Cdd:COG1196  309 ERRRELEERLEELEEELaeleEELEELEEELEELEEELEEAEEELEEaeaelaEAEEALLEAEAELAEAEEELEELAEEL 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 211 QSQIEQHSNRNNKLCKENSELAGKLKTIIEQYERREESLEKIFKHRDLQQKLSDAKLEEANMLLTQAEEKHKREKEYLLT 290
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
                        250       260
                 ....*....|....*....|....*....
gi 528512017 291 QAAEWKLQAKELKEQHTIMQAQLVLYSQK 319
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
27-322 7.13e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 7.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  27 MEDFSRQLEDIINTYGSASSLMQEQISILESEEGKDEEAKADEESESKEVAAGADKEQNtekkllkgLGKEAASLLQSLN 106
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE--------LLAELARLEQDIA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 107 KLgspEEKVEMVLKKYSELVDEHRTEKKQLEQFQQRQGLLVKQRDQLQFEHSRAILARSKLETLCRELQRhNRTLKEESL 186
Cdd:COG1196  306 RL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAEEEL 381
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 187 QRLREDEMKRKEITTHFQSTLVDIQSQIEQHSNRNNKLCKENSELAGKLKTIIEQYERREESLEkifkhrdlQQKLSDAK 266
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE--------EAAEEEAE 453
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528512017 267 LEEANMLLTQAEEKHKREKEYLLTQAAEWKLQAKELKEQHTIMQAQLVLYSQKFDD 322
Cdd:COG1196  454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
PTZ00121 PTZ00121
MAEBL; Provisional
243-791 5.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  243 ERREESLEKIFKHRDLQQKLSDAKLEEANMLLTQAEE-KHKREKEYLLTQAAEWKLQAKELKEQHTIMQAQLVLYSQKFD 321
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEaRMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  322 DFQNTLAKSNEiyvtfKQEMDKMTKKMKKLEKESTTWKTRFESCNKALVEMIDERSEKGKEFELFTLKIDRLETLCRALQ 401
Cdd:PTZ00121 1303 KADEAKKKAEE-----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  402 DERKSLYAKIKEIRFPEKMTAAPVVDIPPIDELPELVQTPNpmlTAEMEKLRAEQVRLQDFAASLLNPIPDvAGESDSED 481
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK---KADEAKKKAEEKKKADEAKKKAEEAKK-ADEAKKKA 1453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  482 EEKEKDSPAIPEAQSIKQADQLESTQEQSSTTKVIEEKPTATKSEMDSKLPEApqlESIKPVDQLKSTQDESSTIKVTIT 561
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA---EAKKKADEAKKAEEAKKADEAKKA 1530
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  562 EKKPTSPATTKPDTESKIPPEPFPKDTKPVDKLESTEEKSITEDLKPEVAVNAVkplIPTILEDAKPEMESKLPEETLKL 641
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKM 1607
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  642 vdkpKSTQVKSSTTEKQNTEKpsvptipelTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDTFKQESAQPKPVVKEES 721
Cdd:PTZ00121 1608 ----KAEEAKKAEEAKIKAEE---------LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528512017  722 K--DEAVKPEVPEPEPPKQEPLKEEDTQKATAVSEGAKASAIKPKAPKSQDAKAKASKAQPKKQTPAKKKGA 791
Cdd:PTZ00121 1675 KkaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
PTZ00121 PTZ00121
MAEBL; Provisional
524-798 6.51e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 6.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  524 KSEMDSKLPEAPQLESIKPVDQLKSTQDESSTIKVTITEKKPTSPATTKPDTESKIPPEPFPKDTKPVDKLESTEEKSIT 603
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  604 EDLKPEVAVNAVKPLIPTILEDAKPEMESKLPEETLKLVD--KPKSTQVKSSTTEKQNTEKPSVPTIPELTKPEVESKLP 681
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  682 QEAGKPES------AKEEPRQEEVKKAEDTFKQESAQPKPVVKEESKDEAVKPEVPEPEPPKQEPLKEEDTQKATAV--- 752
Cdd:PTZ00121 1373 KEEAKKKAdaakkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAkkk 1452
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 528512017  753 -SEGAKASAIKPKAPKSQDAKAKASKAQPKKQTPAKKKGAAKGPNKS 798
Cdd:PTZ00121 1453 aEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
14-254 2.72e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017    14 EQVNESEEQQVDPM-EDFSRQLEDIINTYGSASSLMQEQISILES--EEGKDEEAKADEE-SESKEVAAGADKEQNTEKK 89
Cdd:TIGR02169  271 EQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERelEDAEERLAKLEAEiDKLLAEIEELEREIEEERK 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017    90 LLKGLGKEAASLLQSLNKLgspEEKVEMVLKKYSELVDEHRTEKKQLEQFQQRQGLLVKQRDQLQFEHSRAILARSKLET 169
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDL---RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   170 -LCRELQRHNR--TLKEESLQRLREDEMKRKEItthfQSTLVDIQSQIEQHSNRNNKLCKENSELAGKL------KTIIE 240
Cdd:TIGR02169  428 aIAGIEAKINEleEEKEDKALEIKKQEWKLEQL----AADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaeaqARASE 503
                          250
                   ....*....|....
