|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1511-1801 |
1.69e-123 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 390.89 E-value: 1.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1511 NRLMQDEIARLRLEKDTIKNQNLEK--KYLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLE 1588
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKekKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1589 KQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHV-------LILSLQLSKAESKS 1661
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1662 RVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQ----ERFCQLKKQNMLLQQQLDDA 1737
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQesleERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613720 1738 RNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAER 1801
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-260 |
9.48e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 167.44 E-value: 9.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034613720 196 LGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDL 260
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
36-128 |
5.63e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 115
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034613720 116 LLLQNGANPNITD 128
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
36-223 |
1.49e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 90.49 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLAC-----ATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ--L 108
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 109 RQEACATLLLQNGANPNITDFFGRTALHYAV-YNE-DTSMIEKLLSHGTNIEECSKCEY----------------QPLLF 170
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKiDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHY 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034613720 171 AVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDV 223
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1274-1904 |
1.53e-09 |
|
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: 63.21 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1274 KNSVLNTATKMKDVQTSTPAEQDLEMASEGEQKRLEEyennqpQVKNQIH----SRDDLDDIIQSSQTVSEDGDSLCCNC 1349
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN------QLQNTVHeleaAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1350 KNVI-----LLIDQHEMKCK-----DCVHLLKIKNTFCLWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKS 1419
Cdd:pfam15921 183 EGVLqeirsILVDFEEASGKkiyehDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1420 QLKHEilELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVS 1499
Cdd:pfam15921 263 QQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1500 EtDEKEDLLHENRLMQDEIARLRLEKDTIKNQ--NLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgqlAALT 1577
Cdd:pfam15921 341 E-DKIEELEKQLVLANSELTEARTERDQFSQEsgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG------NSIT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1578 DENttLRSKLEKQRESRQRLETEMQSYHcrlnaarcdhDQSHSSKRDQELAFQG---TVDKCRHLQENLNSHVLILSLQL 1654
Cdd:pfam15921 414 IDH--LRRELDDRNMEVQRLEALLKAMK----------SECQGQMERQMAAIQGkneSLEKVSSLTAQLESTKEMLRKVV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1655 SKAESKSRVLKTELHYTGE---ALKEKALVFEHVQSELKQKQS----QMKDIEKMYKSG---YNTMEKCIEKQERFCQLK 1724
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDltaSLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGdhlRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1725 KQNMLLQQQLDDARNKADNQEK---AILNIQARCDARVQNLQAECRKHRLLLEEDNKMlVNELnHSKEKECQYEKEK--- 1798
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IREL-EARVSDLELEKVKlvn 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1799 --AEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLD----QMRSQFQEIQDQLTATIRCTKEME 1872
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670
....*....|....*....|....*....|...
gi 1034613720 1873 G-DTQKLEVEHVMMRKIIKKQdDQIERLEKILQ 1904
Cdd:pfam15921 720 GsDGHAMKVAMGMQKQITAKR-GQIDALQSKIQ 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1517-1872 |
3.27e-08 |
|
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: 58.91 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1517 EIARLRLEKdtiKNQNLEKkyLKD--FEIvKRKHEDLQ---------KALKRNGETLAKTIacYSGQLAALTDENTTLRS 1585
Cdd:TIGR02168 175 KETERKLER---TRENLDR--LEDilNEL-ERQLKSLErqaekaeryKELKAELRELELAL--LVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1586 KLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQE---LAFQGTVDKC----RHLQE---NLNSHVLILSLQLS 1655
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLeqqkQILRErlaNLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1656 KAESKSRVLKTELHytgeALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQER-FCQLKKQNMLLQQQL 1734
Cdd:TIGR02168 327 ELESKLDELAEELA----ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1735 DDARNKADNQEKAILNIQARCDARVQNLQ-AECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRD 1813
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613720 1814 DVLNKGSATKALLDASSRHCTYlengmQDSRKKLDQMRSQFQEIQDQLTATIRCTKEME 1872
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGF-----SEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1397-1882 |
2.89e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1397 IRKLKNKASVLQKRISEKEEIKSQlkhEILELEKELcslrfaiqqeKKKRRNVEEVHQKVREKLRITEEQYRIEAdvtkp 1476
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEEL----------KEAEEKEEEYAELQEELEELEEELEELEA----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1477 ikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDfEIvKRKHEDLQKALK 1556
Cdd:COG4717 110 ---ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA-EL-AELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1557 RNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAArcdhdqshsskrdqelafqgtvDKC 1636
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA----------------------ALE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1637 RHLQENLNShVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMyksGYNTMEKCIEK 1716
Cdd:COG4717 243 ERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL---QALPALEELEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1717 QERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQAECRKHRL-LLEEDNKMLVNELNHSKEKECQYE 1795
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRAALEQAEEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1796 KEKAEREVAVRQLQQKRDDVLnkgsatkALLDASSRhcTYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDT 1875
Cdd:COG4717 399 ELKEELEELEEQLEELLGELE-------ELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
....*..
gi 1034613720 1876 QKLEVEH 1882
Cdd:COG4717 470 ELAELLQ 476
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
682-1153 |
6.66e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 682 SSQKQPALKATTDEEDSVSNIA-TEIKDGEKSGTVSSQKQPALKATTDEE----DSVSNIATEIKDGE---KSGTVSSQK 753
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAkkkaDAAKKKAEEKKKADeakKKAEEDKKK 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 754 QPALKATTDEK---DSVSNIATEIKDGEKSGTVSSQKPPALTATSDEEGS-----VLSIARENKDGEKSRTVSSRKKPAL 825
Cdd:PTZ00121 1407 ADELKKAAAAKkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeeAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 826 KATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEedsvLGIARENKDGEKSRTVSSEKppglKASSAEKDSVLN 905
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE----AKKAEEAKKADEAKKAEEKK----KADELKKAEELK 1558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 906 IARGKKDGEKTKRVSSRKKPSLEATSDEKDSfsnitREKKDGEISRKVSSQKPPALKGTSDEEDSVLGIARENKDGEKSR 985
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 986 TVSSEKPPGL----KATSDEKDSVLNIARGKKDGEKTRTVSSQKPPTLKATSDEEDSVLSIARENKDGEKSRTV----SS 1057
Cdd:PTZ00121 1634 KVEQLKKKEAeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkkeAE 1713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1058 EKPSGLKATSAEKDSVLNIARGKKYGEKTKRvssrKKPALKATSDEKDSVLYIAREKKdgEKSRTVSSPKQPALKAICDK 1137
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKK----KAEEAKKDEEEKKKIAHLKKEEE--KKAEEIRKEKEAVIEEELDE 1787
|
490
....*....|....*.
gi 1034613720 1138 EDSVPNMATEKKDEQI 1153
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDI 1803
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
92-229 |
1.33e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.08 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 92 NLCDREDRTPLIK-AVQLRQEACATLLLQNGANPNItdffGRTALHYAVyNEDTSMIEKLLSH-------GTNIE---EC 160
Cdd:TIGR00870 46 NCPDRLGRSALFVaAIENENLELTELLLNLSCRGAV----GDTLLHAIS-LEYVDAVEAILLHllaafrkSGPLElanDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 161 SKCEYQ----PLLFAVSRRKVKMVEFLLKKKANVNA------------IDYL--GRSALIHAVTLGEKDIVILLLQHNID 222
Cdd:TIGR00870 121 YTSEFTpgitALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALLSEDPAD 200
|
....*..
