NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1493556022|ref|NP_001353710|]
View 

protein BCAP isoform f [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 340-596 8.73e-09

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 58.93  E-value: 8.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 419
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  420 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 497
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  498 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 577
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903

                          250
                   ....*....|....*....
gi 1493556022  578 KILDLETELRKKNEEQNQL 596
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 135-443 1.71e-05

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  135 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 214
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  215 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 294
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  295 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 371
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493556022  372 LQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 443
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 340-596 8.73e-09

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: 58.93  E-value: 8.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 419
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  420 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 497
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  498 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 577
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903

                          250
                   ....*....|....*....
gi 1493556022  578 KILDLETELRKKNEEQNQL 596
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
420-596 9.93e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 9.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  420 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 487
Cdd:COG4913    242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  488 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 561
Cdd:COG4913    321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1493556022  562 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 596
Cdd:COG4913    401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 135-443 1.71e-05

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: 48.13  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  135 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 214
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  215 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 294
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  295 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 371
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493556022  372 LQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 443
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
187-591 4.07e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 187 ERLQIQIHKREAENdkLKEYVKSLETKIAKwnlqsrmnkneaivmkeaSRQKTVALKKASKVYKQRLDHFTGAIEKLTSQ 266
Cdd:PRK02224  333 CRVAAQAHNEEAES--LREDADDLEERAEE------------------LREEAAELESELEEAREAVEDRREEIEELEEE 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 267 IRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME---DHGK-NSCEEILRK---VHSIEY 339
Cdd:PRK02224  393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEallEAGKcPECGQPVEGsphVETIEE 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 340 ENEtlnlENTKLKTTLAALKDEVVSVE---NELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitk 416
Cdd:PRK02224  473 DRE----RVEELEAELEDLEEEVEEVEerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA--------- 539

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 417 tknknvEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQgqvdgnhNLLTKLSLEEEncl 496
Cdd:PRK02224  540 ------EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-------RIRTLLAAIAD--- 603

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 497 IQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYtalARQLEAALEEGRQKVAEEIEKMSSRESALQ 576
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEE---AREDKERAEEYLEQVEEKLDELREERDDLQ 680

                         410
                  ....*....|....*
gi 1493556022 577 IKILDLETELRKKNE 591
Cdd:PRK02224  681 AEIGAVENELEELEE 695
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
196-396 2.47e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 196 REAENDKLKEYVKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL- 274
Cdd:COG3206   166 LELRREEARKALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLa 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 275 --------SETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEY 339
Cdd:COG3206   244 alraqlgsGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEA 320

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1493556022 340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 396
Cdd:COG3206   321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 33-624 3.88e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.57  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022   33 ESHLSCLKQDILNEKTELEATLKEAElvtHSVELLLPLFKDTIEKInfenanLSALNLKISEQKEILIKELDTFKSVKLA 112
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQ---NKIELLLQQHQDRIEQL------ISEHEVEITGLTEKASSARSQANSIQSQ 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  113 LEHLlrkrdyKQTGDNLSSMLLENLTDNESENTNLKKKVFEK----EAHIQELS---CLFQSEKANT-LKANRFSQSVKV 184
Cdd:pfam15921  301 LEII------QEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEkqlVLANSELTEArTERDQFSQESGN 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  185 VHERLQ---IQIHKREAENDKLKEYVKSLETK-----IAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQR--LD 254
Cdd:pfam15921  375 LDDQLQkllADLHKREKELSLEKEQNKRLWDRdtgnsITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMaaIQ 454

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  255 HFTGAIEKLTSQIRDQEA------KLSETISASNAWKSHYEKIVIEKT----ELEVQIETMKKQIINL----------LE 314
Cdd:pfam15921  455 GKNESLEKVSSLTAQLEStkemlrKVVEELTAKKMTLESSERTVSDLTaslqEKERAIEATNAEITKLrsrvdlklqeLQ 534

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  315 DLKKMEDHGKN---SCEEILRKVHSIEYENETL--NLENT------------KLKTTLAALKDEVVSVENELSELQEVEK 377
Cdd:pfam15921  535 HLKNEGDHLRNvqtECEALKLQMAEKDKVIEILrqQIENMtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKD 614

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  378 KQKTLIEMYKTQVQKLQ-EAAEIVKSRCENLlhknnQITKTKNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQES 456
Cdd:pfam15921  615 KKDAKIRELEARVSDLElEKVKLVNAGSERL-----RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEE 689