gi 528512017   241 QYERREESLEKIFK 254
Cdd:TIGR02169  504 ERVRGGRAVEEVLK 517
PTZ00121 PTZ00121
MAEBL; Provisional
493-791 4.84e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  493 EAQSIKQADQLESTQEQSSTTKVIEEKPTAT--KSEMDSKLPEAPQLESIKPVDQLKSTQDESStikvtITEKKPTSPAT 570
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKAEDAKK-----AEAVKKAEEAK 1236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  571 TKPDTESKIPPEPFPKDTKPVDKLESTEEKSITEDLKPEVAVNAvkpliptilEDAKPEMESKLPEETLKLVDKPKSTQV 650
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA---------DELKKAEEKKKADEAKKAEEKKKADEA 1307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  651 KSSTTEKQNTEKPSVPTIPELTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDTFKQESAQPKPVVKEESK-DEAVKPE 729
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKaDAAKKKA 1387
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528512017  730 VPEPEPPKQEPLKEEDTQKATAVSEGA----KASAIKPKAPKSQDAKAKASKAQPKKQTPAKKKGA 791
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKAAaakkKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA 1453
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
503-720 8.25e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 8.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 503 LESTQEQSSTTKVIEEKPTATKSEMDSKLPEAPQLESIKPVDQLKSTQDESSTIKVTITEKKPTSPATTKPDTESKIPPE 582
Cdd:NF033839 214 LDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPS 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 583 PFPKDTKPVDKLESTEEKSITEDLKPEVAVNAVKPLIPTILEDAKPEMESKLPEETLKLVDKPKSTQVKSSTTEKQNTEK 662
Cdd:NF033839 294 APKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPK 373
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528512017 663 PSVPTIPELTKPEVESKL--PQEAGKPESAKEEPR-QEEVKKAEDTFKQESAQPKPVVKEE 720
Cdd:NF033839 374 PEVKPQPETPKPEVKPQPekPKPEVKPQPEKPKPEvKPQPEKPKPEVKPQPEKPKPEVKPQ 434
PRK12704 PRK12704
phosphodiesterase; Provisional
182-285 1.28e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 182 KEESLQRLREDEMKRKEITTHFQSTLVDIQSQIEQHSNRNNKLCKENSELAGKLKTI---IEQYERREESLEK-IFKHRD 257
Cdd:PRK12704  63 KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELeqkQQELEKKEEELEElIEEQLQ 142
                         90       100
                 ....*....|....*....|....*....
gi 528512017 258 LQQKLSDAKLEEA-NMLLTQAEEKHKREK 285
Cdd:PRK12704 143 ELERISGLTAEEAkEILLEKVEEEARHEA 171
valS PRK14900
valyl-tRNA synthetase; Provisional
629-798 1.38e-03

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 42.29  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  629 EMESKLpEETLKLVDKPKSTQVKSSTTEKQNTEKPSvptipeltkpevesklpQEAGKPESAKEE--PRQEEVKKAEDTF 706
Cdd:PRK14900  891 EKRGKL-EAHRAMLSGSEANSARRDTMEIQNEQKPT-----------------QDGPAAEAQPAQenTVVESAEKAVAAV 952
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  707 KQESAQPKPVVKEeskdeAVKPEVPEPEPPKQEPLKEEDTQKATAVSEGAKASAIKPKAPKSQDAKAKASKAQPKKQTPA 786
Cdd:PRK14900  953 SEAAQQAATAVAS-----GIEKVAEAVRKTVRRSVKKAAATRAAMKKKVAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPA 1027
                         170
                  ....*....|..