gi 1034613720 223 VLSRDAF 229
Cdd:TIGR00870 201 ILTADSL 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1391-1803 |
1.37e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1391 EQLRVKIRKLKNKASVLQKRISEKEEI-----KSQLKHEILELEKELCSLRFAIQQEKK--KRRNVEEVHQKVREKLRit 1463
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKK-- 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1464 EEQYRIEADVTKPIKPALKSAEvELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEiarLRLEKDTIKNQNLEKKYLKDF 1541
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKkaEEAKKADE---AKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1542 EIVKRKHEDLQKALKRNGETLAKTiacysgqlaALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSS 1621
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK---------AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1622 K-RDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIE 1700
Cdd:PTZ00121 1619 KiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1701 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAI--LNIQARCDARVQNLQAECRKHRLLLEEDNK 1778
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
410 420
....*....|....*....|....*
gi 1034613720 1779 MLVNELNHSKEKECQYEKEKAEREV 1803
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1396-1603 |
2.11e-05 |
|
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: 48.99 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1396 KIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQY-------- 1467
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelraele 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1468 RIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHE-NRLMQDEIARLRLEKDTIKNQNlekkylKDFEIVKR 1546
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALR------AELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613720 1547 KHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1603
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
114-220 |
1.68e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 46.54 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 114 ATLLLQNGA-----NPNITDFF-GRTALHYAVYNEDTSMIEKLLSHGTNI------------EECSKCEY--QPLLFAVS 173
Cdd:cd22192 66 AAVVLMEAApelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYgeHPLSFAAC 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034613720 174 RRKVKMVEFLLKKKANVNAIDYLGRSALiHavtlgekdivILLLQHN 220
Cdd:cd22192 146 VGNEEIVRLLIEHGADIRAQDSLGNTVL-H----------ILVLQPN 181
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
131-159 |
1.98e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 1.98e-04
10 20
....*....|....*....|....*....
gi 1034613720 131 GRTALHYAVYNEDTSMIEKLLSHGTNIEE 159
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1391-1628 |
2.32e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1391 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITEEQYRI 1469
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1470 EADVtKPIKPALKSAEVELKTGG--------NNSNQVSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKKYLKDF 1541
Cdd:PRK02224 432 EATL-RTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEE---LEAELEDLEEEVEEVEERLERAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1542 EIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhCRLNAARCDHDQSHSS 1621
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE--AREEVAELNSKLAELK 585
|
....*..
gi 1034613720 1622 KRDQELA 1628
Cdd:PRK02224 586 ERIESLE 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1380-1609 |
3.79e-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: 42.36 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1380 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcsLRFAIQQEKKKRRNVEEVHQKVREK 1459
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1460 LRiteeqyrieadvtkpikpalksaEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRlekDTIKNQNLEKkylk 1539
Cdd:TIGR02169 814 LR-----------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE---KEIENLNGKK---- 863
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1540 dfEIVKRKHEDLQKALKRngetlaktiacYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLN 1609
Cdd:TIGR02169 864 --EELEEELEELEAALRD-----------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1511-1801 |
1.69e-123 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 390.89 E-value: 1.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1511 NRLMQDEIARLRLEKDTIKNQNLEK--KYLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLE 1588
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKekKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1589 KQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHV-------LILSLQLSKAESKS 1661
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1662 RVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQ----ERFCQLKKQNMLLQQQLDDA 1737
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQesleERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613720 1738 RNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAER 1801
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-260 |
9.48e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 167.44 E-value: 9.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034613720 196 LGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDL 260
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
28-266 |
2.16e-41 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 154.73 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 28 IKPYHLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 107
Cdd:COG0666 17 LLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 108 LRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:COG0666 97 NGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613720 188 ANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDLPINSNP 266
Cdd:COG0666 177 ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-233 |
6.37e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 147.79 E-value: 6.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034613720 196 LGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIA 233
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-201 |
3.48e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 122.37 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
....*.
gi 1034613720 196 LGRSAL 201
Cdd:COG0666 284 DLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
45-252 |
2.16e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 111.20 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 45 LEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANP 124
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 125 NITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHA 204
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034613720 205 VTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEY 252
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
36-128 |
5.63e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 115
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034613720 116 LLLQNGANPNITD 128
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
36-223 |
1.49e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 90.49 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLAC-----ATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ--L 108
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 109 RQEACATLLLQNGANPNITDFFGRTALHYAV-YNE-DTSMIEKLLSHGTNIEECSKCEY----------------QPLLF 170
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKiDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHY 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034613720 171 AVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDV 223
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
135-227 |
3.26e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 135 LHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKkANVNAIDYlGRSALIHAVTLGEKDIVI 214
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034613720 215 LLLQHNIDVLSRD 227
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
44-249 |
1.99e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 84.24 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 44 NLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGAN 123
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 124 PNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKvKMVEfLLKKKANVNAIDYLGRSALIH 203
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIE-LLINNASINDQDIDGSTPLHH 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034613720 204 AVTLG-EKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNR--VIFDLI 249
Cdd:PHA02874 261 AINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKdpVIKDII 309
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
102-194 |
7.82e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.38 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 102 LIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGtNIEECSKcEYQPLLFAVSRRKVKMVE 181
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034613720 182 FLLKKKANVNAID 194
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
51-205 |
2.28e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 78.00 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 51 LLLTY-YDANKRDR-KERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITD 128
Cdd:PHA02878 152 LLLSYgADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 129 FFGRTALHYAV-YNEDTSMIEKLLSHGTNIEECSKC-EYQPLLFAV-SRRKVKMvefLLKKKANVNAIDYLGRSALIHAV 205
Cdd:PHA02878 232 KCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIkSERKLKL---LLEYGADINSLNSYKLTPLSSAV 308
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
32-280 |
2.36e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 74.68 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 32 HLKRIHRAVLHGNL--------EKLKYLLLTYYDANKRDRKERTALHLacatgqpemvhlLVSRRCElnlcdredrtPLI 103
Cdd:PHA03095 6 SVDIIMEAALYDYLlnasnvtvEEVRRLLAAGADVNFRGEYGKTPLHL------------YLHYSSE----------KVK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 104 KAVQLrqeacatlLLQNGANPNITDFFGRTALHYAVYNEDT-SMIEKLLSHGTNIEECSKCEYQPL--LFAVSRRKVKMV 180
Cdd:PHA03095 64 DIVRL--------LLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 181 EFLLKKKANVNAIDYLGRSALihAVTLGEKDIvilllqhNIDVLsRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEdl 260
Cdd:PHA03095 136 RLLLRKGADVNALDLYGMTPL--AVLLKSRNA-------NVELL-RLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAR-- 203
|
250 260
....*....|....*....|
gi 1034613720 261 pINSNPVSSQKQPALKATSG 280
Cdd:PHA03095 204 -IVRELIRAGCDPAATDMLG 222
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
100-223 |
4.94e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 73.55 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 100 TPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHY-----AVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSR 174
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034613720 175 RK--VKMVEFLLKKKANVNAIDYLGRSaLIHAVTLG---EKDIVILLLQHNIDV 223
Cdd:PHA03100 117 KSnsYSIVEYLLDNGANVNIKNSDGEN-LLHLYLESnkiDLKILKLLIDKGVDI 169
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
39-222 |
8.00e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 72.72 E-value: 8.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 39 AVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSR-----------RCELN-------------LC 94
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHgaipdvkypdiESELHdaveegdvkaveeLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 95 D----------REDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHG--TNIEECsk 162
Cdd:PHA02875 89 DlgkfaddvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKacLDIEDC-- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613720 163 CEYQPLLFAVSRRKVKMVEFLLKKKANvnaIDYLGR----SALIHAVTLGEKDIVILLLQHNID 222
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKngcvAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
32-252 |
3.23e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.55 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 32 HLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRT----------- 100
Cdd:PHA02876 145 YMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecavdskni 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 101 ------------------PLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTS-MIEKLLSHGTNIEECS 161
Cdd:PHA02876 225 dtikaiidnrsninkndlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 162 KCEYQPL-LFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGE-KDIVILLLQHNIDVLSRDAFRKIAGDYAIE 239
Cdd:PHA02876 305 IKGETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAV 384
|
250
....*....|...
gi 1034613720 240 AKNRVIFDLIYEY 252
Cdd:PHA02876 385 RNNVVIINTLLDY 397
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
36-223 |
8.39e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.01 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKL-KYLLLTYYDANKRDRKERTALHLACATG-QPEMVHLLVSRRCELNLCDREDRTPLIKAVQL-RQEA 112
Cdd:PHA02876 277 LHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLdRNKD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 113 CATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKM-VEFLLKKKANVN 191
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436
|
170 180 190
....*....|....*....|....*....|...
gi 1034613720 192 AIDYLGRSALIHAVTLGEK-DIVILLLQHNIDV 223
Cdd:PHA02876 437 SKNKDLSTPLHYACKKNCKlDVIEMLLDNGADV 469
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
36-193 |
1.05e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.17 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKE-RTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACA 114
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 115 TLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLL-FAVSRRKVKMVEFLLKKKANVNAI 193
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
30-194 |
2.06e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.07 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 30 PYHLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACAT--GQPEMVHLLVSRRCELNLCDREDRTPLIKAVq 107
Cdd:PHA03100 71 PLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 108 lrqEACAT------LLLQNGANPN----------------ITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEY 165
Cdd:PHA03100 150 ---ESNKIdlkilkLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
|
170 180
....*....|....*....|....*....