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  457 LQCCKGKCADQehtIRELQGQVDGNHNLLTklSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKF 536
Cdd:pfam15921  690 METTTNKLKMQ---LKSAQSELEQTRNTLK--SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK 764

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  537 KEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQlvCKMNSKAQHQEVCLKEVQN 616
Cdd:pfam15921  765 HFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAE--CQDIIQRQEQESVRLKLQH 841


                   ....*...
gi 1493556022  617 SLEKSENQ 624
Cdd:pfam15921  842 TLDVKELQ 849
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 307-420 1.63e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 39.61  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 307 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 386
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1493556022 387 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 420
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-563 3.91e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918  200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSML------LENLTDNESENTNLKKKVFEKEAHIQELSC 163
Cdd:PRK03918  280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerIKELEEKEERLEELKKKLKELEKRLEELEE 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 164 ---LFQSEKANTLKANRFSQSVKVVH-ERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:PRK03918  360 rheLYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 240 VALKKASKVYKQRLdhftgaIEKLTSQIRDQEAKLSETISASnawkshyEKIVIEKTELEVQIETMKKqIINLLEDLKKM 319
Cdd:PRK03918  440 VCGRELTEEHRKEL------LEEYTAELKRIEKELKEIEEKE-------RKLRKELRELEKVLKKESE-LIKLKELAEQL 505

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 320 EdhgknSCEEILRKVHSIEYENETLNLEntKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktqvqKLQEaaei 399
Cdd:PRK03918  506 K-----ELEEKLKKYNLEELEKKAEEYE--KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK-------KLDE---- 567

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 400 VKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDS---LTAAERRLHECQESLQCCKGKCADQEHTIRELQG 476
Cdd:PRK03918  568 LEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRK 647

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 477 QVDGnhnlLTKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLK--HSNLKFKEKSAEYTALARQLEAAL 554
Cdd:PRK03918  648 ELEE----LEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEklKEELEEREKAKKELEKLEKALERV 723


                  ....*....
gi 1493556022 555 EEGRQKVAE 563
Cdd:PRK03918  724 EELREKVKK 732
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 340-596 8.73e-09

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: 58.93  E-value: 8.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 419
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  420 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 497
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  498 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 577
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903

                          250
                   ....*....|....*....
gi 1493556022  578 KILDLETELRKKNEEQNQL 596
Cdd:TIGR02169  904 KIEELEAQIEKKRKRLSEL 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 293-597 4.20e-07

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: 53.52  E-value: 4.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  293 IEKTELEVQIETMKKQIINLLEDLKKMEDhgknSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSEL 372
Cdd:TIGR02168  225 LELALLVLRLEELREELEELQEELKEAEE----ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  373 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQItktkNKNVEKMRGQMESHLKELERVCDSLTAAERRLHE 452
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELESLEAELEELEAELEELESRLEE 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  453 CQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENcliqLKCENLQQKLEQMDAENKELEKKLANQEECLKHS 532
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQAELEELEEELEEL 452

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1493556022  533 NLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQikilDLETELRKKNEEQNQLV 597
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQA-LDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALL 512
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
420-596 9.93e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 9.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  420 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 487
Cdd:COG4913    242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  488 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 561
Cdd:COG4913    321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1493556022  562 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 596
Cdd:COG4913    401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 135-443 1.71e-05

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: 48.13  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  135 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 214
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  215 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 294
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  295 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 371
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493556022  372 LQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 443
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
187-591 4.07e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 187 ERLQIQIHKREAENdkLKEYVKSLETKIAKwnlqsrmnkneaivmkeaSRQKTVALKKASKVYKQRLDHFTGAIEKLTSQ 266
Cdd:PRK02224  333 CRVAAQAHNEEAES--LREDADDLEERAEE------------------LREEAAELESELEEAREAVEDRREEIEELEEE 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 267 IRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME---DHGK-NSCEEILRK---VHSIEY 339
Cdd:PRK02224  393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEallEAGKcPECGQPVEGsphVETIEE 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 340 ENEtlnlENTKLKTTLAALKDEVVSVE---NELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitk 416
Cdd:PRK02224  473 DRE----RVEELEAELEDLEEEVEEVEerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA--------- 539

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 417 tknknvEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQgqvdgnhNLLTKLSLEEEncl 496
Cdd:PRK02224  540 ------EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-------RIRTLLAAIAD--- 603