gi 528512017  787 KKKGAAKGPNKS 798
Cdd:PRK14900 1028 KKVARKPAAKKA 1039
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
493-783 1.66e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 493 EAQSIKQADQLESTQEQSSTTK---VIEEKPTatKSEMDSKLPEAPQlESIKPVDQlkstqDESSTIKVTITEKKPTSPA 569
Cdd:PTZ00449 539 ESDEPKEGGKPGETKEGEVGKKpgpAKEHKPS--KIPTLSKKPEFPK-DPKHPKDP-----EEPKKPKRPRSAQRPTRPK 610
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 570 TTKPDTESKIPPEPF-----------PKDTKPVDKLESTEEKSITEDLKPEvavnavKPLIPTiledaKPEMESKLPEET 638
Cdd:PTZ00449 611 SPKLPELLDIPKSPKrpespkspkrpPPPQRPSSPERPEGPKIIKSPKPPK------SPKPPF-----DPKFKEKFYDDY 679
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 639 LKLVDKPKSTQVKSSTTEKQNT----EKPSVPTIPELTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDTFKQESAQPK 714
Cdd:PTZ00449 680 LDAAAKSKETKTTVVLDESFESilkeTLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTF 759
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 715 pvVKEESKDeavkpevPEPEPPKQEPLKEEDTQKATAVSEGAKAsaiKPKAP-KSQDAKAKASKAQPKKQ 783
Cdd:PTZ00449 760 --FHETPAD-------TPLPDILAEEFKEEDIHAETGEPDEAMK---RPDSPsEHEDKPPGDHPSLPKKR 817
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
489-640 2.07e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.77  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 489 PAIPEAQSIKQADQLESTQEQSSTTKVIEEKPTATKSEMDSKLPEAPQLESIKPVDQLKSTQDESSTIKVTITEKKPTSP 568
Cdd:PRK07994 372 PQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEPAAASRARP 451
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528512017 569 ATTKPDTESKIPPEPFPKDTKPVDKlESTEEKSITEDLKPEVAVNAVKPLIPTILEDAKPEMESKLPEETLK 640
Cdd:PRK07994 452 VNSALERLASVRPAPSALEKAPAKK-EAYRWKATNPVEVKKEPVATPKALKKALEHEKTPELAAKLAAEAIE 522
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
55-328 2.11e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017    55 LESEEGKDEEAKADEESESKEVAAGADKEQNTEKKLlkglgkeaaSLLQSlnKLGSPEEKVEMVLKKYSELVDEHRTEKK 134
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKL---------EELRL--EVSELEEEIEELQKELYALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   135 QLEQFQQRQGLLVKQRDQLQFEHSRailARSKLETLCRELQRHNRTLKE--ESLQRLREDEMKRKEITTHFQSTLVDIQS 212
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEE---LESKLDELAEELAELEEKLEElkEELESLEAELEELEAELEELESRLEELEE 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   213 QIEQHSNRNNKLCKENSELAGKLKTIIEQYERREESLEKifkhRDLQQKLSDAKLEEANMLLTQAE-EKHKREKEYLLTQ 291
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQAElEELEEELEELQEE 455
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 528512017   292 AAEWKLQAKELKEQHTIMQAQLVLYSQKFDDFQNTLA 328
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
65-286 2.42e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  65 AKADEESESKEVAAGADKEQNTEKKLLKGLGKEAASLLQSLNKLgspEEKVEMVLKKYSELVDEHRTEKKQLEQFQQRQG 144
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKEIA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 145 LLVKQRDQLQFEHSRAILARSKLETLCRE---LQRHNRTLKEESLQRLREDEMKRKEITTHFQSTLVDIQSQIEQHSNRN 221
Cdd:COG4942   94 ELRAELEAQKEELAELLRALYRLGRQPPLallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528512017 222 NKLCKENSELAGKLKTIIEQYERREESLEKIFKHRDLQQKLSDAKLEEANMLLTQAEEKHKREKE 286
Cdd:COG4942  174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
21-291 3.93e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017    21 EQQVDPMEDFSRQLEDIINTYGSASSLMQEQISILESEEGKDEEAKADEESESKEVAAGADKEQN---TEKKLLKGLGKE 97
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkALREALDELRAE 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017    98 AASL----LQSLNKLGSPEEKVEMVLKKYSELVDEHRTEKKQLEQFQQRQGLLVKQRDQLQFEHSRAILARSKLETLcRE 173
Cdd:TIGR02168  812 LTLLneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA-LA 890
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   174 LQRHNRTLKEESLQRLREDEMKRKEITTHFQSTLVDIQSQIEQ-HSNRNNKLCKENSELAGKLKTIIEQYERREESLEKI 252