gi 1034613720 166 QPLLFAVSRRKVKMVEFLLKKKANVNAID 194
Cdd:PHA03100 227 TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
99-151 |
1.33e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 1.33e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034613720 99 RTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLL 151
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1274-1904 |
1.53e-09 |
|
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: 63.21 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1274 KNSVLNTATKMKDVQTSTPAEQDLEMASEGEQKRLEEyennqpQVKNQIH----SRDDLDDIIQSSQTVSEDGDSLCCNC 1349
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN------QLQNTVHeleaAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1350 KNVI-----LLIDQHEMKCK-----DCVHLLKIKNTFCLWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKS 1419
Cdd:pfam15921 183 EGVLqeirsILVDFEEASGKkiyehDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1420 QLKHEilELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVS 1499
Cdd:pfam15921 263 QQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1500 EtDEKEDLLHENRLMQDEIARLRLEKDTIKNQ--NLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgqlAALT 1577
Cdd:pfam15921 341 E-DKIEELEKQLVLANSELTEARTERDQFSQEsgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG------NSIT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1578 DENttLRSKLEKQRESRQRLETEMQSYHcrlnaarcdhDQSHSSKRDQELAFQG---TVDKCRHLQENLNSHVLILSLQL 1654
Cdd:pfam15921 414 IDH--LRRELDDRNMEVQRLEALLKAMK----------SECQGQMERQMAAIQGkneSLEKVSSLTAQLESTKEMLRKVV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1655 SKAESKSRVLKTELHYTGE---ALKEKALVFEHVQSELKQKQS----QMKDIEKMYKSG---YNTMEKCIEKQERFCQLK 1724
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDltaSLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGdhlRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1725 KQNMLLQQQLDDARNKADNQEK---AILNIQARCDARVQNLQAECRKHRLLLEEDNKMlVNELnHSKEKECQYEKEK--- 1798
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IREL-EARVSDLELEKVKlvn 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1799 --AEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLD----QMRSQFQEIQDQLTATIRCTKEME 1872
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670
....*....|....*....|....*....|...
gi 1034613720 1873 G-DTQKLEVEHVMMRKIIKKQdDQIERLEKILQ 1904
Cdd:pfam15921 720 GsDGHAMKVAMGMQKQITAKR-GQIDALQSKIQ 751
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
32-85 |
3.24e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 3.24e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034613720 32 HLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLV 85
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
36-255 |
6.63e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 60.36 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 116 LLLQNGANPNITDFFGRTALHYAV-YNEdtSMIEKLLSHGTnIEECSKCEYQPLLFAVSRR-KVKMVEFLLKKKANVNAI 193
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIiHNR--SAIELLINNAS-INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIK 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034613720 194 DYLGRSALIHAVTLGEKDIVILLLQHNIdVLSRDAFRKIAGDY--AIEAK-NRVIFDLIYEYERK 255
Cdd:PHA02874 285 DNKGENPIDTAFKYINKDPVIKDIIANA-VLIKEADKLKDSDFleHIEIKdNKEFSDFIKECNEE 348
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
44-194 |
8.63e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.04 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 44 NLEKLKYLLLTYYDANKRDRKERTALHLACATGQP--EMVHLLVSRRCELNLCDREDRTPLIKAVQlrQEACATLLLQN- 120
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLPl 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613720 121 ---GANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAID 194
Cdd:PHA03095 244 liaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
67-226 |
2.78e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.44 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 67 TALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANP---------------------- 124
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 125 -NITDFFGRTALHYAVYNEDTSMIEKLLSHG--TNIEECSKCeyQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSAL 201
Cdd:PHA02874 117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGadVNIEDDNGC--YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
|
170 180
....*....|....*....|....*
gi 1034613720 202 IHAVTLGEKDIVILLLQHNIDVLSR 226
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNK 219
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1517-1872 |
3.27e-08 |
|
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: 58.91 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1517 EIARLRLEKdtiKNQNLEKkyLKD--FEIvKRKHEDLQ---------KALKRNGETLAKTIacYSGQLAALTDENTTLRS 1585
Cdd:TIGR02168 175 KETERKLER---TRENLDR--LEDilNEL-ERQLKSLErqaekaeryKELKAELRELELAL--LVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1586 KLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQE---LAFQGTVDKC----RHLQE---NLNSHVLILSLQLS 1655
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLeqqkQILRErlaNLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1656 KAESKSRVLKTELHytgeALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQER-FCQLKKQNMLLQQQL 1734
Cdd:TIGR02168 327 ELESKLDELAEELA----ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1735 DDARNKADNQEKAILNIQARCDARVQNLQ-AECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRD 1813
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613720 1814 DVLNKGSATKALLDASSRHCTYlengmQDSRKKLDQMRSQFQEIQDQLTATIRCTKEME 1872
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGF-----SEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1394-1905 |
4.98e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.44 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1394 RVKIRKLKNKASVLQKRISEKE---EIKSQLKHEILE-LEKELCSLRFAIQQEKkkrrnveEVHQKVREKLRITEEQYRI 1469
Cdd:TIGR00618 186 FAKKKSLHGKAELLTLRSQLLTlctPCMPDTYHERKQvLEKELKHLREALQQTQ-------QSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1470 EAdvtkpikpALKSAEVELKTGGNNSNQVSETDEKED--------LLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDF 1541
Cdd:TIGR00618 259 QQ--------LLKQLRARIEELRAQEAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1542 EIVKRKHEDLQKALKRNGETLAKTIacysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhcrlNAARCDHDQSHSS 1621
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEI-----HIRDAHEVATSIREISCQQHTLTQHIHTLQQQ-----KTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1622 KRDQELAFQGTVDKCRHLQENLNSHVLIL--SLQLSKAESKSRVLKTELHYTGEALKEKALVfEHVQS--ELKQKQSQMK 1697
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAkkQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-ESAQSlkEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1698 DIEKMYKSGYNTMEKCIEK-QERFCQLKKQNMLLQQQLDDARNKADNQEK--AILNIQARCDARVQNLQAEC---RKHRL 1771
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLElQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqRGEQTYAQLETSEEDVYHQLtseRKQRA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1772 LLEEDnkmlVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGS-ATKALLDASSRHCTYLENGMQDSRKKLDQm 1850
Cdd:TIGR00618 560 SLKEQ----MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeAEDMLACEQHALLRKLQPEQDLQDVRLHL- 634
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613720 1851 rSQFQEIQDQLTATIrcTKEMEGDTQKLEVEHVMMRKIIKKQDDQI-ERLEKILQH 1905
Cdd:TIGR00618 635 -QQCSQELALKLTAL--HALQLTLTQERVREHALSIRVLPKELLASrQLALQKMQS 687
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
131-184 |
4.98e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 4.98e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034613720 131 GRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLL 184
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1394-1758 |
7.43e-08 |
|
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: 57.76 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1394 RVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITEEQYRIEAD 1472
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1473 VTKPIKpalKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQ-NLEKKYLKDFEIVKRKHEDL 1551
Cdd:TIGR02168 756 LTELEA---EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1552 QKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQG 1631
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1632 TVDKCRHLQENLNSHVlilsLQLSKAESKSRVLKTEL--HY--TGEALKEKALVFEHVQSELKQKQSQMK-DIEKMYKSG 1706
Cdd:TIGR02168 913 LRRELEELREKLAQLE----LRLEGLEVRIDNLQERLseEYslTLEEAEALENKIEDDEEEARRRLKRLEnKIKELGPVN 988
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1034613720 1707 YNTMEKCIEKQERFCQLKKQnmllQQQLDDARNKAdnqEKAILNIQARCDAR 1758
Cdd:TIGR02168 989 LAAIEEYEELKERYDFLTAQ----KEDLTEAKETL---EEAIEEIDREARER 1033