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 497 IQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYtalARQLEAALEEGRQKVAEEIEKMSSRESALQ 576
Cdd:PRK02224  604 AEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEE---AREDKERAEEYLEQVEEKLDELREERDDLQ 680

                         410
                  ....*....|....*
gi 1493556022 577 IKILDLETELRKKNE 591
Cdd:PRK02224  681 AEIGAVENELEELEE 695
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 241-526 4.95e-05

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: 46.59  E-value: 4.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  241 ALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKme 320
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-- 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  321 dhgknsceeilrkvhsIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 400
Cdd:TIGR02168  321 ----------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  401 KSRCENLLHKNNQITKTknknVEKMRGQMESHLKELERVCDSLTAAERRLHECQesLQCCKGKCADQEHTIRELQGQVDG 480
Cdd:TIGR02168  385 RSKVAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELER 458

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1493556022  481 NHNLLTKLSLEEEncLIQLKCENLQQKLEQMDAENKELEKKLANQE 526
Cdd:TIGR02168  459 LEEALEELREELE--EAEQALDAAERELAQLQARLDSLERLQENLE 502
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
258-620 8.65e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 8.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 258 GAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNS------CEEIL 331
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeLEEKV 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 332 RKVHSIEYENET----------LNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTL----------IEMYKTQVQ 391
Cdd:PRK03918  283 KELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELkkklkelekrLEELEERHE 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 392 KLQEAAEIvKSRCENLLHK--NNQITKTKNK--NVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQ 467
Cdd:PRK03918  363 LYEEAKAK-KEELERLKKRltGLTPEKLEKEleELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 468 EHTIRElqgqvDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEECLKhsnlkFKEKSAEYTALA 547
Cdd:PRK03918  442 GRELTE-----EHRKELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELE 509

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1493556022 548 RQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVcKMNSKAQHQEVCLKEVQNSLEK 620
Cdd:PRK03918  510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEE 581
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-558 1.06e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 252 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 331
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 332 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 411
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 412 NQITKTKNKNVEKmrgqmESHLKELERVCDSLTAAERRLHECQESLQcckgkcADQEHTIRELqgqvdgnhnlltkLSLE 491
Cdd:COG1196   386 EELLEALRAAAEL-----AAQLEELEEAEEALLERLERLEEELEELE------EALAELEEEE-------------EEEE 441

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1493556022 492 EENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGR 558
Cdd:COG1196   442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
PTZ00121 PTZ00121
MAEBL; Provisional
 139-636 1.24e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  139 DNESENTNLKKKVFEKEAHIQELSCLFQSEKAntlkanRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKiaKWN 218
Cdd:PTZ00121  1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEA------RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKA 1317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  219 LQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKiVIEKTEL 298
Cdd:PTZ00121  1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEA 1396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  299 EVQIETMKKQIINL--LEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVE 376
Cdd:PTZ00121  1397 KKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  377 KKQKTliemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN-KNVEKMRGQMESHLKELERVCDSLTAAERR-----L 450
Cdd:PTZ00121  1477 KKAEE-----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadeL 1551

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  451 HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQM-DAENKELEKKLANQEECL 529
Cdd:PTZ00121  1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEELKKAEEE 1631

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  530 KHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKmsSRESALQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEV 609
Cdd:PTZ00121  1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK--AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709

                          490       500
                   ....*....|....*....|....*..
gi 1493556022  610 CLKEVQNSLEKSENQNESIKNYLQFLK 636
Cdd:PTZ00121  1710 KEAEEKKKAEELKKAEEENKIKAEEAK 1736
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 296-595 1.52e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 296 TELEVQIETMKKQiinlledLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEV 375
Cdd:COG1196   196 GELERQLEPLERQ-------AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 376 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN----------KNVEKMRGQMESHLKELERVCDSLTA 445
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerleeleEELAELEEELEELEEELEELEEELEE 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 446 AERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLK-----CENLQQKLEQMDAENKELEK 520
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEeleeaEEALLERLERLEEELEELEE 428