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 528512017   253 FKH-RDLQQKLsdAKLEEANMLLTQAEEKHKREKEYLLTQ 291
Cdd:TIGR02168  971 RRRlKRLENKI--KELGPVNLAAIEEYEELKERYDFLTAQ 1008
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
582-705 4.72e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 40.26  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  582 EPFPKDTKPVDKLESTEEKSITEDLKPEVAVNAVKpLIPT--ILEDAKPEMESKLPEE--TLKLVDKPKSTQVKSSTTEK 657
Cdd:TIGR00601  11 QKFKIDMEPDETVKELKEKIEAEQGKDAYPVAQQK-LIYSgkILSDDKTVKEYKIKEKdfVVVMVSKPKTGTGKVAPPAA 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 528512017  658 QNTEKPSVPTIPELTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDT 705
Cdd:TIGR00601  90 TPTSAPTPTPSPPASPASGMSAAPASAVEEKSPSEESATATAPESPST 137
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
673-798 4.75e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017 673 KPEVESKLPQEAGKPESAKEEPRQE-EVKKAEDTFKQESAQPKPVVKEESKDEAVKPEVPEPEPPKQEPLKEEDTQKATA 751
Cdd:PRK09510 126 QAALKQKQAEEAAAKAAAAAKAKAEaEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528512017 752 VSEGAKASAIKPKAPKsqDAKAKASKAQPKKQTPAKKKGAAKGPNKS 798
Cdd:PRK09510 206 EAKKKAAAEAKKKAAA--EAKAAAAKAAAEAKAAAEKAAAAKAAEKA 250
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
571-789 4.77e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 40.46  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  571 TKPDTESKIPPEPFPKDTKPVDKLESTEEKSITEDLKPEvavnavkpliPTILEDAKPemESKLPEETLKLVDKPKSTQV 650
Cdd:NF033875   48 TQPGTTTVQPDNPDPQSGSETPKTAVSEEATVQKDTTSQ----------PTKVEEVAS--EKNGAEQSSATPNDTTNAQQ 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  651 KSSTTEKQNTEKPSVP---TIPELTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDTFKQEsaqPKPVVKEESKDEAVK 727
Cdd:NF033875  116 PTVGAEKSAQEQPVVSpetTNEPLGQPTEVAPAENEANKSTSIPKEFETPDVDKAVDEAKKD---PNITVVEKPAEDLGN 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528512017  728 PEVPEPEPPKQEPLKEEDTQKATAVSEGAKASAIKPKAPKSQ---DAKAKASKAQPKKQTPAKKK 789
Cdd:NF033875  193 VSSKDLAAKEKEVDQLQKEQAKKIAQQAAELKAKNEKIAKENaeiAAKNKAEKERYEKEVAEYNK 257
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
176-415 6.00e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   176 RHNRTLKEESLQRLREDEMKRKEITTHFQsTLVDIQSQIEQHSNRNNKLCKENSELAGKLKTIIEQYERREESLEKIFKH 255
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   256 RDLQQKLSDAKLEEANMLLTQAEEkhkrEKEYLLTQAAEWKLQAKELKEQHTIMQAQLVLYSQKFDDFQNTLAKSNEIYV 335
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017   336 TFKQEMDKMTKKMKKLEKESTTWKTRFESCNKALVEMIDERSEKGKEFELFTLKIDRLETLCRALQDERKSLYAKIKEIR 415
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
PHA03247 PHA03247
large tegument protein UL36; Provisional
421-717 6.72e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  421 TAAPVVDI---PPIDELPElvQTPNPMLTAEMEKLRAEQVRlQDFAASLLNPIPDVAgesdsedeekeKDSPAIPEAQSI 497
Cdd:PHA03247 2691 TVGSLTSLadpPPPPPTPE--PAPHALVSATPLPPGPAAAR-QASPALPAAPAPPAV-----------PAGPATPGGPAR 2756
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  498 KQADQLESTQEQSSTTKVIEEKP--TATKSEMDSKLPEAPQLESIK-PVDQLKSTQDESSTIKVTITEKKPTSPATTKPD 574
Cdd:PHA03247 2757 PARPPTTAGPPAPAPPAAPAAGPprRLTRPAVASLSESRESLPSPWdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQP 2836
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528512017  575 TESKIPPEPFPkdtkpvdklesteeksitEDLKPEVAVNAVKPLI---PTILEDAKPEMESKLPEETLKLVDKPKSTQvk 651
Cdd:PHA03247 2837 TAPPPPPGPPP------------------PSLPLGGSVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLARPAVSRSTE-- 2896
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528512017  652 sstTEKQNTEKPSVPTIPELTKPEVESKLPQEAGKPESAKEEPRQEEVKKAEDTFKQESAQPKPVV 717
Cdd:PHA03247 2897 ---SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAV 2959
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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