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
36-259 |
1.86e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.80 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTY-YDANKRDRKERTALHlACATGQ---PEMVHLLVSRRCELNLCDREDRTPLikAVQLRQE 111
Cdd:PHA03095 87 LHLYLYNATTLDVIKLLIKAgADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 112 ACAT----LLLQNGANPNITDFFGRTALHY---------AVYNEDT----------------------------SMIEKL 150
Cdd:PHA03095 164 NANVellrLLIDAGADVYAVDDRFRSLLHHhlqsfkpraRIVRELIragcdpaatdmlgntplhsmatgssckrSLVLPL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 151 LSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLL--QHNIDVLSR-- 226
Cdd:PHA03095 244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALakNPSAETVAAtl 323
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034613720 227 DAFRKIAGDYAIEAKNRVI--------FDLIYEYERKRYED 259
Cdd:PHA03095 324 NTASVAGGDIPSDATRLCVakvvlrgaFSLLPEPIRAYHAD 364
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1378-1699 |
2.11e-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: 56.22 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1378 LWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcslrfaiqQEKKKRRN--VEEVHQK 1455
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI--------EELQKELYalANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1456 VREKLRITEEQYRIEADvtkpikpaLKSAEVELKTGGnnsnqvSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEK 1535
Cdd:TIGR02168 301 EQQKQILRERLANLERQ--------LEELEAQLEELE------SKLDELAEELAE---LEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1536 KylKDFEIVKRKHEDLQKALkrngETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDH 1615
Cdd:TIGR02168 364 E--AELEELESRLEELEEQL----ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1616 DQSHSSKRDQELAfqgtvdKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQS------EL 1689
Cdd:TIGR02168 438 LQAELEELEEELE------ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkAL 511
|
330
....*....|
gi 1034613720 1690 KQKQSQMKDI 1699
Cdd:TIGR02168 512 LKNQSGLSGI 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1397-1882 |
2.89e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1397 IRKLKNKASVLQKRISEKEEIKSQlkhEILELEKELcslrfaiqqeKKKRRNVEEVHQKVREKLRITEEQYRIEAdvtkp 1476
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEEL----------KEAEEKEEEYAELQEELEELEEELEELEA----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1477 ikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDfEIvKRKHEDLQKALK 1556
Cdd:COG4717 110 ---ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA-EL-AELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1557 RNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAArcdhdqshsskrdqelafqgtvDKC 1636
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA----------------------ALE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1637 RHLQENLNShVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMyksGYNTMEKCIEK 1716
Cdd:COG4717 243 ERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL---QALPALEELEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1717 QERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQAECRKHRL-LLEEDNKMLVNELNHSKEKECQYE 1795
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRAALEQAEEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1796 KEKAEREVAVRQLQQKRDDVLnkgsatkALLDASSRhcTYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDT 1875
Cdd:COG4717 399 ELKEELEELEEQLEELLGELE-------ELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
....*..
gi 1034613720 1876 QKLEVEH 1882
Cdd:COG4717 470 ELAELLQ 476
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
164-217 |
1.51e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 1.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034613720 164 EYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLL 217
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
100-226 |
2.11e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 52.30 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 100 TPLIKAVQLRQEACATLLLQNGANPN-------------------------------ITDFF---GRTALHYAVYNEDTS 145
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDvkypdieselhdaveegdvkaveelldlgkfADDVFykdGMTPLHLATILKKLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 146 MIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQH--NIDV 223
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSgaNIDY 196
|
...
gi 1034613720 224 LSR 226
Cdd:PHA02875 197 FGK 199
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
43-192 |
2.69e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.56 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 43 GNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQ--N 120
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaS 615
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034613720 121 GANPNItdffGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNA 192
Cdd:PLN03192 616 ISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
57-105 |
3.88e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 3.88e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1034613720 57 DANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKA 105
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
65-118 |
5.19e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 5.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034613720 65 ERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLL 118
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
72-223 |
6.43e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.41 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 72 ACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSmIEKLL 151
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRIL 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034613720 152 SHGTNIEEcSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDV 223
Cdd:PLN03192 611 YHFASISD-PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
682-1153 |
6.66e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 682 SSQKQPALKATTDEEDSVSNIA-TEIKDGEKSGTVSSQKQPALKATTDEE----DSVSNIATEIKDGE---KSGTVSSQK 753
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAkkkaDAAKKKAEEKKKADeakKKAEEDKKK 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 754 QPALKATTDEK---DSVSNIATEIKDGEKSGTVSSQKPPALTATSDEEGS-----VLSIARENKDGEKSRTVSSRKKPAL 825
Cdd:PTZ00121 1407 ADELKKAAAAKkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeeAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 826 KATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEedsvLGIARENKDGEKSRTVSSEKppglKASSAEKDSVLN 905
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE----AKKAEEAKKADEAKKAEEKK----KADELKKAEELK 1558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 906 IARGKKDGEKTKRVSSRKKPSLEATSDEKDSfsnitREKKDGEISRKVSSQKPPALKGTSDEEDSVLGIARENKDGEKSR 985
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 986 TVSSEKPPGL----KATSDEKDSVLNIARGKKDGEKTRTVSSQKPPTLKATSDEEDSVLSIARENKDGEKSRTV----SS 1057
Cdd:PTZ00121 1634 KVEQLKKKEAeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkkeAE 1713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1058 EKPSGLKATSAEKDSVLNIARGKKYGEKTKRvssrKKPALKATSDEKDSVLYIAREKKdgEKSRTVSSPKQPALKAICDK 1137
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKK----KAEEAKKDEEEKKKIAHLKKEEE--KKAEEIRKEKEAVIEEELDE 1787
|
490
....*....|....*.
gi 1034613720 1138 EDSVPNMATEKKDEQI 1153
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDI 1803
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
36-225 |
1.24e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.88 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrrcELNLCDREDRTPLIK-AVQLRQEACA 114
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR---SINKCSVFYTLVAIKdAFNNRNVEIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 115 TLLLQNG--ANPNITDFFGRTALHYAVYneDTSMIEKLLSHGTNIEECSK-CEYQPLLFAVSRRKVKMVEFLLKKKANVN 191
Cdd:PHA02878 118 KIILTNRykNIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVN 195
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034613720 192 AIDYLGRSALIHAVTLGEKDIVILLLQH--NIDVLS 225
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENgaSTDARD 231
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
92-229 |
1.33e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.08 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 92 NLCDREDRTPLIK-AVQLRQEACATLLLQNGANPNItdffGRTALHYAVyNEDTSMIEKLLSH-------GTNIE---EC 160
Cdd:TIGR00870 46 NCPDRLGRSALFVaAIENENLELTELLLNLSCRGAV----GDTLLHAIS-LEYVDAVEAILLHllaafrkSGPLElanDQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 161 SKCEYQ----PLLFAVSRRKVKMVEFLLKKKANVNA------------IDYL--GRSALIHAVTLGEKDIVILLLQHNID 222
Cdd:TIGR00870 121 YTSEFTpgitALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALLSEDPAD 200
|
....*..