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1493556022 521 KLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQ 595
Cdd:COG1196   429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
PRK11637 PRK11637
AmiB activator; Provisional
 418-591 1.89e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.30  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 418 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK---------- 487
Cdd:PRK11637   59 KEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAqldaafrqge 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 488 -------LSLEEE-------------NCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLkhSNLKFKEKSAEYTALA 547
Cdd:PRK11637  139 htglqliLSGEESqrgerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQARNE 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1493556022 548 RQ-----LEAALEEGRQKVAEeiekMSSRESALQIKILDLETELRKKNE 591
Cdd:PRK11637  217 RKktltgLESSLQKDQQQLSE----LRANESRLRDSIARAEREAKARAE 261
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
196-396 2.47e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 196 REAENDKLKEYVKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL- 274
Cdd:COG3206   166 LELRREEARKALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLa 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 275 --------SETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEY 339
Cdd:COG3206   244 alraqlgsGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEA 320

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1493556022 340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 396
Cdd:COG3206   321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 33-624 3.88e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.57  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022   33 ESHLSCLKQDILNEKTELEATLKEAElvtHSVELLLPLFKDTIEKInfenanLSALNLKISEQKEILIKELDTFKSVKLA 112
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQ---NKIELLLQQHQDRIEQL------ISEHEVEITGLTEKASSARSQANSIQSQ 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  113 LEHLlrkrdyKQTGDNLSSMLLENLTDNESENTNLKKKVFEK----EAHIQELS---CLFQSEKANT-LKANRFSQSVKV 184
Cdd:pfam15921  301 LEII------QEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEkqlVLANSELTEArTERDQFSQESGN 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  185 VHERLQ---IQIHKREAENDKLKEYVKSLETK-----IAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQR--LD 254
Cdd:pfam15921  375 LDDQLQkllADLHKREKELSLEKEQNKRLWDRdtgnsITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMaaIQ 454

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  255 HFTGAIEKLTSQIRDQEA------KLSETISASNAWKSHYEKIVIEKT----ELEVQIETMKKQIINL----------LE 314
Cdd:pfam15921  455 GKNESLEKVSSLTAQLEStkemlrKVVEELTAKKMTLESSERTVSDLTaslqEKERAIEATNAEITKLrsrvdlklqeLQ 534

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  315 DLKKMEDHGKN---SCEEILRKVHSIEYENETL--NLENT------------KLKTTLAALKDEVVSVENELSELQEVEK 377
Cdd:pfam15921  535 HLKNEGDHLRNvqtECEALKLQMAEKDKVIEILrqQIENMtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKD 614

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  378 KQKTLIEMYKTQVQKLQ-EAAEIVKSRCENLlhknnQITKTKNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQES 456
Cdd:pfam15921  615 KKDAKIRELEARVSDLElEKVKLVNAGSERL-----RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEE 689

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  457 LQCCKGKCADQehtIRELQGQVDGNHNLLTklSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKF 536
Cdd:pfam15921  690 METTTNKLKMQ---LKSAQSELEQTRNTLK--SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK 764

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  537 KEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQlvCKMNSKAQHQEVCLKEVQN 616
Cdd:pfam15921  765 HFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAE--CQDIIQRQEQESVRLKLQH 841


                   ....*...
gi 1493556022  617 SLEKSENQ 624
Cdd:pfam15921  842 TLDVKELQ 849
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 232-438 3.90e-04

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: 43.21  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 232 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 311
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 312 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 377
Cdd:COG4942   102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1493556022 378 KQKTLiemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELER 438
Cdd:COG4942   182 ELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 428-596 5.87e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 428 QMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENC-----LIQLKCE 502
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiaRLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 503 NLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDL 582
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         170
                  ....*....|....
gi 1493556022 583 ETELRKKNEEQNQL 596
Cdd:COG1196   393 RAAAELAAQLEELE 406
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 418-642 6.67e-04

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: 43.12  E-value: 6.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  418 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVdgnhnlltkLSLEEENCLI 497
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL---------TELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  498 QLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTalarqleaALEEGRQKVAEEIEKMSSRESALQI 577
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------LLNEEAANLRERLESLERRIAATER 838

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1493556022  578 KILDLETELRKKNEEQNQLVCKMNSkaqhQEVCLKEVQNSLEKSENQNESIKNYLQFLKTSYVTM 642
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEE----LEELIEELESELEALLNERASLEEALALLRSELEEL 899
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 297-575 8.60e-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: 42.75  E-value: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  297 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 373
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  374 EVEKKQKTLIEMYKTQVQKLQEAAEIVKSRcenLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTA----AERR 449
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeyLEKE 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  450 LHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKL-----SLEEENCLIQLKCENLQQKLEQMDAENKELEKKLAN 524
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1493556022  525 QEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQ-----KVAEEIEKMSSRESAL 575
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsleDVQAELQRVEEEIRAL 970
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
433-609 8.62e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 8.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 433 LKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMD 512
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 513 AENKELEKKLANQEECLKhsnlKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEE 592
Cdd:COG4717   153 ERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228