gi 1034613720 223 VLSRDAF 229
Cdd:TIGR00870 201 ILTADSL 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1391-1803 |
1.37e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1391 EQLRVKIRKLKNKASVLQKRISEKEEI-----KSQLKHEILELEKELCSLRFAIQQEKK--KRRNVEEVHQKVREKLRit 1463
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKK-- 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1464 EEQYRIEADVTKPIKPALKSAEvELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEiarLRLEKDTIKNQNLEKKYLKDF 1541
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKkaEEAKKADE---AKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1542 EIVKRKHEDLQKALKRNGETLAKTiacysgqlaALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSS 1621
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK---------AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1622 K-RDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIE 1700
Cdd:PTZ00121 1619 KiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1701 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAI--LNIQARCDARVQNLQAECRKHRLLLEEDNK 1778
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
410 420
....*....|....*....|....*
gi 1034613720 1779 MLVNELNHSKEKECQYEKEKAEREV 1803
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1412-1915 |
1.68e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1412 SEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTG 1491
Cdd:pfam01576 57 AEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1492 GNNSNQVSETDEKedLLHENRLMQDEIARL--RLEKDTIKNQNLEKkylkdfeiVKRKHE----DLQKALKRNGET---L 1562
Cdd:pfam01576 137 EEDILLLEDQNSK--LSKERKLLEERISEFtsNLAEEEEKAKSLSK--------LKNKHEamisDLEERLKKEEKGrqeL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1563 AKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQElafqgtvDKCRHLQEN 1642
Cdd:pfam01576 207 EKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELE-------AQISELQED 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1643 LNSHvlilSLQLSKAESKSRVLKTELhytgEALK---EKALVFEHVQSELKQKQSQMkdiekmyksgYNTMEKCIEKQER 1719
Cdd:pfam01576 280 LESE----RAARNKAEKQRRDLGEEL----EALKtelEDTLDTTAAQQELRSKREQE----------VTELKKALEEETR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1720 FCQLKKQNML---------LQQQLDDARNKADNQEKAilniqarcdarvqnlqaecrkhRLLLEEDNKMLVNELNHSKEK 1790
Cdd:pfam01576 342 SHEAQLQEMRqkhtqaleeLTEQLEQAKRNKANLEKA----------------------KQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1791 ECQYEKEKAEREVAVRQLQQK-------RDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQEIQDQLTA 1863
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARlseserqRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1034613720 1864 TIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKilQHSSLMLQVFES 1915
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER--QLSTLQAQLSDM 529
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1380-1701 |
1.90e-05 |
|
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: 50.07 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1380 KRLIKLKDNHCEQLRVKI---RKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKK----KRRNVEEV 1452
Cdd:TIGR02169 198 QQLERLRREREKAERYQAllkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrleeIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1453 HQKVREKlrITEEQYRIEADVtkpikpalksAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQn 1532
Cdd:TIGR02169 278 NKKIKDL--GEEEQLRVKEKI----------GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1533 lekkyLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEK---QRESRQRLETEMQSYHCRLN 1609
Cdd:TIGR02169 345 -----IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkrEINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1610 AARCDHDQSHSSKRDQELAFQGTVD----KCRHLQENLNShvliLSLQLSKAESKSRVLKTELhytgealkekalvfEHV 1685
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEdkalEIKKQEWKLEQ----LAADLSKYEQELYDLKEEY--------------DRV 481
|
330
....*....|....*.
gi 1034613720 1686 QSELKQKQSQMKDIEK 1701
Cdd:TIGR02169 482 EKELSKLQRELAEAEA 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1396-1603 |
2.11e-05 |
|
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: 48.99 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1396 KIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQY-------- 1467
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelraele 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1468 RIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHE-NRLMQDEIARLRLEKDTIKNQNlekkylKDFEIVKR 1546
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALR------AELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613720 1547 KHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1603
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1391-1818 |
4.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1391 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIE 1470
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1471 ADVTKpIKPALKSAEVELKTGGNNSNQVSETDEKEDLLhenrlmQDEIARLrlekdtiknqnleKKYLKDFEIVKRKHED 1550
Cdd:PRK03918 314 KRLSR-LEEEINGIEERIKELEEKEERLEELKKKLKEL------EKRLEEL-------------EERHELYEEAKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1551 LQKALKR-NGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhcrlnaarcdhdqshsskrdqelaf 1629
Cdd:PRK03918 374 LERLKKRlTGLTPEKLEK----ELEELEKAKEEIEEEISKITARIGELKKEIKE-------------------------- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1630 qgtvdkcrhLQENLNshvlilslQLSKAESKSRVLKTEL--HYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSgy 1707
Cdd:PRK03918 424 ---------LKKAIE--------ELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1708 ntMEKCIEKQERFCQLKKqnmlLQQQLDDARNKAD--NQEKailniqarcdarvqnLQAECRKHRLLLEEDNKML--VNE 1783
Cdd:PRK03918 485 --LEKVLKKESELIKLKE----LAEQLKELEEKLKkyNLEE---------------LEKKAEEYEKLKEKLIKLKgeIKS 543
|
410 420 430
....*....|....*....|....*....|....*
gi 1034613720 1784 LNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNK 1818
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1382-1905 |
4.97e-05 |
|
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: 48.48 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1382 LIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVRE-KL 1460
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQlKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1461 RITEEQYRIEA------DVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLhENRLMQDEIARLRLEKDtiKNQNLE 1534
Cdd:TIGR04523 233 NIEKKQQEINEktteisNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-EKQLNQLKSEISDLNNQ--KEQDWN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1535 KKYLKDFEIVKRKHEDLQKALKRNGET---LAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNaa 1611
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1612 rcdhdQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLqLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQ 1691
Cdd:TIGR04523 388 -----NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL-LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1692 KQSQMKDIEKMYKSGYNTMEKCIEKQerfcqlkkqnmllQQQLDDarnkaDNQEKAILNIQARcdarvqnlqaecrkhrl 1771
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQK-------------QKELKS-----KEKELKKLNEEKK----------------- 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1772 LLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQ---KRDDVLNKGSATKAL------LDASSRHCTYLENGMQD 1842
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnKDDFELKKENLEKEIdeknkeIEELKQTQKSLKKKQEE 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034613720 1843 SRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQH 1905
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1283-1811 |
5.91e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1283 KMKDVqtSTPAEQDLEMASEGEQKRLEEYENNQPQVKNQIHSRDDLDDI-------IQSSQTVSEDgdsLCCNCKNVILL 1355
Cdd:pfam05483 255 KMKDL--TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrsMSTQKALEED---LQIATKTICQL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1356 IDQHEMKCKD-----CVHLL---KIKNTFCLWKRLIKLK----DNHCEQLRVKIRKLKNKASVLQkrisEKEEIKSQLKH 1423
Cdd:pfam05483 330 TEEKEAQMEElnkakAAHSFvvtEFEATTCSLEELLRTEqqrlEKNEDQLKIITMELQKKSSELE----EMTKFKNNKEV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1424 EILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYR------IEADVTKPIKPALKSAEVELKTGGNNS-- 1495
Cdd:pfam05483 406 ELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKeihdleIQLTAIKTSEEHYLKEVEDLKTELEKEkl 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1496 NQVSETDEKEDLLHENRLMQDEIARLRLEkdtiknqnlekkylkdfeiVKRKHEDLQKALKRNGETLAktiacysgQLAA 1575
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDMTLE-------------------LKKHQEDIINCKKQEERMLK--------QIEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1576 LTDENTTLRSKLEKQRESRQRLETEMQsyhCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLnshvlilslqls 1655
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVK---CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI------------ 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1656 kaESKSRVLKtELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLlqQQLD 1735
Cdd:pfam05483 604 --ENKNKNIE-ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL--EEVE 678
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613720 1736 DARNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQK 1811
Cdd:pfam05483 679 KAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAE 754
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
67-154 |
7.39e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.77 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 67 TALHLACATGQPEMVHLLVSR------RCELNLCDREDRTPLIKAVQLR--------QEACATLLLQNGANPNITDFFGR 132
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSFYHGESPlnaaaclgSPSIVALLSEDPADILTADSLGN 209
|
90 100 110
....*....|....*....|....*....|.
gi 1034613720 133 TALHYAVYNED---------TSMIEKLLSHG 154
Cdd:TIGR00870 210 TLLHLLVMENEfkaeyeelsCQMYNFALSLL 240
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
98-229 |
8.12e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.29 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 98 DRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKV 177
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034613720 178 KMVEFLLKKKANVNAIDYLGRSALIHAVTLGEK-DIVILLLQH--NIDVLSRDAF 229
Cdd:PHA02875 82 KAVEELLDLGKFADDVFYKDGMTPLHLATILKKlDIMKLLIARgaDPDIPNTDKF 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1391-1603 |
9.07e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1391 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIE 1470
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1471 ADVTKpikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIVKRKHED 1550
Cdd:COG1196 364 EEALL----EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034613720 1551 LQKALKRNGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1603
Cdd:COG1196 440 EEEALEEAAEEEAELEE----EEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
83-138 |
1.50e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 1.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613720 83 LLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYA 138
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1378-1659 |
1.61e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1378 LWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVR 1457
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1458 EKLR-ITEEQYRIEADVTkpikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKK 1536
Cdd:COG1196 309 ERRReLEERLEELEEELA-----ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1537 YLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHD 1616
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034613720 1617 QSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES 1659
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
114-220 |
1.68e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 46.54 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 114 ATLLLQNGA-----NPNITDFF-GRTALHYAVYNEDTSMIEKLLSHGTNI------------EECSKCEY--QPLLFAVS 173
Cdd:cd22192 66 AAVVLMEAApelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYgeHPLSFAAC 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034613720 174 RRKVKMVEFLLKKKANVNAIDYLGRSALiHavtlgekdivILLLQHN 220
Cdd:cd22192 146 VGNEEIVRLLIEHGADIRAQDSLGNTVL-H----------ILVLQPN 181
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
131-159 |
1.98e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 1.98e-04
10 20
....*....|....*....|....*....