                         170
                  ....*....|....*..
gi 1493556022 593 QNQLVCKMNSKAQHQEV 609
Cdd:COG4717   229 LEQLENELEAAALEERL 245
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 47-601 1.19e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  47 KTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTG 126
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 127 DNLSSMLLE-----------NLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHK 195
Cdd:TIGR04523 199 LELLLSNLKkkiqknkslesQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 196 REAENDKLKEYVKSLETKIAKWNLQSRMNKNEAI--VMKEASRQKTVALKKASKVyKQRLDHFTGAIEKLTSQIRDQEAK 273
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELksELKNQEKKLEEIQNQISQN-NKIISQLNEQISQLKKELTNSESE 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 274 LSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEIlrkvHSIEYENETLNLENTKLKT 353
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI----KKLQQEKELLEKEIERLKE 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 354 TLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENllhknnqiTKTKNKNVEKMRGQMESHL 433
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ--------KQKELKSKEKELKKLNEEK 505

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 434 KELERVCDSLTAAERRLHECQESLQCCKGKcadQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMDA 513
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKE---KESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKK 582

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 514 ENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRqKVAEEIEKMSSRESALQIKILDLETELRKKNEEQ 593
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661


                  ....*...
gi 1493556022 594 NQLVCKMN 601
Cdd:TIGR04523 662 PEIIKKIK 669
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 307-420 1.63e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 39.61  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 307 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 386
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1493556022 387 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 420
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 373-597 1.81e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 41.55  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 373 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKEL--ERVCDSLTAAERRL 450
Cdd:pfam05667 243 RKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLqfTNEAPAATSSPPTK 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 451 HECQESLQcckgkcADQEHTIRELQGQVDGNHNLLTKLSLEEENCliQLKCENLQQKLEQMDAENKELEKKLANQ----- 525
Cdd:pfam05667 323 VETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKKL--ESSIKQVEEELEELKEQNEELEKQYKVKkktld 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 526 -----EECLKHSNLKFKEKSAEYTALARQLEA----------ALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKN 590
Cdd:pfam05667 395 llpdaEENIAKLQALVDASAQRLVELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKE 474


                  ....*..
gi 1493556022 591 EEQNQLV 597
Cdd:pfam05667 475 ELYKQLV 481
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 367-600 2.56e-03

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: 41.21  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  367 NELSELQEVEKKQKTLIEMYKTQVQKLQeaaeivKSRCENLLHKNNQITKTKNKNVEKMRgQMESHLKELERVCDSLTAA 446
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLR------REREKAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  447 ERRLHECQESLQCCKGKCADQEHTIRELQGQVDgnhnlltKLSlEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQE 526
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-------DLG-EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1493556022  527 ECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVCKM 600
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-452 2.59e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 166 QSEKAntLKANRFSQSVKVV-HERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEaivmKEASRQKTVALKK 244
Cdd:COG1196   208 QAEKA--ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE----LEELRLELEELEL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 245 ASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGK 324
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 325 NSCEEILRKVHSIEYENETLNlentKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRC 404
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELE----ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1493556022 405 ENLLHKNNQITKTKNKNVEKMRgQMESHLKELERVCDSLTAAERRLHE 452
Cdd:COG1196   438 EEEEEALEEAAEEEAELEEEEE-ALLELLAELLEEAALLEAALAELLE 484
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-563 3.91e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918  200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSML------LENLTDNESENTNLKKKVFEKEAHIQELSC 163
Cdd:PRK03918  280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerIKELEEKEERLEELKKKLKELEKRLEELEE 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 164 ---LFQSEKANTLKANRFSQSVKVVH-ERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:PRK03918  360 rheLYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 240 VALKKASKVYKQRLdhftgaIEKLTSQIRDQEAKLSETISASnawkshyEKIVIEKTELEVQIETMKKqIINLLEDLKKM 319
Cdd:PRK03918  440 VCGRELTEEHRKEL------LEEYTAELKRIEKELKEIEEKE-------RKLRKELRELEKVLKKESE-LIKLKELAEQL 505

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 320 EdhgknSCEEILRKVHSIEYENETLNLEntKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktqvqKLQEaaei 399
Cdd:PRK03918  506 K-----ELEEKLKKYNLEELEKKAEEYE--KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK-------KLDE---- 567

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 400 VKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDS---LTAAERRLHECQESLQCCKGKCADQEHTIRELQG 476
Cdd:PRK03918  568 LEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRK 647

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022 477 QVDGnhnlLTKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLK--HSNLKFKEKSAEYTALARQLEAAL 554
Cdd:PRK03918  648 ELEE----LEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEklKEELEEREKAKKELEKLEKALERV 723


                  ....*....
gi 1493556022 555 EEGRQKVAE 563
Cdd:PRK03918  724 EELREKVKK 732
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 344-633 4.28e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  344 LNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhkNNQITKTKNkNVE 423
Cdd:TIGR00606  693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV---NRDIQRLKN-DIE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  424 KMRGQMESHLKELERVCDSLTAAERrLHECQESLQcckgkcaDQEHTIRELQGQVDGNHNLLTKLSLEEENcliqlkcEN 503
Cdd:TIGR00606  769 EQETLLGTIMPEEESAKVCLTDVTI-MERFQMELK-------DVERKIAQQAAKLQGSDLDRTVQQVNQEK-------QE 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  504 LQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLE--AALEEGRQKVAEEIEKMSSRESALQIKILD 581
Cdd:TIGR00606  834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQrrQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1493556022  582 LETELRKKNEEQNQLVCKMNSKAQHQEVCLKEVQNSLEKSENQNESIKNYLQ 633
Cdd:TIGR00606  914 LETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
PTZ00121 PTZ00121
MAEBL; Provisional
 195-629 4.60e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  195 KREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL 274
Cdd:PTZ00121  1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  275 SETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNS-----CEEILRKVHSIEYENETLN-LEN 348
Cdd:PTZ00121  1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeakkADEAKKKAEEAKKADEAKKkAEE 1494

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  349 TKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSrceNLLHKNNQITKTKN-KNVEKMRG 427
Cdd:PTZ00121  1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA---DELKKAEELKKAEEkKKAEEAKK 1571

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  428 QMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGnhnllTKLSLEEENCLIQLKCENLQQK 507
Cdd:PTZ00121  1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-----LKKAEEEKKKVEQLKKKEAEEK 1646

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  508 LEQMDAENKELEKKLANQEECLKHSNLKFK---------EKSAEYTALARQLEAA--LEEGRQKVAEEIEKMSSRESALQ 576
Cdd:PTZ00121  1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKaeeakkaeeDEKKAAEALKKEAEEAkkAEELKKKEAEEKKKAEELKKAEE 1726

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1493556022  577 IKILDLEtELRKKNEEQNqlvcKMNSKAQHQEVCLKEVQNSLEKSENQNESIK 629
Cdd:PTZ00121  1727 ENKIKAE-EAKKEAEEDK----KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 193-626 5.41e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  193 IHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEaiVMKEASRQKtvALKKASKVYKQRLDHFTG----AIEKLTSQIR 268
Cdd:pfam12128  236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSD--ETLIASRQE--ERQETSAELNQLLRTLDDqwkeKRDELNGELS 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  269 DQEAKLS---ETISASNAWKSHYEKIVIEKTELEV-QIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETl 344
Cdd:pfam12128  312 AADAAVAkdrSELEALEDQHGAFLDADIETAAADQeQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNR- 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  345 nlENTKLKTTLAALKDEVVSVENELSElqEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKT------- 417
Cdd:pfam12128  391 --DIAGIKDKLAKIREARDRQLAVAED--DLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATpelllql 466

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  418 --KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVD-GNHNLLTKLSLE--- 491
Cdd:pfam12128  467 enFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFpQAGTLLHFLRKEapd 546

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  492 ------------------------EENCLIQLKCENLQQKLEQMD-----AENKELEKKLANQEECLKHSNLKFKEKSAE 542
Cdd:pfam12128  547 weqsigkvispellhrtdldpevwDGSVGGELNLYGVKLDLKRIDvpewaASEEELRERLDKAEEALQSAREKQAAAEEQ 626

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493556022  543 YTALARQLEAA-LEEGRQKVA-----EEIEKMSSRESALQIKILD-LETELRKKNEEQNQLVCKMNSKAQHQEVCLKEVQ 615
Cdd:pfam12128  627 LVQANGELEKAsREETFARTAlknarLDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK 706

                          490
                   ....*....|.
gi 1493556022  616 NslEKSENQNE 626
Cdd:pfam12128  707 E--QKREARTE 715
 
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