gi 1034613720 131 GRTALHYAVYNEDTSMIEKLLSHGTNIEE 159
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
728-946 |
2.20e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.58 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 728 DEEDSVSNIATEIKDGEKSGTVSS---QKQPALKATTDEKDSV-----SNIATEIKDGEKSGTVSSQKPPALTATSDEEG 799
Cdd:PTZ00108 1144 QEEVEEKEIAKEQRLKSKTKGKASklrKPKLKKKEKKKKKSSAdkskkASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGS 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 800 SVLSIARENKDGEKS------RTVSSRKKPALKATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEEDSVLGIA 873
Cdd:PTZ00108 1224 DQEDDEEQKTKPKKSsvkrlkSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 874 RENKDGEKSRTVSSEKppGLKASSAEKDSVLNIARGKKD-----GEKTKRVSSRKKPSLEATS--DEKDSFSNITREKKD 946
Cdd:PTZ00108 1304 SPTKKKVKKRLEGSLA--ALKKKKKSEKKTARKKKSKTRvkqasASQSSRLLRRPRKKKSDSSseDDDDSEVDDSEDEDD 1381
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
51-107 |
2.25e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 2.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613720 51 LLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 107
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
117-171 |
2.47e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 2.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613720 117 LLQNG-ANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFA 171
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1420-1750 |
2.68e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1420 QLKHEILELEKELCSLRFAIQQEKKKRRNvEEVHQKVREKLRITEEQYRIEAdvtkpikpALKSAEVELKTggnnsnqvs 1499
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELE-AELEELEAELEELEAELAELEA--------ELEELRLELEE--------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1500 ETDEKEDLLHENRLMQDEIArlRLEKDTIKNQNLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgQLAALTDE 1579
Cdd:COG1196 279 LELELEEAQAEEYELLAELA--RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1580 NTTLRSKLEKQRESRQRLETEMQsyhcrlnaarcDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES 1659
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELA-----------EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1660 KSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKsgyntmekciEKQERFCQLKKQNMLLQQQLDDARN 1739
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA----------ELLEEAALLEAALAELLEELAEAAA 491
|
330
....*....|.
gi 1034613720 1740 KADNQEKAILN 1750
Cdd:COG1196 492 RLLLLLEAEAD 502
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
139-222 |
2.72e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 45.72 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 139 VYNEDTSMIEKLLSHGTNIEECSKCE-YQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLL 217
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKGNCINISVDEtTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
....*
gi 1034613720 218 QHNID 222
Cdd:PHA02874 89 DNGVD 93
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1386-1872 |
3.88e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1386 KDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITE 1464
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIcQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1465 EqyrieadvtkpikpalKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEkkylkdfeiV 1544
Cdd:pfam05483 332 E----------------KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---------L 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1545 KRKHEDLQK--ALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRL-------ETEMQSYHCRLNAARCdh 1615
Cdd:pfam05483 387 QKKSSELEEmtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarEKEIHDLEIQLTAIKT-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1616 DQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYtgealkekalvfEHVQSELKQKQSQ 1695
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ------------EDIINCKKQEERM 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1696 MKDIEkmyksgyNTMEKCIEKQERFCQLKKQnmlLQQQLDDARNKADNQEKAILNIQARCdarvqnlqaecrkhrLLLEE 1775
Cdd:pfam05483 533 LKQIE-------NLEEKEMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEV---------------LKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1776 DNKMLVNELNHSKekecqyeKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQ 1855
Cdd:pfam05483 588 QMKILENKCNNLK-------KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ 660
|
490
....*....|....*...
gi 1034613720 1856 -EIQDQLTATIRCTKEME 1872
Cdd:pfam05483 661 kEIEDKKISEEKLLEEVE 678
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1384-1775 |
4.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1384 KLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKvREKLRIT 1463
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK-ELLEEYT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1464 EEQYRIEADVtKPIKPALKSAEVELKtggnnsnQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYlKDFEI 1543
Cdd:PRK03918 459 AELKRIEKEL-KEIEEKERKLRKELR-------ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA-EEYEK 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1544 VKRKHEDLQKALKRNGETLAKtiacysgqLAALTDENTTLRSKLEKQRESRQRLETEMQSY--------HCRLNAARCDH 1615
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEK--------LEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPFY 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1616 DQSHSSKrDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES-KSRVLKTELHYTGEALKEKALVFEHVQSELKQKQS 1694
Cdd:PRK03918 602 NEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEElRKELEELEKKYSEEEYEELREEYLELSRELAGLRA 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1695 QMKDIEKMYKsgynTMEKCIEKQERfcQLKKqnmllqqqLDDARNKADNQEKAIlniqarcdARVQNLQAECRKHRLLLE 1774
Cdd:PRK03918 681 ELEELEKRRE----EIKKTLEKLKE--ELEE--------REKAKKELEKLEKAL--------ERVEELREKVKKYKALLK 738
|
.
gi 1034613720 1775 E 1775
Cdd:PRK03918 739 E 739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1391-1901 |
4.61e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1391 EQLRVKIRKLKNKASVLQKRISEK----EEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQ 1466
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAkkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1467 YRIEADVTKpiKPALKSAEVELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIV 1544
Cdd:PTZ00121 1398 KKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1545 KRKHEDLQKA--LKRNGETLAKTiacysgqlaalTDEnttLRSKLEKQRESRQRLETEmqsyhcrlNAARCDHDQSHSSK 1622
Cdd:PTZ00121 1476 KKKAEEAKKAdeAKKKAEEAKKK-----------ADE---AKKAAEAKKKADEAKKAE--------EAKKADEAKKAEEA 1533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1623 RdqelafqgTVDKCRHLQENLNSHVLILSLQLSKAESKSRVlktELHYTGEALKEKAL--VFEHVQSELKQKQSQMKDIE 1700
Cdd:PTZ00121 1534 K--------KADEAKKAEEKKKADELKKAEELKKAEEKKKA---EEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYE 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1701 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAilnIQARCDARVQNLQAECRKHRlllEEDNKML 1780
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA---EELKKAEEENKIKAAEEAKK---AEEDKKK 1676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1781 VNELNHSKEKECQYE---KEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSqfQEI 1857
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAealKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK--DEE 1754
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1034613720 1858 QDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEK 1901
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
36-187 |
5.58e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 45.00 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 36 IHRAVLHGNLEKLKYLLltyyDANKRDRKE---------RTALHLACATGQPEMVHLLVSRRCELN------LCDREDRT 100
Cdd:cd22192 55 LHVAALYDNLEAAVVLM----EAAPELVNEpmtsdlyqgETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 101 --------PLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTS----MIEKLLSHGTNIEECS------K 162
Cdd:cd22192 131 nliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLILSYDKEDDLQPldlvpnN 210
|
170 180
....*....|....*....|....*
gi 1034613720 163 CEYQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:cd22192 211 QGLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
90-229 |
6.29e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 44.62 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 90 ELNLCD--REDRTPLIKAVQLRQ-EACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNI--EECSKCE 164
Cdd:cd22192 7 ELHLLQqkRISESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 165 YQ---PLLFAVSRRKVKMVEFLLKKKANVN--------------AIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRD 227
Cdd:cd22192 87 YQgetALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
|
..
gi 1034613720 228 AF 229
Cdd:cd22192 167 SL 168
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1398-1913 |
8.87e-04 |
|
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: 44.44 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1398 RKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQE--------KKKRRNVEEVHQKVREKLRITEEQYRI 1469
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsaadaavAKDRSELEALEDQHGAFLDADIETAAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1470 EADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLmQDEIARLRLEKDTIKN-------------QNLEKK 1536
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN-NRDIAGIKDKLAKIREardrqlavaeddlQALESE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1537 YLKDFEIVKRKHEDLQKALKRNGETLAKTI--ACYSG----QLAALTDENTTLRSKLEKQRESRQRLETEmqsyhcrLNA 1610
Cdd:pfam12128 424 LREQLEAGKLEFNEEEYRLKSRLGELKLRLnqATATPelllQLENFDERIERAREEQEAANAEVERLQSE-------LRQ 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1611 ARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLN--SHVLILSLQLSKA---ESKSRVLKTELhytgeaLKEKALVFEHV 1685
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELELQLFpqAGTLLHFLRKEAPdweQSIGKVISPEL------LHRTDLDPEVW 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1686 QSELKQKQSQMK---DIEKMYKSGYNTMEKciekqerfcQLKKQNMLLQQQLDDARNKADNQEKAILNIqarcDARVQNL 1762
Cdd:pfam12128 571 DGSVGGELNLYGvklDLKRIDVPEWAASEE---------ELRERLDKAEEALQSAREKQAAAEEQLVQA----NGELEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1763 QAECRKHRLLLE---EDNKMLVNELNHSKEK-ECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKA-----LLDASSRHC 1833
Cdd:pfam12128 638 SREETFARTALKnarLDLRRLFDEKQSEKDKkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEKQ 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1834 TYLENGMQDSRKKLDQMRSQFQEIQDQLTATIR-CTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQHSSLMLQV 1912
Cdd:pfam12128 718 AYWQVVEGALDAQLALLKAAIAARRSGAKAELKaLETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY 797
|
.
gi 1034613720 1913 F 1913
Cdd:pfam12128 798 F 798
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
168-254 |
9.12e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 44.47 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 168 LLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFD 247
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
|
....*..
gi 1034613720 248 LIYEYER 254
Cdd:PLN03192 609 ILYHFAS 615
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
64-187 |
1.67e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.33 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 64 KERTALHLACATGQPEMVHLLVSRRCELNL--CDREDRT-----------PLIKAVQLRQEACATLLLQNGANP---NIT 127
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVSAraTGRFFRKspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPaalEAQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613720 128 DFFGRTALHYAVYNED---------TSMIEKLLSHGTNIEECSKCE-------YQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:cd21882 152 DSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQLEeipnhqgLTPLKLAAVEGKIVMFQHILQRE 227
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
66-96 |
1.74e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.65 E-value: 1.74e-03
10 20 30
....*....|....*....|....*....|..
gi 1034613720 66 RTALHLACA-TGQPEMVHLLVSRRCELNLCDR 96
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
66-93 |
2.28e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 2.28e-03
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1391-1628 |
2.32e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1391 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITEEQYRI 1469
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1470 EADVtKPIKPALKSAEVELKTGG--------NNSNQVSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKKYLKDF 1541
Cdd:PRK02224 432 EATL-RTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEE---LEAELEDLEEEVEEVEERLERAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1542 EIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhCRLNAARCDHDQSHSS 1621
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE--AREEVAELNSKLAELK 585
|
....*..
gi 1034613720 1622 KRDQELA 1628
Cdd:PRK02224 586 ERIESLE 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1683-1901 |
2.80e-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: 42.75 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1683 EHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARnKADNQEKAILNiqarcdARVQNL 1762
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-ENVKSELKELE------ARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1763 QAECRKHRLLLEEdnkmLVNELNHSKEKECQYEKEKAEREVA-----VRQLQQKrddvLNKGSATKALLDASSRHctyLE 1837
Cdd:TIGR02169 771 EEDLHKLEEALND----LEARLSHSRIPEIQAELSKLEEEVSriearLREIEQK----LNRLTLEKEYLEKEIQE---LQ 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613720 1838 NGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKiikkqddQIERLEK 1901
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK-------ERDELEA 896
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1379-1908 |
3.28e-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: 42.31 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1379 WKRLIKLKDNHCEQLRVKIRKLKN-------KASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEE 1451
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNelknkekELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1452 VHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTggNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQ 1531
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDK--FLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1532 NLEKKYlkdfEIVKRKHEDLQKALK-RNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNA 1610
Cdd:TIGR04523 182 KLNIQK----NIDKIKNKLLKLELLlSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1611 ARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLN---SHVLILSLQ------------LSKAESKSRVLKTELHYTGEAL 1675
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeqdwnkelkseLKNQEKKLEEIQNQISQNNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1676 KEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQErfcQLKKQNMLLQQQLDDARNKADNQEKailnIQARC 1755
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ---SYKQEIKNLESQINDLESKIQNQEK----LNQQK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1756 DARVQNLQAEcrkhRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTY 1835
Cdd:TIGR04523 411 DEQIKKLQQE----KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034613720 1836 LENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQHSSL 1908
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
131-162 |
3.76e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 3.76e-03
10 20 30
....*....|....*....|....*....|...
gi 1034613720 131 GRTALHYAVYNE-DTSMIEKLLSHGTNIEECSK 162
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1380-1609 |
3.79e-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: 42.36 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1380 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcsLRFAIQQEKKKRRNVEEVHQKVREK 1459
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1460 LRiteeqyrieadvtkpikpalksaEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRlekDTIKNQNLEKkylk 1539
Cdd:TIGR02169 814 LR-----------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE---KEIENLNGKK---- 863
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1540 dfEIVKRKHEDLQKALKRngetlaktiacYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLN 1609
Cdd:TIGR02169 864 --EELEEELEELEAALRD-----------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1623-1897 |
3.82e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1623 RDQELAFQgtVDKCRHLQEnlnshvlilsLQLSKAESKSRVlKTELhytgEALKEKALVFEHVQSELKQKQSQMKDIEKM 1702
Cdd:pfam17380 366 RQEEIAME--ISRMRELER----------LQMERQQKNERV-RQEL----EAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1703 YKSGYN-TMEKCIEKQER-FCQLKKQNMLLQQQLDDARNKADNQEKAILNiqarcdarvqnLQAECRKHRLLLEEDNKML 1780
Cdd:pfam17380 429 QEEARQrEVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLE-----------LEKEKRDRKRAEEQRRKIL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1781 VNELNHSKEKECQ-------YEKEKAEREVAVRQLQQKRDdvlnkgsatkalldassrhctylengMQDSRKKLDQMRSQ 1853
Cdd:pfam17380 498 EKELEERKQAMIEeerkrklLEKEMEERQKAIYEEERRRE--------------------------AEEERRKQQEMEER 551
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034613720 1854 fQEIQDQltatIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIE 1897
Cdd:pfam17380 552 -RRIQEQ----MRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1391-1863 |
4.88e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1391 EQLRVKIRKLKNKASVLQKRISEKEEIK--SQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKlriTEEQYR 1468
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL---QEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1469 IEADVTKPIKPALKSAevelktggnnsnqvseTDEKEDLLHENRLMQDEIARLRLEKDTIKNQnleKKYLKDFEIVKRKH 1548
Cdd:COG4717 182 LLEQLSLATEEELQDL----------------AEELEELQQRLAELEEELEEAQEELEELEEE---LEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1549 EDLQKA------------LKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRlnaarcdhd 1616
Cdd:COG4717 243 ERLKEArlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL--------- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1617 qshssKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLktelhytgEALKEKALVfEHVQSELKQ--KQS 1694
Cdd:COG4717 314 -----EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA--------EELEEELQL-EELEQEIAAllAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1695 QMKDIEKMYksgyntmeKCIEKQERFCQLKKQNMLLQQQLDDARNkaDNQEKAILNIQARCDARVQNLQAEcrkhRLLLE 1774
Cdd:COG4717 380 GVEDEEELR--------AALEQAEEYQELKEELEELEEQLEELLG--ELEELLEALDEEELEEELEELEEE----LEELE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1775 EDnkmlVNELnHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNK-------GSATKALLDASSRHCTYLEngmqdsRKKL 1847
Cdd:COG4717 446 EE----LEEL-REELAELEAELEQLEEDGELAELLQELEELKAElrelaeeWAALKLALELLEEAREEYR------EERL 514
|
490
....*....|....*.
gi 1034613720 1848 DQMRSQFQEIQDQLTA 1863
Cdd:COG4717 515 PPVLERASEYFSRLTD 530
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1391-1905 |
4.94e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1391 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLK--HEILELEKELCSLRFAIQQEKKKRRNVEevHQKvreklRITEEQYR 1468
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAriEELRAQEAVLEETQERINRARKAAPLAA--HIK-----AVTQIEQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1469 IEADVTKpIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARL----RLEKDTIKNQNLEKKYLKDFEIV 1544
Cdd:TIGR00618 309 AQRIHTE-LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAhevaTSIREISCQQHTLTQHIHTLQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1545 KRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDH-DQSHSSKR 1623
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQS 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1624 DQELAFQGTVDKCRHLQENlNSHVLILSLQLSKAESKSRVLKTELHYTGEAlkEKALVFEHVQSELKQKQSQMKDIEKmy 1703
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQET-RKKAVVLARLLELQEEPCPLCGSCIHPNPAR--QDIDNPGPLTRRMQRGEQTYAQLET-- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1704 kSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDdARNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNE 1783
Cdd:TIGR00618 543 -SEEDVYHQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1784 LNHSKEK------ECQYEKEKAEREVAVRQLQQK--RDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQ 1855
Cdd:TIGR00618 621 LQPEQDLqdvrlhLQQCSQELALKLTALHALQLTltQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1034613720 1856 EIQDQLtatiRC--TKEMEGDTQKLEVEHVMMRKI--IKKQDDQIERLEKILQH 1905
Cdd:TIGR00618 701 QCQTLL----REleTHIEEYDREFNEIENASSSLGsdLAAREDALNQSLKELMH 750
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
884-1173 |
7.65e-03 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 41.31 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 884 TVSSEKPPGLKASSAEKDSVlniarGKKDGEKTKRVSSRKKPSLEATSDEKDSFSNITREKKD-----GEISRKVSSQKP 958
Cdd:PRK08581 30 PQKDSTAKTTSHDSKKSNDD-----ETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDsnniiDFIYKNLPQTNI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 959 PALKGTSDEEDSV-LGIARENKDGEKSRTVSSEKPpgLKATSDEKDSVLNIARGKKDGEKTRTVSSQKPPTLKATSDEED 1037
Cdd:PRK08581 105 NQLLTKNKYDDNYsLTTLIQNLFNLNSDISDYEQP--RNSEKSTNDSNKNSDSSIKNDTDTQSSKQDKADNQKAPSSNNT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1038 SVLSIARENKDGEKSRTVSSEKPSGLKATSAEKDSvlniargkkygekTKRVSSRKKPALKATSDE------KDSVLYIA 1111
Cdd:PRK08581 183 KPSTSNKQPNSPKPTQPNQSNSQPASDDTANQKSS-------------SKDNQSMSDSALDSILDQysedakKTQKDYAS 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034613720 1112 REKKDGEKSRTVSSPKQPALKAICDKEDSVPNMATEKKDEQISGTVSCQKQPALKATSDKKD 1173
Cdd:PRK08581 250 QSKKDKTETSNTKNPQLPTQDELKHKSKPAQSFENDVNQSNTRSTSLFETGPSLSNNDDSGS 311
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
876-1840 |
7.71e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 876 NKDGEKSRTVSSEKPPGLKASSAEKDSVLNIARGKKDGEKTKRVSSRKKP-SLEATSDEKDSFSNITR-EKKDGEISRKV 953
Cdd:PTZ00121 1038 NDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNrADEATEEAFGKAEEAKKtETGKAEEARKA 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 954 SSQKPPALKGTSDEEdsvLGIARENKDGEKSRTVSSEKPPGLKATSDEKDSVlNIARGKKDGEKT----RTVSSQKPPTL 1029
Cdd:PTZ00121 1118 EEAKKKAEDARKAEE---ARKAEDARKAEEARKAEDAKRVEIARKAEDARKA-EEARKAEDAKKAeaarKAEEVRKAEEL 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1030 KATSD----------EEDSVLSIARENKDGEKSRTVSSEKPSGLKATSAEK-DSVLNIARGKKYGEKTKRVSSRKKPALK 1098
Cdd:PTZ00121 1194 RKAEDarkaeaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKaEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1099 ATSDEKDSVLYIAREKKDGEKSRTvSSPKQPALKAICDKEDSVPNMATEKKDEQISGTVSCQKQPALKATsdKKDSVSNI 1178
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK--KAAEAAKA 1350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1179 PTEIKDGQQSGTVSSQKQPAWKATSVKK--DSVSNIATEIKDG-QIRGTVSPQKQSAQKV----IFKKKVSLLNIAT--- 1248
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKkaDAAKKKAEEKKKAdEAKKKAEEDKKKADELkkaaAAKKKADEAKKKAeek 1430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1249 RITGGWKSGTEYPENLPTLKATIENKNSVLNTATKMKDVQTSTPAEQDLEMASEGEQ--KRLEEYENNQPQVKNQIHSRD 1326
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakKKAEEAKKKADEAKKAAEAKK 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1327 DLDDIIQSSQTVSEDGDSLCCNCKNVILLIDQHEMKCKDCVHLLKikntfclwkrliklkdnhceqlrvKIRKLKNKASV 1406
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE------------------------ELKKAEEKKKA 1566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1407 LQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVhqKVREKLRITEEQYRIEADVTKPIKPALKSAEV 1486
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA--KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1487 ELKtggnNSNQVSETDEkedllhENRLMQDEIARlRLEKDTIKNQNL---EKKYLKDFEIVKRKHEDLQKA--LKRNGET 1561
Cdd:PTZ00121 1645 EKK----KAEELKKAEE------ENKIKAAEEAK-KAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEAKKAeeLKKKEAE 1713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1562 LAKTiacySGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAArcdhdqSHSSKRDQELAFQGTVDKCRHLQE 1641
Cdd:PTZ00121 1714 EKKK----AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI------AHLKKEEEKKAEEIRKEKEAVIEE 1783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1642 NLNSHVLILSLQLSKaesKSRVLKTELHYTGEALKEKALVFEhvqselKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFC 1721
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDK---KIKDIFDNFANIIEGGKEGNLVIN------DSKEMEDSAIKEVADSKNMQLEEADAFEKHKF 1854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1722 QLKKQNMLLQQQLDDARNKADNQEKAILNIQarcdarvqnlqaECRKHRLLLEEDNKMLVNELNHS-KEKECQYEKEKAE 1800
Cdd:PTZ00121 1855 NKNNENGEDGNKEADFNKEKDLKEDDEEEIE------------EADEIEKIDKDDIEREIPNNNMAgKNNDIIDDKLDKD 1922
|
970 980 990 1000
....*....|....*....|....*....|....*....|
gi 1034613720 1801 rEVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGM 1840
Cdd:PTZ00121 1923 -EYIKRDAEETREEIIKISKKDMCINDFSSKFCDYMKDNI 1961
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1398-1877 |
7.79e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1398 RKLKNKASVLQKRISEKEEIKSQLKHEIL-ELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQyRIEADVtkp 1476
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELET--- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1477 ikpaLKSAEVELKTggnnsnQVSET-DEKEDLLHENRLMQDEIARLRLEKDTIknqnLEKKYLKDFEI--VKRKHEDLQK 1553
Cdd:PRK02224 256 ----LEAEIEDLRE------TIAETeREREELAEEVRDLRERLEELEEERDDL----LAEAGLDDADAeaVEARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1554 ---ALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQ 1630
Cdd:PRK02224 322 rdeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1631 GTVDKcrhlQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFE---------------HVQS-------- 1687
Cdd:PRK02224 402 DAPVD----LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegspHVETieedrerv 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1688 -ELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAIlniqARCDARVQNLQAEC 1766
Cdd:PRK02224 478 eELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA----EELRERAAELEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1767 RKHRLLLE------EDNKMLVNELNhSKEKECQYEKEKAER-----------EVAVRQLQQKRDDVLNKGSATKALLDAS 1829
Cdd:PRK02224 554 EEKREAAAeaeeeaEEAREEVAELN-SKLAELKERIESLERirtllaaiadaEDEIERLREKREALAELNDERRERLAEK 632
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034613720 1830 SRHCTYLENGMQDSR-KKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQK 1877
Cdd:PRK02224 633 RERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1380-1827 |
7.85e-03 |
|
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.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1380 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKElcslrfaiQQEKKKRRNVEEVHQKVREK 1459
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE--------YLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1460 LRiTEEQYRIEADVTKPIKPALKSAEVELKTggNNSNQVSETDEKEDLLHENRLMQDEIARLRLEkdtiKNQNLEKKYLK 1539
Cdd:pfam02463 245 LL-RDEQEEIESSKQEIEKEEEKLAQVLKEN--KEEEKEKKLQEEELKLLAKEEEELKSELLKLE----RRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1540 DFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETemqsyhcrlnaarcdhdqsh 1619
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA-------------------- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1620 ssKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDI 1699
Cdd:pfam02463 378 --KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613720 1700 EKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQ-EKAILNIQARCDARVQNLQAECRKHRLLLEEDNK 1778
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1034613720 1779 MLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKALLD 1827
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLI 584
|
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